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Volumn 36, Issue 1, 2003, Pages 1-69

Helicase mechanisms and the coupling of helicases within macromolecular machines Part II: Integration of helicases into cellular processes

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN; HELICASE; NUCLEIC ACID; PROTEIN; RNA;

EID: 0037294467     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0033583502003864     Document Type: Review
Times cited : (132)

References (289)
  • 1
    • 0017668829 scopus 로고
    • DNA unwinding enzyme II of Escherichia coli. 1. Purification and characterization of the ATPase activity
    • ABDEL-MONEM, M., CHANAL, M. C. & HOFFMANN-BERLING, H. (1977). DNA unwinding enzyme II of Escherichia coli. 1. Purification and characterization of the ATPase activity. Eur. J. Biochem. 79, 33-38.
    • (1977) Eur. J. Biochem. , vol.79 , pp. 33-38
    • Abdel-Monem, M.1    Chanal, M.C.2    Hoffmann-Berling, H.3
  • 2
    • 0028869149 scopus 로고
    • Relaxing and unwinding on Holliday: DNA helicase-mediated branch migration
    • ADAMS, D. E. & WEST, S. C. (1995). Relaxing and unwinding on Holliday: DNA helicase-mediated branch migration. Mutation Res. 337, 149-159.
    • (1995) Mutation Res. , vol.337 , pp. 149-159
    • Adams, D.E.1    West, S.C.2
  • 3
    • 0034739530 scopus 로고    scopus 로고
    • A physical interaction of UvrD with nucleotide excision repair protein UvrB
    • AHN, B. (2000). A physical interaction of UvrD with nucleotide excision repair protein UvrB. Molecules and Cells 10, 592-597.
    • (2000) Molecules and Cells , vol.10 , pp. 592-597
    • Ahn, B.1
  • 4
    • 0029829895 scopus 로고    scopus 로고
    • RNA polymerase signals UvrAB landing sites
    • AHN, B. & GROSSMAN, L. (1996). RNA polymerase signals UvrAB landing sites. J. biol. Chem. 271, 21453-21461.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21453-21461
    • Ahn, B.1    Grossman, L.2
  • 5
    • 0034600838 scopus 로고    scopus 로고
    • A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein
    • AHNERT, P., PICHA, K. M. & PATEL, S. S. (2000). A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein. EMBO J. 19, 3418-3427.
    • (2000) EMBO J. , vol.19 , pp. 3418-3427
    • Ahnert, P.1    Picha, K.M.2    Patel, S.S.3
  • 6
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • ALI, J. A. & LOHMAN, T. M. (1997). Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275, 377-380.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 7
    • 0033527761 scopus 로고    scopus 로고
    • An oligomeric form of E. coli UvrD is required for optimal helicase activity
    • ALI, J. A., MALUF, N. K. & LOHMAN, T. M. (1999). An oligomeric form of E. coli UvrD is required for optimal helicase activity. J. molec. Biol 293, 815-834.
    • (1999) J. Molec. Biol. , vol.293 , pp. 815-834
    • Ali, J.A.1    Maluf, N.K.2    Lohman, T.M.3
  • 9
    • 0035989351 scopus 로고    scopus 로고
    • A domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme
    • AMUNDSEN, S. K., TAYLOR, A. F. & SMITH, G. R. (2002). A Domain of RecC Required for Assembly of the Regulatory RecD Subunit Into the Escherichia coli RecBCD Holoenzyme. Genetics 161, 483-492.
    • (2002) Genetics , vol.161 , pp. 483-492
    • Amundsen, S.K.1    Taylor, A.F.2    Smith, G.R.3
  • 10
    • 0033937402 scopus 로고    scopus 로고
    • Functional specificity of the replication fork-arrest complexes of Bacillus subtilis and Escherichia coli: Significant specificity for Tus-Ter functioning in E. coli
    • ANDERSEN, P. A., GRIFFITHS, A. A., DUGGIN, I. G. & WAKE, R. G. (2000). Functional specificity of the replication fork-arrest complexes of Bacillus subtilis and Escherichia coli: significant specificity for Tus-Ter functioning in E. coli. Molec. Microbiol. 36, 1327-1335.
    • (2000) Molec. Microbiol. , vol.36 , pp. 1327-1335
    • Andersen, P.A.1    Griffiths, A.A.2    Duggin, I.G.3    Wake, R.G.4
  • 11
    • 0019826123 scopus 로고
    • Rep protein as a helicase in an active, isolatable replication fork of duplex phi X174 DNA
    • ARAI, N. & KORNBERG, A. (1981). Rep protein as a helicase in an active, isolatable replication fork of duplex phi X174 DNA. J. biol. Chem. 256, 5294-5298.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5294-5298
    • Arai, N.1    Kornberg, A.2
  • 12
    • 0040241960 scopus 로고    scopus 로고
    • Protein complexes in nucleotide excision repair
    • ARAUJO, S. J. & WOOD, R. D. (1999). Protein complexes in nucleotide excision repair. Mutation Res. 435, 23-33.
    • (1999) Mutation Res. , vol.435 , pp. 23-33
    • Araujo, S.J.1    Wood, R.D.2
  • 13
    • 0027306799 scopus 로고
    • Genetics of eukaryotic RNA polymerases I, II, and III
    • ARCHAMBAULT, J. & FRIESEN, J. D. (1993). Genetics of eukaryotic RNA polymerases I, II, and III. Microbiol. Rev. 57, 703-724.
    • (1993) Microbiol. Rev. , vol.57 , pp. 703-724
    • Archambault, J.1    Friesen, J.D.2
  • 15
  • 16
    • 0034647421 scopus 로고    scopus 로고
    • A novel, 11 nucleotide variant of chi, chi*: One of a class of sequences defining the Escherichia coli recombination hotspot chi
    • ARNOLD, D. A., HANDA, N., KOBAYASHI, I. & KOWALCZY-KOWSSA, S. C. (2000). A novel, 11 nucleotide variant of chi, chi*: one of a class of sequences defining the Escherichia coli recombination hotspot chi. J. molec. Biol. 300, 469-479.
    • (2000) J. Molec. Biol. , vol.300 , pp. 469-479
    • Arnold, D.A.1    Handa, N.2    Kobayashi, I.3    Kowalczy-Kowssa, S.C.4
  • 17
    • 0022611929 scopus 로고
    • Structure of the uvrB gene of Escherichia coli. Homology with other DNA repair enzymes and characterization of the uvrB5 mutation
    • BACKENDORF, C., SPAINK, H., BARBEIRO, A. P. & VAN DE PUTTE, P. (1986). Structure of the uvrB gene of Escherichia coli. Homology with other DNA repair enzymes and characterization of the uvrB5 mutation. Nucleic Acids Res. 14, 2877-2890.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 2877-2890
    • Backendorf, C.1    Spaink, H.2    Barbeiro, A.P.3    Van de Putte, P.4
  • 18
    • 0035943341 scopus 로고    scopus 로고
    • Isolation and characterization of sigma(70)-retaining transcription elongation complexes from Escherichia coli
    • BAR-NAHUM, G. & NUDLER, E. (2001). Isolation and characterization of sigma(70)-retaining transcription elongation complexes from Escherichia coli. Cell 106, 443-451.
    • (2001) Cell , vol.106 , pp. 443-451
    • Bar-Nahum, G.1    Nudler, E.2
  • 19
    • 0035868712 scopus 로고    scopus 로고
    • The DnaB, DnaC complex: A structure based on dimers assembled around an occluded channel
    • BARCENA, M., RUIZ, T., DONATE, L. E., BROWN, S. E., DIXON, N. E., RADERMACHER, M. & CARAZO, J. M. (2001). The DnaB. DnaC complex: a structure based on dimers assembled around an occluded channel. EMBO J. 20, 1462-1468.
    • (2001) EMBO J. , vol.20 , pp. 1462-1468
    • Barcena, M.1    Ruiz, T.2    Donate, L.E.3    Brown, S.E.4    Dixon, N.E.5    Radermacher, M.6    Carazo, J.M.7
  • 20
    • 0028586099 scopus 로고
    • Purification and characterization of bacteriophage T4 gene 59 protein. A DNA helicase assembly protein involved in DNA replication
    • BARRY, J. & ALBERTS, B. (1994). Purification and characterization of bacteriophage T4 gene 59 protein. A DNA helicase assembly protein involved in DNA replication. J. biol. Chem. 269, 33049-33062.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33049-33062
    • Barry, J.1    Alberts, B.2
  • 21
    • 0002844816 scopus 로고    scopus 로고
    • Mechanism for completing DNA replication
    • Cold Spring Harbor Laboratory Press
    • BASTIA, D. & MOHANTY, B. K. (1996). Mechanism for completing DNA replication. In DNA Replication in Eukaryotic Cells, pp. 177-215. Cold Spring Harbor Laboratory Press.
    • (1996) DNA Replication in Eukaryotic Cells , pp. 177-215
    • Bastia, D.1    Mohanty, B.K.2
  • 23
    • 0030915446 scopus 로고    scopus 로고
    • Kinetic analysis of pairing and strand exchange catalyzed by RecA. Detection by fluorescence energy transfer
    • BAZEMORE, L. R., TAKAHASHI, M. & RADDING, C. M. (1997b). Kinetic analysis of pairing and strand exchange catalyzed by RecA. Detection by fluorescence energy transfer. J. biol. Chem. 272, 14672-14682.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14672-14682
    • Bazemore, L.R.1    Takahashi, M.2    Radding, C.M.3
  • 24
    • 0023898207 scopus 로고
    • Interactions of Escherichia coli transcription termination factor rho with RNA. II. Electron microscopy and nudease protection experiments
    • BEAR, D. G., HICKS, P. S., ESCUDERO, K. W., ANDREWS, C. L., MCSWIGGEN, J. A. & VON HIPPEL, P. H. (1988). Interactions of Escherichia coli transcription termination factor rho with RNA. II. Electron microscopy and nudease protection experiments. J. molec. Biol. 199, 623-635.
    • (1988) J. Molec. Biol. , vol.199 , pp. 623-635
    • Bear, D.G.1    Hicks, P.S.2    Escudero, K.W.3    Andrews, C.L.4    Mcswiggen, J.A.5    Von Hippel, P.H.6
  • 25
    • 0033214860 scopus 로고    scopus 로고
    • RMPs: Recombination/replication mediator proteins
    • BEERNINK, H. T. & MORRICAL, S. W. (1999). RMPs: recombination/replication mediator proteins. Trends biochem. Sci. 24, 385-389.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 385-389
    • Beernink, H.T.1    Morrical, S.W.2
  • 26
    • 0026296795 scopus 로고
    • Identification of the different intermediates in the interaction of (A)BC excinudease with its substrates by DNaseI footprinting on two uniquely modified oligonucleotides
    • BERTRAND-BURGGRAF, E., SELBY, C., HEARST, J. E. & SANCAR, A. (1991). Identification of the different intermediates in the interaction of (A)BC excinudease with its substrates by DNaseI footprinting on two uniquely modified oligonucleotides. J. molec. Biol. 219, 27-36.
    • (1991) J. Molec. Biol. , vol.219 , pp. 27-36
    • Bertrand-Burggraf, E.1    Selby, C.2    Hearst, J.E.3    Sancar, A.4
  • 27
    • 0032468201 scopus 로고    scopus 로고
    • A model for parallel triple helix formation by RecA: Single-single association with a homologous duplex via the minor groove
    • BERTUCAT, G., LAVERY, R. & PREVOST, C. (1998). A model for parallel triple helix formation by RecA: single-single association with a homologous duplex via the minor groove. J. biomolec. Struct. Dynam. 16, 535-546.
    • (1998) J. Biomolec. Struct. Dynam. , vol.16 , pp. 535-546
    • Bertucat, G.1    Lavery, R.2    Prevost, C.3
  • 28
    • 0032865485 scopus 로고    scopus 로고
    • A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices
    • BERTUCAT, G., LAVERY, R. & PREVOST, C. (1999). A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices. Biophys. J. 77, 1562-1576.
    • (1999) Biophys. J. , vol.77 , pp. 1562-1576
    • Bertucat, G.1    Lavery, R.2    Prevost, C.3
  • 30
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • BIANCO, P. R. & KOWALCZYKOWSKI, S. C. (2000). Translocation step size and mechanism of the RecBC DNA helicase. Nature 405, 368-372.
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 31
    • 0035902508 scopus 로고    scopus 로고
    • Mediator proteins orchestrate enzyme-ssDNA assembly during T4 recombination-dependent DNA replication and repair
    • BLEUIT, J. S., XU, H., MA, Y., WANG, T., LIU, J. & MORRICAL, S. W. (2001). Mediator proteins orchestrate enzyme-ssDNA assembly during T4 recombination-dependent DNA replication and repair. Proc. natn. Acad. Sci. USA 98, 8298-8305.
    • (2001) Proc. Natn. Acad. Sci. USA , vol.98 , pp. 8298-8305
    • Bleuit, J.S.1    Xu, H.2    Ma, Y.3    Wang, T.4    Liu, J.5    Morrical, S.W.6
  • 32
    • 0033120903 scopus 로고    scopus 로고
    • The structural basis for terminator recognition by the Rho transcription termination factor
    • BOGDEN, C. E., FASS, D., BERGMAN, N., NICHOLS, M. D. & BERGER, J. M. (1999). The structural basis for terminator recognition by the Rho transcription termination factor. Molec. Cell 3, 487-493.
    • (1999) Molec. Cell , vol.3 , pp. 487-493
    • Bogden, C.E.1    Fass, D.2    Bergman, N.3    Nichols, M.D.4    Berger, J.M.5
  • 33
    • 0035816649 scopus 로고    scopus 로고
    • Dna repair excision nuclease attacks undamaged DNA. A potential source of spontaneous mutations
    • BRANUM, M. E., REARDON, J. T. & SANCAR, A. (2001). Dna repair excision nuclease attacks undamaged DNA. A potential source of spontaneous mutations. J. biol. Chem. 276, 25421-25426.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25421-25426
    • Branum, M.E.1    Reardon, J.T.2    Sancar, A.3
  • 34
    • 0031921626 scopus 로고    scopus 로고
    • The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions
    • BRIERCHECK, D. M., WOOD, T. C., ALLISON, T. J., RICHARDSON, J. P. & RULE, G. S. (1998). The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions. Nature struct. Biol. 5, 393-399.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 393-399
    • Briercheck, D.M.1    Wood, T.C.2    Allison, T.J.3    Richardson, J.P.4    Rule, G.S.5
  • 35
    • 0029620994 scopus 로고
    • Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction
    • BROSH, JR., R. M. & MATSON, S. W. (1995). Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction. J. Bacteriol. 177, 5612-5621.
    • (1995) J. Bacteriol. , vol.177 , pp. 5612-5621
    • Brosh R.M., Jr.1    Matson, S.W.2
  • 36
    • 10144248959 scopus 로고    scopus 로고
    • A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III
    • BROSH, JR., R. M. & MATSON, S. W. (1996). A partially functional DNA helicase II mutant defective in forming stable binary complexes with ATP and DNA. A role for helicase motif III. J. biol. Chem. 271, 25360-25368.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25360-25368
    • Brosh R.M., Jr.1    Matson, S.W.2
  • 37
    • 15444357274 scopus 로고    scopus 로고
    • A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo
    • BROSH, JR., R. M. & MATSON, S. W. (1997). A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo. J. biol. Chem. 272, 572-579.
    • (1997) J. Biol. Chem. , vol.272 , pp. 572-579
    • Brosh R.M., Jr.1    Matson, S.W.2
  • 38
    • 0033958431 scopus 로고    scopus 로고
    • UvrD-dependent replication of rolling-circle plasmids in Escherichia coli
    • BRUAND, C. & EHRLICH, S. D. (2000). UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Molec. Microbiol. 35, 204-210.
    • (2000) Molec. Microbiol. , vol.35 , pp. 204-210
    • Bruand, C.1    Ehrlich, S.D.2
  • 39
    • 0033593474 scopus 로고    scopus 로고
    • The kinetics of sigma subunit directed promoter recognition by E. coli RNA polymerase
    • BUCKLE, M., PEMBERTON, I. K., JACQUET, M. A. & BUC, H. (1999). The kinetics of sigma subunit directed promoter recognition by E. coli RNA polymerase. J. molec. Biol. 285, 955-964.
    • (1999) J. Molec. Biol. , vol.285 , pp. 955-964
    • Buckle, M.1    Pemberton, I.K.2    Jacquet, M.A.3    Buc, H.4
  • 40
    • 0029072199 scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer
    • BUJALOWSKI, W. & JEZEWSKA, M. J. (1995). Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer. Biochemistry 34, 8513-8519.
    • (1995) Biochemistry , vol.34 , pp. 8513-8519
    • Bujalowski, W.1    Jezewska, M.J.2
  • 41
    • 0034723155 scopus 로고    scopus 로고
    • Kinetic mechanism of the single-stranded DNA recognition by Escherichia coli replicative helicase DnaB protein. Application of the matrix projection operator technique to analyze stopped-flow kinetics
    • BUJALOWSKI, W. & JEZEWSKA, M. J. (2000). Kinetic mechanism of the single-stranded DNA recognition by Escherichia coli replicative helicase DnaB protein. Application of the matrix projection operator technique to analyze stopped-flow kinetics. J. molec. Biol. 295, 831-852.
    • (2000) J. Molec. Biol. , vol.295 , pp. 831-852
    • Bujalowski, W.1    Jezewska, M.J.2
  • 42
    • 0001468848 scopus 로고    scopus 로고
    • Splicing of precursors to mRNAs by the spliceosomes
    • eds. R. F. Gesteland, T. R. Cech & J. F. Atkins. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • BURGE, C. B., TUSCHL, T. & SHARP, P. A. (1999). Splicing of precursors to mRNAs by the spliceosomes. In The RNA World, 2nd edn (eds. R. F. Gesteland, T. R. Cech & J. F. Atkins), pp. 525-560. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • (1999) The RNA World, 2nd Edn. , pp. 525-560
    • Burge, C.B.1    Tuschl, T.2    Sharp, P.A.3
  • 43
    • 0014663102 scopus 로고
    • Factor stimulating transcription by RNA polymerase
    • BURGESS, R. R., TRAVERS, A. A., DUNN, J. J. & BAUTZ, E. K. (1969). Factor stimulating transcription by RNA polymerase. Nature 221, 43-46.
    • (1969) Nature , vol.221 , pp. 43-46
    • Burgess, R.R.1    Travers, A.A.2    Dunn, J.J.3    Bautz, E.K.4
  • 44
    • 0033032373 scopus 로고    scopus 로고
    • Termination of DNA replication of bacterial and plasmid chromosomes
    • BUSSIERE, D. E. & BASTIA, D. (1999). Termination of DNA replication of bacterial and plasmid chromosomes. Molec. Microbiol. 31, 1611-1618.
    • (1999) Molec. Microbiol. , vol.31 , pp. 1611-1618
    • Bussiere, D.E.1    Bastia, D.2
  • 45
    • 0028918469 scopus 로고
    • Crystal structure of the replication terminator protein from B. subtilis at 2·6 Å
    • BUSSIERE, D. E., BASTIA, D. & WHITE, S. W. (1995). Crystal structure of the replication terminator protein from B. subtilis at 2·6 Å. Cell 80, 651-660.
    • (1995) Cell , vol.80 , pp. 651-660
    • Bussiere, D.E.1    Bastia, D.2    White, S.W.3
  • 46
    • 0033083036 scopus 로고    scopus 로고
    • Core RNA polymerase from E. coli induces a major change in the domain arrangement of the sigma 70 subunit
    • CALLACI, S., HEYDUK, E. & HEYDUK, T. (1999). Core RNA polymerase from E. coli induces a major change in the domain arrangement of the sigma 70 subunit. Molec. Cell 3, 229-238.
    • (1999) Molec. Cell , vol.3 , pp. 229-238
    • Callaci, S.1    Heyduk, E.2    Heyduk, T.3
  • 48
    • 0023776040 scopus 로고
    • Involvement of a crytic ATPase activity on UvrB and its proteolysis product UvrB* in DNA repair
    • CARON, P. R. & GROSSMAN, L. (1988). Involvement of a crytic ATPase activity on UvrB and its proteolysis product UvrB* in DNA repair. Nucleic Acids Res. 16, 9651-9662.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9651-9662
    • Caron, P.R.1    Grossman, L.2
  • 49
    • 1842379671 scopus 로고
    • Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the UvrABC protein complex
    • CARON, P. R., KUSHNER, S. & GROSSMAN, L. (1985). Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the UvrABC protein complex. Proc. natn. Acad. Sci. USA 82, 4925-4929.
    • (1985) Proc. Natn. Acad. Sci. USA , vol.82 , pp. 4925-4929
    • Caron, P.R.1    Kushner, S.2    Grossman, L.3
  • 50
    • 0032916509 scopus 로고    scopus 로고
    • mRNA degradation. A tale of poly(A) and multiprotein machines
    • CARPOUSIS, A. J., VANZO, N. F. & RAYNAL, L. C. (1999). mRNA degradation. A tale of poly(A) and multiprotein machines. Trends Genet. 15, 24-28.
    • (1999) Trends Genet. , vol.15 , pp. 24-28
    • Carpousis, A.J.1    Vanzo, N.F.2    Raynal, L.C.3
  • 51
    • 0033966457 scopus 로고    scopus 로고
    • The terminase enzyme from bacteriophage lambda: A DNA-packaging machine
    • CATALANO, C. E. (2000). The terminase enzyme from bacteriophage lambda: a DNA-packaging machine. Cell. molec. Life Sci. 57, 128-148.
    • (2000) Cell. Molec. Life Sci. , vol.57 , pp. 128-148
    • Catalano, C.E.1
  • 52
    • 0025051903 scopus 로고
    • Effects of the bacteriophage T4 gene 41 and gene 32 proteins on RNA primer synthesis: Coupling of leading- and lagging-strand DNA synthesis at a replication fork
    • CHA, T. A. & ALBERTS, B. M. (1990). Effects of the bacteriophage T4 gene 41 and gene 32 proteins on RNA primer synthesis: coupling of leading- and lagging-strand DNA synthesis at a replication fork. Biochemistry 29, 1791-1798.
    • (1990) Biochemistry , vol.29 , pp. 1791-1798
    • Cha, T.A.1    Alberts, B.M.2
  • 53
    • 0025022318 scopus 로고
    • DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteins
    • CHAO, K. & LOHMAN, T. M. (1990). DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteins. J. biol. Chem. 265, 1067-1076.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1067-1076
    • Chao, K.1    Lohman, T.M.2
  • 54
    • 0035105921 scopus 로고    scopus 로고
    • Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor
    • CHEN, J. Y., STANDS, L., STALEY, J. P., JACKUPS, JR., R. R., LATUS, L. J. & CHANG, T. H. (2001). Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor. Molec. Cell 7, 227-232.
    • (2001) Molec. Cell , vol.7 , pp. 227-232
    • Chen, J.Y.1    Stands, L.2    Staley, J.P.3    Jackups R.R., Jr.4    Latus, L.J.5    Chang, T.H.6
  • 55
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • CHENG, W., HSIEH, J., BRENDZA, K. M. & LOHMAN, T. M. (2001). E. coli Rep oligomers are required to initiate DNA unwinding in vitro. J. molec. Biol. 310, 327-350.
    • (2001) J. Molec. Biol. , vol.310 , pp. 327-350
    • Cheng, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 56
    • 0033792637 scopus 로고    scopus 로고
    • The question remains: Is the spliceosome a ribozyme?
    • COLLINS, C. A. & GUTHRIE, C. (2000). The question remains: is the spliceosome a ribozyme? Nature struct. Biol. 7, 850-854.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 850-854
    • Collins, C.A.1    Guthrie, C.2
  • 57
    • 0030704679 scopus 로고    scopus 로고
    • Sequence-specific interactions in the Tus-Ter complex and the effect of base pair substitutions on arrest of DNA replication in Escherichia coli
    • COSKUN-ARI, F. F. & HILL, T. M. (1997). Sequence-specific interactions in the Tus-Ter complex and the effect of base pair substitutions on arrest of DNA replication in Escherichia coli. J. biol. Chem. 272, 26448-26456.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26448-26456
    • Coskun-Ari, F.F.1    Hill, T.M.2
  • 58
    • 0030890705 scopus 로고    scopus 로고
    • reeF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli
    • COURCELLE, J., CARSWELL-CRUMPTON, C. & HANAWALT, P. C. (1997). reeF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli. Proc. natn. Acad. Sci. USA 94, 3714-3719.
    • (1997) Proc. Natn. Acad. Sci. USA , vol.94 , pp. 3714-3719
    • Courcelle, J.1    Carswell-Crumpton, C.2    Hanawalt, P.C.3
  • 59
    • 0032740855 scopus 로고    scopus 로고
    • RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli
    • COURCELLE, J. & HANAWALT, P. C. (1999). RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli. Molec. gen. Genet. 262, 543-551.
    • (1999) Molec. Gen. Genet. , vol.262 , pp. 543-551
    • Courcelle, J.1    Hanawalt, P.C.2
  • 60
    • 0028290444 scopus 로고
    • Why does RecA protein hydrolyse ATP?
    • COX, M. M. (1994). Why does RecA protein hydrolyse ATP? Trends biochem. Sci. 19, 217-222.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 217-222
    • Cox, M.M.1
  • 61
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 Å resolution
    • CRAMER, P., BUSHNELL, D. A. & KORNBERG, R. D. (2001). Structural basis of transcription: RNA polymerase II at 2.8 Å resolution. Science 292, 1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 62
  • 63
    • 0036295581 scopus 로고    scopus 로고
    • The Isomerization of the UvrB-DNA preincision complex couples the UvrB and UvrC activities
    • DELAGOUTTE, E., FUCHS, R. P. & BERTRAND-BURGGRAF, E. (2002). The Isomerization of the UvrB-DNA preincision complex couples the UvrB and UvrC activities. J. molec. Biol. 320, 73-84.
    • (2002) J. Molec. Biol. , vol.320 , pp. 73-84
    • Delagoutte, E.1    Fuchs, R.P.2    Bertrand-Burggraf, E.3
  • 64
    • 0031557405 scopus 로고    scopus 로고
    • Sequence-dependent modulation of nucleotide excision repair: The efficiency of the incision reaction is inversely correlated with the stability of the pre-incision UvrB-DNA complex
    • DELAGOUTTE, E., BERTRAND-BURGGRAF, E., DUNAND, J. & FUCHS, R. P. (1997). Sequence-dependent modulation of nucleotide excision repair: the efficiency of the incision reaction is inversely correlated with the stability of the pre-incision UvrB-DNA complex. J. molec. Biol. 266, 703-710.
    • (1997) J. Molec. Biol. , vol.266 , pp. 703-710
    • Delagoutte, E.1    Bertrand-Burggraf, E.2    Dunand, J.3    Fuchs, R.P.4
  • 65
    • 0035836479 scopus 로고    scopus 로고
    • Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork
    • DELAGOUTTE, E. & VON HIPPEL, P. H. (2001). Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork. Biochemistry 40, 4459-4477.
    • (2001) Biochemistry , vol.40 , pp. 4459-4477
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 66
    • 0036880196 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I. Structures and properties of isolated helicases
    • DELAGOUTTE, E. & VON HIPPEL, P. H. (2002). Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I. Structures and properties of isolated helicases. Q. Rev. Biophys. 35, 431-478.
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 431-478
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 67
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRML domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • DING, J., HAYASHI, M. K., ZHANG, Y., MANCHE, L., KRAINER, A. R. & XU, R. M. (1999). Crystal structure of the two-RRML domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev. 13, 1102-1115.
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 68
    • 0035905807 scopus 로고    scopus 로고
    • Chi-sequence recognition and DNA translocation by single RecBCD helicase/nudease molecules
    • DOHONEY, K. M. & GELLES, J. (2001). Chi-sequence recognition and DNA translocation by single RecBCD helicase/nudease molecules. Nature 409, 370-374.
    • (2001) Nature , vol.409 , pp. 370-374
    • Dohoney, K.M.1    Gelles, J.2
  • 70
    • 0029741204 scopus 로고    scopus 로고
    • The ATP-activated hexameric helicase of bacteriophage T4 (gp41) forms a stable primosome with a single subunit of T4-coded primase (gp61)
    • DONG, F. & VON HIPPEL, P. H. (1996). The ATP-activated hexameric helicase of bacteriophage T4 (gp41) forms a stable primosome with a single subunit of T4-coded primase (gp61). J. biol. Chem. 271, 1925-1931.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1925-1931
    • Dong, F.1    Von Hippel, P.H.2
  • 71
    • 0033548584 scopus 로고    scopus 로고
    • Site-directed mutants of RTP of Bacillus subtilis and the mechanism of replication fork arrest
    • DUGGIN, I. G., ANDERSEN, P. A., SMITH, M. T., WILCE, J. A., KING, G. F. & WAKE, R. G. (1999). Site-directed mutants of RTP of Bacillus subtilis and the mechanism of replication fork arrest. J. molec. Biol. 286, 1325-1335.
    • (1999) J. Molec. Biol. , vol.286 , pp. 1325-1335
    • Duggin, I.G.1    Andersen, P.A.2    Smith, M.T.3    Wilce, J.A.4    King, G.F.5    Wake, R.G.6
  • 72
    • 0018352189 scopus 로고
    • The rep protein of Escherichia coli: Interaction with DNA and other proteins
    • DUGUET, M., YARRANTON, G. & GEFTER, M. (1979). The rep protein of Escherichia coli: interaction with DNA and other proteins. Cold Spring Harbor Symp. Quant. Biol. 43, 335-343.
    • (1979) Cold Spring Harbor Symp. Quant. Biol. , vol.43 , pp. 335-343
    • Duguet, M.1    Yarranton, G.2    Gefter, M.3
  • 73
    • 0032450639 scopus 로고    scopus 로고
    • RNA polymerase-DNA interaction: Structures of intermediate, open, and elongation complexes
    • EBRIGHT, R. H. (1998). RNA polymerase-DNA interaction: structures of intermediate, open, and elongation complexes. Cold Spring Harbor Symp. Quant. Biol. 63, 11-20.
    • (1998) Cold Spring Harbor Symp. Quant. Biol. , vol.63 , pp. 11-20
    • Ebright, R.H.1
  • 74
    • 0019185071 scopus 로고
    • The role of gene A protein and E. coli rep protein in the replication of phi X 174 replicative form DNA
    • EISENBERG, S. (1980). The role of gene A protein and E. coli rep protein in the replication of phi X 174 replicative form DNA. Phil. Trans. R. Soc. Lond. (Series B: Biol. Sci.) 210, 337-349.
    • (1980) Phil. Trans. R. Soc. Lond. (Series B: Biol. Sci.) , vol.210 , pp. 337-349
    • Eisenberg, S.1
  • 75
    • 0033610911 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 helicase-primase. Analysis of helicase activity
    • FALKENBERG, M., ELIAS, P. & LEHMAN, I. R. (1998). The herpes simplex virus type 1 helicase-primase. Analysis of helicase activity. J. biol. Chem. 273, 32154-32157.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32154-32157
    • Falkenberg, M.1    Elias, P.2    Lehman, I.R.3
  • 76
    • 0033152872 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the DnaB hexameric helicase
    • FASS, D., BOGDEN, C. E. & BERGER, J. M. (1999). Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Struct. Folding Design 7, 691-698.
    • (1999) Struct. Folding Design , vol.7 , pp. 691-698
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 77
    • 0034161515 scopus 로고    scopus 로고
    • Escherichia coli promoter opening and -10 recognition: Mutational analysis of sigma70
    • FENTON, M. S., LEE, S. J. & GRALLA, J. D. (2000). Escherichia coli promoter opening and -10 recognition: mutational analysis of sigma70. EMBO J. 19, 1130-1137.
    • (2000) EMBO J. , vol.19 , pp. 1130-1137
    • Fenton, M.S.1    Lee, S.J.2    Gralla, J.D.3
  • 79
    • 0034711089 scopus 로고    scopus 로고
    • Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein
    • GALLETTO, R., RAJENDRAN, S. & BUJALOWSKI, W. (2000). Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein. Biochemistry 39, 12959-12969.
    • (2000) Biochemistry , vol.39 , pp. 12959-12969
    • Galletto, R.1    Rajendran, S.2    Bujalowski, W.3
  • 80
    • 0024355282 scopus 로고
    • A mutant Escherichia coli sigma 70 subunit of RNA polymerase with altered promoter specificity
    • GARDELLA, T., MOYLE, H. & SUSSKIND, M. M. (1989). A mutant Escherichia coli sigma 70 subunit of RNA polymerase with altered promoter specificity. J. molec. Biol. 206, 579-590.
    • (1989) J. Molec. Biol. , vol.206 , pp. 579-590
    • Gardella, T.1    Moyle, H.2    Susskind, M.M.3
  • 81
    • 0035968270 scopus 로고    scopus 로고
    • A single domain of the replication termination protein of Bacillus subtilis is involved in arresting both DnaB helicase and RNA polymerase
    • GAUTAM, A., MULUGU, S., ALEXANDER, K. & BASTIA, D. (2001). A single domain of the replication termination protein of Bacillus subtilis is involved in arresting both DnaB helicase and RNA polymerase. J. biol. Chem. 276, 23471-23479.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23471-23479
    • Gautam, A.1    Mulugu, S.2    Alexander, K.3    Bastia, D.4
  • 82
    • 0033980541 scopus 로고    scopus 로고
    • RuvAB-mediated branch migration does not involve extensive DNA opening within the RuvB hexamer
    • GEORGE, H., KURAOKA, I., NAUMAN, D. A., KOBERTZ, W. R., WOOD, R. D. & WEST, S. C. (2000). RuvAB-mediated branch migration does not involve extensive DNA opening within the RuvB hexamer. Curr. Biol. 10, 103-106.
    • (2000) Curr. Biol. , vol.10 , pp. 103-106
    • George, H.1    Kuraoka, I.2    Nauman, D.A.3    Kobertz, W.R.4    Wood, R.D.5    West, S.C.6
  • 83
    • 0028047403 scopus 로고
    • A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization
    • GEORGE, J. W., BROSH, JR., R. M. & MATSON, S. W. (1994). A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization. J. molec. Biol. 235, 424-435.
    • (1994) J. Molec. Biol. , vol.235 , pp. 424-435
    • George, J.W.1    Brosh R.M., Jr.2    Matson, S.W.3
  • 84
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
    • GNATT, A. L., CRAMER, P., FU, J., BUSHNELL, D. A. & KORNBERG, R. D. (2001). Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution. Science 292, 1876-1882.
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 85
    • 0026091055 scopus 로고
    • Structure and assembly of the Escherichia coli transcription termination factor rho and its interaction with RNA. I. Cryoelectron microscopic studies
    • GOGOL, E. P., SEIFRIED, S. E. & VON HIPPEL, P. H. (1991). Structure and assembly of the Escherichia coli transcription termination factor rho and its interaction with RNA. I. Cryoelectron microscopic studies. J. molec. Biol. 221, 1127-1138.
    • (1991) J. Molec. Biol. , vol.221 , pp. 1127-1138
    • Gogol, E.P.1    Seifried, S.E.2    Von Hippel, P.H.3
  • 86
    • 0031039924 scopus 로고    scopus 로고
    • The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage
    • GORDIENKO, I. & RUPP, W. D. (1997a). The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage. EMBO J. 16, 889-895.
    • (1997) EMBO J. , vol.16 , pp. 889-895
    • Gordienko, I.1    Rupp, W.D.2
  • 87
    • 0031046737 scopus 로고    scopus 로고
    • UvrAB activity at a damaged DNA site: Is unpaired DNA present?
    • GORDIENKO, I. & RUPP, W. D. (1997b). UvrAB activity at a damaged DNA site: is unpaired DNA present? EMBO J. 16, 880-888.
    • (1997) EMBO J. , vol.16 , pp. 880-888
    • Gordienko, I.1    Rupp, W.D.2
  • 88
    • 0344765478 scopus 로고    scopus 로고
    • A specific 3′ exonuclease activity of UvrABC
    • GORDIENKO, I. & RUPP, W. D. (1998). A specific 3′ exonuclease activity of UvrABC. EMBO J. 17, 626-633.
    • (1998) EMBO J. , vol.17 , pp. 626-633
    • Gordienko, I.1    Rupp, W.D.2
  • 89
    • 0035971070 scopus 로고    scopus 로고
    • Equilibrium binding of single-stranded DNA to the secondary DNA binding site of the bacterial recombinase RecA
    • GOURVES, A. S., DEFAIS, M. & JOHNSON, N. P. (2001). Equilibrium binding of single-stranded DNA to the secondary DNA binding site of the bacterial recombinase RecA. J. biol. Chem. 276, 9613-9619.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9613-9619
    • Gourves, A.S.1    Defais, M.2    Johnson, N.P.3
  • 93
    • 0032213250 scopus 로고    scopus 로고
    • A simple polypyrimidine repeat acts as an artificial Rho-dependent terminator in vivo and in vitro
    • GUERIN, M., ROBICHON, N., GEISELMANN, J. & RAHMOUNI, A. R. (1998). A simple polypyrimidine repeat acts as an artificial Rho-dependent terminator in vivo and in vitro. Nucleic Acids Res. 26, 4895-4900.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4895-4900
    • Guerin, M.1    Robichon, N.2    Geiselmann, J.3    Rahmouni, A.R.4
  • 94
    • 0033120034 scopus 로고    scopus 로고
    • The mechanism of intrinsic transcription termination
    • GUSAROV, I. & NUDLER, E. (1999). The mechanism of intrinsic transcription termination. Molec. Cell 3, 495-504.
    • (1999) Molec. Cell , vol.3 , pp. 495-504
    • Gusarov, I.1    Nudler, E.2
  • 96
    • 0033031935 scopus 로고    scopus 로고
    • RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: A conserved mechanism for control of DNA recombination
    • HARMON, F. G., DIGATE, R. J. & KOWALCZYKOWSKI, S. C. (1999). RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination. Molec. Cell 3, 611-620.
    • (1999) Molec. Cell , vol.3 , pp. 611-620
    • Harmon, F.G.1    Digate, R.J.2    Kowalczykowski, S.C.3
  • 97
    • 0029165036 scopus 로고
    • Changes in conserved region 3 of Escherichia coli sigma 70 mediate ppGpp-dependent functions in vivo
    • HERNANDEZ, V. J. & CASHEL, M. (1995). Changes in conserved region 3 of Escherichia coli sigma 70 mediate ppGpp-dependent functions in vivo. J. molec. Biol. 252, 536-549.
    • (1995) J. Molec. Biol. , vol.252 , pp. 536-549
    • Hernandez, V.J.1    Cashel, M.2
  • 98
    • 0024293493 scopus 로고
    • DNA-dependent RNA polymerase of Escherichia coli induces bending or an increased flexibility of DNA by specific complex formation
    • HEUMANN, H., RICHETTI, M. & WEREL, W. (1988). DNA-dependent RNA polymerase of Escherichia coli induces bending or an increased flexibility of DNA by specific complex formation. EMBO J. 7, 4379-4381.
    • (1988) EMBO J. , vol.7 , pp. 4379-4381
    • Heumann, H.1    Richetti, M.2    Werel, W.3
  • 99
    • 0032478638 scopus 로고    scopus 로고
    • Introduction of a tryptophan reporter group into the ATP binding motif of the Escherichia coli UvrB protein for the study of nucleotide binding and conformational dynamics
    • HILDEBRAND, E. L. & GROSSMAN, L. (1998). Introduction of a tryptophan reporter group into the ATP binding motif of the Escherichia coli UvrB protein for the study of nucleotide binding and conformational dynamics. J. biol. Chem. 273, 7818-7827.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7818-7827
    • Hildebrand, E.L.1    Grossman, L.2
  • 100
    • 0032544708 scopus 로고    scopus 로고
    • ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme
    • HINGORANI, M. M. & O'DONNELL, M. (1998). ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J. biol. Chem. 273, 24550-24563.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.2
  • 101
  • 102
    • 84959678845 scopus 로고
    • A mechanism for gene conversion in fungi
    • HOLLIDAY, R. (1964). A mechanism for gene conversion in fungi. Genet. Res. 5, 282-304.
    • (1964) Genet. Res. , vol.5 , pp. 282-304
    • Holliday, R.1
  • 103
    • 0032565509 scopus 로고    scopus 로고
    • Endogenous lesions, S-phase-independent spontaneous mutations, and evolutionary strategies for base excision repair
    • HOLMQUIST, G. P. (1998). Endogenous lesions, S-phase-independent spontaneous mutations, and evolutionary strategies for base excision repair. Mutation Res. 400, 59-68.
    • (1998) Mutation Res. , vol.400 , pp. 59-68
    • Holmquist, G.P.1
  • 104
    • 0027944087 scopus 로고
    • Substrate spectrum of human excinuclease: Repair of abasic sites, methylated bases, mismatches, and bulky adducts
    • HUANG, J. C., HSU, D. S., KAZANTSEV, A. & SANCAR, A. (1994). Substrate spectrum of human excinuclease: repair of abasic sites, methylated bases, mismatches, and bulky adducts. Proc. natn. Acad. Sci. USA 91, 12213-12217.
    • (1994) Proc. Natn. Acad. Sci. USA , vol.91 , pp. 12213-12217
    • Huang, J.C.1    Hsu, D.S.2    Kazantsev, A.3    Sancar, A.4
  • 105
    • 0040581590 scopus 로고
    • Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease
    • HUSAIN, I., VAN HOUTEN, B., THOMAS, D. C., ABDEL-MONEM, M. & SANCAR, A. (1985). Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease. Proc. natn. Acad. Sci. USA 82, 6774-6778.
    • (1985) Proc. Natn. Acad. Sci. USA , vol.82 , pp. 6774-6778
    • Husain, I.1    Van Houten, B.2    Thomas, D.C.3    Abdel-Monem, M.4    Sancar, A.5
  • 106
    • 0034669196 scopus 로고    scopus 로고
    • The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome
    • INGLESTON, S. M., SHARPLES, G. J. & LLOYD, R. G. (2000). The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. EMBO J. 19, 6266-6274.
    • (2000) EMBO J. , vol.19 , pp. 6266-6274
    • Ingleston, S.M.1    Sharples, G.J.2    Lloyd, R.G.3
  • 107
    • 0035816713 scopus 로고    scopus 로고
    • Identification and mapping of protein-protein interactions between gp32 and gp59 by cross-linking
    • ISHMAEL, F. T., ALLEY, S. C. & BENKOVIC, S. J. (2001). Identification and mapping of protein-protein interactions between gp32 and gp59 by cross-linking. J. biol. Chem. 276, 25236-25242.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25236-25242
    • Ishmael, F.T.1    Alley, S.C.2    Benkovic, S.J.3
  • 108
    • 0037036347 scopus 로고    scopus 로고
    • Assembly of the bacteriophage T4 helicase. Architecture and stoichiometry of the gp41-gp59 complex
    • ISHMAEL, F. T., ALLEY, S. C. & BENKOVIC, S. J. (2002). Assembly of the bacteriophage T4 helicase. Architecture and stoichiometry of the gp41-gp59 complex. J. biol. Chem. 277, 20555-20562.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20555-20562
    • Ishmael, F.T.1    Alley, S.C.2    Benkovic, S.J.3
  • 109
    • 0032562822 scopus 로고    scopus 로고
    • Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies
    • JEZEWSKA, M. J., RAJENDRAN, S., BUJALOWSKA, D. & BUJALOWSKI, W. (1998a). Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies. J. biol. Chem. 273, 10515-10529.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 110
    • 0032478286 scopus 로고    scopus 로고
    • Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: Recognition and structure
    • JEZEWSKA, M. J., RAJENDRAN, S. & BUJALOWSKI, W. (1998b). Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: recognition and structure. Biochemistry 37, 3116-3136.
    • (1998) Biochemistry , vol.37 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 111
    • 0032502678 scopus 로고    scopus 로고
    • Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein
    • JEZEWSKA, M. J., RAJENDRAN, S. & BUJALOWSKI, W. (1998c). Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein. J. biol. Chem. 273, 9058-9069.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 112
    • 0026527507 scopus 로고
    • Termination efficiency at tho-dependent terminators depends on kinetic coupling between RNA polymerase and rho
    • JIN, D. J., BURGESS, R. R., RICHARDSON, J. P. & GROSS, C. A. (1992). Termination efficiency at tho-dependent terminators depends on kinetic coupling between RNA polymerase and rho. Proc. natn. Acad. Sci. USA 89, 1453-1457.
    • (1992) Proc. Natn. Acad. Sci. USA , vol.89 , pp. 1453-1457
    • Jin, D.J.1    Burgess, R.R.2    Richardson, J.P.3    Gross, C.A.4
  • 113
    • 0033578723 scopus 로고    scopus 로고
    • Interactions of bacteriophage T4-coded primase (gp61) with the T4 replication helicase (gp41) and DNA in primosome formation
    • JING, D. H., DONG, F., LATHAM, G. J. & VON HIPPEL, P. H. (1999). Interactions of bacteriophage T4-coded primase (gp61) with the T4 replication helicase (gp41) and DNA in primosome formation. J. biol. Chem. 274, 27287-27298.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27287-27298
    • Jing, D.H.1    Dong, F.2    Latham, G.J.3    Von Hippel, P.H.4
  • 114
    • 0024557468 scopus 로고
    • Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila
    • JOKERST, R. S., WEEKS, J. R., ZEHRING, W. A. & GREEN-LEAF, A. L. (1989). Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila. Molec. gen. Genet. 215, 266-275.
    • (1989) Molec. Gen. Genet. , vol.215 , pp. 266-275
    • Jokerst, R.S.1    Weeks, J.R.2    Zehring, W.A.3    Green-Leaf, A.L.4
  • 115
    • 0035902574 scopus 로고    scopus 로고
    • Bacteriophage T4 gene 41 helicase and gene 59 helicase-loading protein: A versatile couple with roles in replication and recombination
    • JONES, C. E., MUESER, T. C., DUDAS, K. C., KREUZER, K. N. & NOSSAL, N. G. (2001). Bacteriophage T4 gene 41 helicase and gene 59 helicase-loading protein: a versatile couple with roles in replication and recombination. Proc. natn. Acad. Sci. USA 98, 8312-8318.
    • (2001) Proc. Natn. Acad. Sci. USA , vol.98 , pp. 8312-8318
    • Jones, C.E.1    Mueser, T.C.2    Dudas, K.C.3    Kreuzer, K.N.4    Nossal, N.G.5
  • 116
    • 0034282426 scopus 로고    scopus 로고
    • Interaction of the bacteriophage T4 gene 59 helicase loading protein and gene 41 helicase with each other and with fork, flap, and cruciform DNA
    • JONES, C. E., MUESER, T. C. & NOSSAL, N. G. (2000). Interaction of the bacteriophage T4 gene 59 helicase loading protein and gene 41 helicase with each other and with fork, flap, and cruciform DNA. J. biol. Chem. 275, 27145-27154.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27145-27154
    • Jones, C.E.1    Mueser, T.C.2    Nossal, N.G.3
  • 117
    • 0029908981 scopus 로고    scopus 로고
    • Structure of a replication-terminator protein complexed with DNA
    • KAMADA, K., HORIUCHI, T., OHSUMI, K., SHIMAMOTO, N. & MORIKAWA, K. (1996). Structure of a replication-terminator protein complexed with DNA. Nature 383, 598-603.
    • (1996) Nature , vol.383 , pp. 598-603
    • Kamada, K.1    Horiuchi, T.2    Ohsumi, K.3    Shimamoto, N.4    Morikawa, K.5
  • 118
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A tau-DnaB interaction mediates rapid replication fork movement
    • KIM, S., DALLMANN, H. G., MCHENRY, C. S. & MARIANS, K. J. (1996). Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement. Cell 84, 643-650.
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    Mchenry, C.S.3    Marians, K.J.4
  • 119
    • 0035875669 scopus 로고    scopus 로고
    • DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids
    • KING, J. A., DUBIELZIG, R., GRIMM, D. & KLEINSCHMIDT, J. A. (2001). DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids. EMBO J. 20, 3282-3291.
    • (2001) EMBO J. , vol.20 , pp. 3282-3291
    • King, J.A.1    Dubielzig, R.2    Grimm, D.3    Kleinschmidt, J.A.4
  • 120
    • 0019198306 scopus 로고
    • Studies on the functions of DNA helicase I and DNA helicase II of Escherichia coli
    • KLINKERT, M. Q., KLEIN, A. & ABDEL-MONEM, M. (1980). Studies on the functions of DNA helicase I and DNA helicase II of Escherichia coli. J. biol. Chem. 255, 9746-9752.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9746-9752
    • Klinkert, M.Q.1    Klein, A.2    Abdel-Monem, M.3
  • 121
    • 0036863659 scopus 로고    scopus 로고
    • Shortening of RNA: DNA hybrid in elongation complex of RNA polymerase is a prerequisite for transcription termination
    • KOMISSAROVA, N., BECKER, J., SOLTER, S., KIREEVA, M. & KASHLEV, M. (2002). Shortening of RNA: DNA hybrid in elongation complex of RNA polymerase is a prerequisite for transcription termination. Molec. Cell. 10, 1151-1162.
    • (2002) Molec. Cell , vol.10 , pp. 1151-1162
    • Komissarova, N.1    Becker, J.2    Solter, S.3    Kireeva, M.4    Kashlev, M.5
  • 122
    • 0028100641 scopus 로고
    • Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
    • KORANGY, F. & JULIN, D. A. (1994). Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli. Biochemistry 33, 9552-9560.
    • (1994) Biochemistry , vol.33 , pp. 9552-9560
    • Korangy, F.1    Julin, D.A.2
  • 123
    • 0031911760 scopus 로고    scopus 로고
    • Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases
    • KOROLEV, S., YAO, N., LOHMAN, T. M., WEBER, P. C. & WAKSMAN, G. (1998). Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases. Protein Sci. 7, 605-610.
    • (1998) Protein Sci. , vol.7 , pp. 605-610
    • Korolev, S.1    Yao, N.2    Lohman, T.M.3    Weber, P.C.4    Waksman, G.5
  • 125
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • KOWALCZYKOWSKI, S. C. (2000). Initiation of genetic recombination and recombination-dependent replication. Trends biochem. Sci. 25, 156-165.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 126
    • 0028967415 scopus 로고
    • DNA-strand exchange promoted by RecA protein in the absence of ATP: Implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions
    • KOWALCZYKOWSKI, S. C. & KRUPP, R. A. (1995). DNA-strand exchange promoted by RecA protein in the absence of ATP: implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions. Proc. natn. Acad. Sci. USA 92, 3478-3482.
    • (1995) Proc. Natn. Acad. Sci. USA , vol.92 , pp. 3478-3482
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 127
    • 0034176951 scopus 로고    scopus 로고
    • Recombination-dependent DNA replication in phage T4
    • KREUZER, K. N. (2000). Recombination-dependent DNA replication in phage T4. Trends biochem. Sci. 25, 165-173.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 165-173
    • Kreuzer, K.N.1
  • 128
    • 0033047503 scopus 로고    scopus 로고
    • Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome
    • KUHN, A. N., LI, Z. & BROW, D. A. (1999). Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome. Molec. Cell 3, 65-75.
    • (1999) Molec. Cell , vol.3 , pp. 65-75
    • Kuhn, A.N.1    Li, Z.2    Brow, D.A.3
  • 129
    • 0037047049 scopus 로고    scopus 로고
    • Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation
    • KUHN, A. N., REICHI, E. M. & BROW, D. A. (2002). Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation. Proc. natn. Acad. Sci. USA 99, 9145-9149.
    • (2002) Proc. Natn. Acad. Sci. USA , vol.99 , pp. 9145-9149
    • Kuhn, A.N.1    Reichi, E.M.2    Brow, D.A.3
  • 130
    • 0022423227 scopus 로고
    • Stimulation of the UvrABC enzyme-catalyzed reactions by the UvrD protein (DNA helicase II)
    • KUMURA, K., SEKIGUCHI, M., STEINUM, A.-L. & SEEBERG, E. (1985). Stimulation of the UvrABC enzyme-catalyzed reactions by the UvrD protein (DNA helicase II). Nucleic Acids Res. 13, 1483-1492.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1483-1492
    • Kumura, K.1    Sekiguchi, M.2    Steinum, A.-L.3    Seeberg, E.4
  • 133
    • 0035368724 scopus 로고    scopus 로고
    • RNA polymerase damps down
    • LANDICK, R. (2001). RNA polymerase damps down. Cell 105, 567-570.
    • (2001) Cell , vol.105 , pp. 567-570
    • Landick, R.1
  • 134
    • 0031019643 scopus 로고    scopus 로고
    • Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA
    • LEARN, B. A., UM, S. J., HUANG, L. & MCMACKEN, R. (1997). Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA. Proc. natn. Acad. Sci. USA 94, 1154-1159.
    • (1997) Proc. Natn. Acad. Sci. USA , vol.94 , pp. 1154-1159
    • Learn, B.A.1    Um, S.J.2    Huang, L.3    Mcmacken, R.4
  • 135
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LEBOWITZ, J. H. & MCMACKEN, R. (1986). The Escherichia coli dnaB replication protein is a DNA helicase. J. biol. Chem. 261, 4738-4748.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    Mcmacken, R.2
  • 136
    • 0031587293 scopus 로고    scopus 로고
    • Interactions of the bacteriophage T4 gene 59 protein with single-stranded polynucleotides: Binding parameters and ion effects
    • LEFEBVRE, S. D. & MORRICAL, S. W. (1997). Interactions of the bacteriophage T4 gene 59 protein with single-stranded polynucleotides: binding parameters and ion effects. J. molec. Biol. 272, 312-326.
    • (1997) J. Molec. Biol. , vol.272 , pp. 312-326
    • Lefebvre, S.D.1    Morrical, S.W.2
  • 137
    • 0039251501 scopus 로고    scopus 로고
    • Simultaneous interactions of bacteriophage T4 DNA replication proteins gp59 and gp32 with single-stranded (ss) DNA. Co-modulation of ssDNA binding activities in a DNA helicase assembly intermediate
    • LEFEBVRE, S. D., WONG, M. L. & MORRICAL, S. W. (1999). Simultaneous interactions of bacteriophage T4 DNA replication proteins gp59 and gp32 with single-stranded (ss) DNA. Co-modulation of ssDNA binding activities in a DNA helicase assembly intermediate. J. biol. Chem. 274, 22830-22838.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22830-22838
    • Lefebvre, S.D.1    Wong, M.L.2    Morrical, S.W.3
  • 138
    • 0033636685 scopus 로고    scopus 로고
    • Structures of helical junctions in nucleic acids
    • LILLEY, D. M. (2000). Structures of helical junctions in nucleic acids. Q. Rev. Biophys. 33, 109-159.
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 109-159
    • Lilley, D.M.1
  • 139
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • LINDAHL, T. (1993). Instability and decay of the primary structure of DNA. Nature 362, 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 140
    • 0015504253 scopus 로고
    • Rate of chain breakage at apurinic sites in double-stranded deoxyribonucleic acid
    • LINDAHL, T. & ANDERSSON, A. (1972). Rate of chain breakage at apurinic sites in double-stranded deoxyribonucleic acid. Biochemistry 11, 3618-3623.
    • (1972) Biochemistry , vol.11 , pp. 3618-3623
    • Lindahl, T.1    Andersson, A.2
  • 141
    • 0015504248 scopus 로고
    • Rate of depurination of native deoxyribonucleic acid
    • LINDAHL, T. & NYBERG, B. (1972). Rate of depurination of native deoxyribonucleic acid. Biochemistry 11, 3610-3618.
    • (1972) Biochemistry , vol.11 , pp. 3610-3618
    • Lindahl, T.1    Nyberg, B.2
  • 142
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • LOHMAN, T. M. & BJORNSON, K. P. (1996). Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65, 169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 143
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • LORSCH, J. R. & HERSCHLAG, D. (1998a). The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry 37, 2180-2193.
    • (1998) Biochemistry , vol.37 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 144
    • 0032562221 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes
    • LORSCH, J. R. & HERSCHLAG, D. (1998b). The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes. Biochemistry 37, 2194-2206.
    • (1998) Biochemistry , vol.37 , pp. 2194-2206
    • Lorsch, J.R.1    Herschlag, D.2
  • 145
    • 0036447339 scopus 로고    scopus 로고
    • DNA unwinding step-size of E. coli RecBCD determined from single turnover quenched-flow kinetic studies
    • LUCIUS, A. L., VINDIGNI, A., GREGORIAN, R., ALI, J. A., TAYLOR, A. F., SMITH, G. R. & LOHMAN, T. M. (2002). DNA unwinding step-size of E. coli RecBCD determined from single turnover quenched-flow kinetic studies. J. molec. Biol. 324, 409-428.
    • (2002) J. Molec. Biol. , vol.324 , pp. 409-428
    • Lucius, A.L.1    Vindigni, A.2    Gregorian, R.3    Ali, J.A.4    Taylor, A.F.5    Smith, G.R.6    Lohman, T.M.7
  • 146
    • 0035920173 scopus 로고    scopus 로고
    • Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase
    • LUDLAM, A. V., MCNATT, M. W., CARR, K. M. & KAGUNI, J. M. (2001). Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase. J. biol. Chem. 276, 27345-27353.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27345-27353
    • Ludlam, A.V.1    Mcnatt, M.W.2    Carr, K.M.3    Kaguni, J.M.4
  • 147
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial rec A protein and the recombinational DNA repair of stalled replication forks
    • LUSETTI, S. L. & COX, M. M. (2002). The bacterial rec A protein and the recombinational DNA repair of stalled replication forks. Annu. Rev. Biochem. 71, 71-100.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2
  • 148
    • 0032717259 scopus 로고    scopus 로고
    • Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus
    • MACHIUS, M., HENRY, L., PALNITKAR, M. & DEISENHOFER, J. (1999). Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus. Proc. natn. Acad Sci. USA 96, 11717-11722.
    • (1999) Proc. Natn. Acad Sci. USA , vol.96 , pp. 11717-11722
    • Machius, M.1    Henry, L.2    Palnitkar, M.3    Deisenhofer, J.4
  • 149
    • 0012262720 scopus 로고    scopus 로고
    • A dimer of E. coli UvrD is the active form of the helicase in vitro
    • In Press
    • MALUF, N. K., FISHER, C. J. & LOHMAN, T. M. (In Press). A dimer of E. coli UvrD is the active form of the helicase in vitro. J. molec. Biol.
    • J. Molec. Biol.
    • Maluf, N.K.1    Fisher, C.J.2    Lohman, T.M.3
  • 150
    • 0030606278 scopus 로고    scopus 로고
    • Helicase-contrahelicase interaction and the mechanism of termination of DNA replication
    • MANNA, A. C., PAI, K. S., BUSSIERE, D. E., DAVIES, C., WHITE, S. W. & BASTIA, D. (1996). Helicase-contrahelicase interaction and the mechanism of termination of DNA replication. Cell 87, 881-891.
    • (1996) Cell , vol.87 , pp. 881-891
    • Manna, A.C.1    Pai, K.S.2    Bussiere, D.E.3    Davies, C.4    White, S.W.5    Bastia, D.6
  • 151
    • 0026777126 scopus 로고
    • Prokaryotic DNA replication
    • MARIANS, K. J. (1992). Prokaryotic DNA replication. Annu. Rev. Biochem. 61, 673-719.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 673-719
    • Marians, K.J.1
  • 152
    • 0034177963 scopus 로고    scopus 로고
    • PriA-directed replication fork testart in Escherichia coli
    • MARIANS, K. J. (2000). PriA-directed replication fork testart in Escherichia coli. Trends biochem. Sci. 25, 185-189.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 185-189
    • Marians, K.J.1
  • 153
    • 0022840629 scopus 로고
    • Escherichia coli helicase II (uryD gene product) translocates unidirectionally in a 3′ to 5′ direction
    • MATSON, S. W. (1986). Escherichia coli helicase II (uryD gene product) translocates unidirectionally in a 3′ to 5′ direction. J. biol. Chem. 261, 10169-10175.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10169-10175
    • Matson, S.W.1
  • 154
    • 0024318128 scopus 로고
    • Escherichia coli DNA helicase II (uvrD gene product) catalyzes the unwinding of DNA. RNA hybrids in vitro
    • MATSON, S. W. (1989). Escherichia coli DNA helicase II (uvrD gene product) catalyzes the unwinding of DNA. RNA hybrids in vitro. Proc. natn. Acad. Sci. USA 86, 4430-4434.
    • (1989) Proc. Natn. Acad. Sci. USA , vol.86 , pp. 4430-4434
    • Matson, S.W.1
  • 155
    • 0023654061 scopus 로고
    • DNA helicase II of Escherichia coli. Characterization of the single-stranded DNA-dependent NTPase and helicase activities
    • MATSON, S. W. & GEORGE, J. W. (1987). DNA helicase II of Escherichia coli. Characterization of the single-stranded DNA-dependent NTPase and helicase activities. J. biol. Chem. 262, 2066-2076.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2066-2076
    • Matson, S.W.1    George, J.W.2
  • 156
    • 0031690775 scopus 로고    scopus 로고
    • Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1
    • MAYEDA, A., MUNROE, S. H., XU, R. M. & KRAINER, A. R. (1998). Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1. RNA 4, 1111-1123.
    • (1998) RNA , vol.4 , pp. 1111-1123
    • Mayeda, A.1    Munroe, S.H.2    Xu, R.M.3    Krainer, A.R.4
  • 157
    • 0032481374 scopus 로고    scopus 로고
    • The function of the secondary DNA-binding site of RecA protein during DNA strand exchange
    • MAZIN, A. V. & KOWALCZYKOWSKI, S. C. (1998). The function of the secondary DNA-binding site of RecA protein during DNA strand exchange. EMBO J. 17, 1161-1168.
    • (1998) EMBO J. , vol.17 , pp. 1161-1168
    • Mazin, A.V.1    Kowalczykowski, S.C.2
  • 158
    • 0033617191 scopus 로고    scopus 로고
    • Escherichia coli DNA helicase II is active as a monomer
    • MECHANIC, L. E., HALL, M. C. & MATSON, S. W. (1999a). Escherichia coli DNA helicase II is active as a monomer. J. biol. Chem. 274, 12488-12498.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12488-12498
    • Mechanic, L.E.1    Hall, M.C.2    Matson, S.W.3
  • 159
    • 0032907367 scopus 로고    scopus 로고
    • A region near the C-terminal end of Escherichia coli DNA helicase II is required for single-stranded DNA binding
    • MECHANIC, L. E., LATTA, M. E. & MATSON, S. W. (1999b). A region near the C-terminal end of Escherichia coli DNA helicase II is required for single-stranded DNA binding. J. Bacteriol. 181, 2519-2526.
    • (1999) J. Bacteriol. , vol.181 , pp. 2519-2526
    • Mechanic, L.E.1    Latta, M.E.2    Matson, S.W.3
  • 161
    • 0034176967 scopus 로고    scopus 로고
    • Replication fork arrest and DNA recombination
    • MICHEL, B. (2000). Replication fork arrest and DNA recombination. Trends biochem. Sci. 25, 173-178.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 173-178
    • Michel, B.1
  • 162
    • 0037133210 scopus 로고    scopus 로고
    • Incision of DNA-protein crosslinks by UvrABC nuclease suggests a potential repair pathway involving nucleotide excision repair
    • MINKO, I. G., Zou, Y. & LLOYD, R. S. (2002). Incision of DNA-protein crosslinks by UvrABC nuclease suggests a potential repair pathway involving nucleotide excision repair. Proc. natn. Acad. Sci. USA 99, 1905-1909.
    • (2002) Proc. Natn. Acad. Sci. USA , vol.99 , pp. 1905-1909
    • Minko, I.G.1    Zou, Y.2    Lloyd, R.S.3
  • 163
    • 0029557494 scopus 로고
    • The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3′-incision
    • MOOLENAAR, G. F., FRANKEN, K. L. M. C., DIJKSTRA, D. M., THOMAS-OATES, J. E., VISSE, R., VAN DE PUTTE, P. & GOOSEN, N. (1995). The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3′-incision. J. biol. Chem. 270, 30508-30515.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30508-30515
    • Moolenaar, G.F.1    Franken, K.L.M.C.2    Dijkstra, D.M.3    Thomas-Oates, J.E.4    Visse, R.5    Van de Putte, P.6    Goosen, N.7
  • 164
    • 0034677897 scopus 로고    scopus 로고
    • The effect of the DNA flanking the lesion on formation of the UvrB-DNA preincision complex. Mechanism for the UvrA-mediated loading of UvrB onto a DNA damaged site
    • MOOLENAAR, G. F., MONACO, V., VAN DER MAREL, G. A., VAN BOOM, J. H., VISSE, R. & GOOSEN, N. (2000). The effect of the DNA flanking the lesion on formation of the UvrB-DNA preincision complex. Mechanism for the UvrA-mediated loading of UvrB onto a DNA damaged site. J. biol. Chem. 275, 8038-8043.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8038-8043
    • Moolenaar, G.F.1    Monaco, V.2    Van Der Marel, G.A.3    Van Boom, J.H.4    Visse, R.5    Goosen, N.6
  • 165
    • 0028598643 scopus 로고
    • The gene 59 protein of bacteriophage T4 modulates the intrinsic and single-stranded DNA-stimulated ATPase activities of gene 41 protein, the T4 replicative DNA helicase
    • MORRICAL, S. W., HEMPSTEAD, K. & MORRICAL, M. D. (1994). The gene 59 protein of bacteriophage T4 modulates the intrinsic and single-stranded DNA-stimulated ATPase activities of gene 41 protein, the T4 replicative DNA helicase. J. biol. Chem. 269, 33069-33081.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33069-33081
    • Morrical, S.W.1    Hempstead, K.2    Morrical, M.D.3
  • 166
    • 0037133182 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 and simian virus 40 T antigen helicases displace streptavidin from 5′-biotinylated oligonucleotides but not from 3′-biotinylated oligonucleotides: Evidence for directional bias in translocation on single-stranded DNA
    • MORRIS, P. D., BYRD, A. K., TACKETT, A. J., CAMERON, C. E., TANEGA, P., OTT, R., FANNING, E. & RANEY, K. D. (2002). Hepatitis C virus NS3 and simian virus 40 T antigen helicases displace streptavidin from 5′-biotinylated oligonucleotides but not from 3′-biotinylated oligonucleotides: evidence for directional bias in translocation on single-stranded DNA. Biochemistry 41, 2372-2378.
    • (2002) Biochemistry , vol.41 , pp. 2372-2378
    • Morris, P.D.1    Byrd, A.K.2    Tackett, A.J.3    Cameron, C.E.4    Tanega, P.5    Ott, R.6    Fanning, E.7    Raney, K.D.8
  • 167
    • 0033586732 scopus 로고    scopus 로고
    • DNA helicases displace streptavidin from biotin-labeled oligonucleotides
    • MORRIS, P. D. & RANEY, K. D. (1999). DNA helicases displace streptavidin from biotin-labeled oligonucleotides. Biochemistry 38, 5164-5171.
    • (1999) Biochemistry , vol.38 , pp. 5164-5171
    • Morris, P.D.1    Raney, K.D.2
  • 168
    • 0034681291 scopus 로고    scopus 로고
    • Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1·45 Å resolution crystal structure reveals a novel alphahelical two-domain fold
    • MUESER, T. C., JONES, C. E., NOSSAL, N. G. & HYDE, C. C. (2000). Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1·45 Å resolution crystal structure reveals a novel alphahelical two-domain fold. J. molec. Biol. 296, 597-612.
    • (2000) J. Molec. Biol. , vol.296 , pp. 597-612
    • Mueser, T.C.1    Jones, C.E.2    Nossal, N.G.3    Hyde, C.C.4
  • 169
    • 0035943446 scopus 로고    scopus 로고
    • Translocation of sigma(70) with RNA polymerase during transcription: Fluorescence resonance energy transfer assay for movement relative to DNA
    • MUKHOPADHYAY, J., KAPANIDIS, A. N., MEKLER, V., KORT-KHONJIA, E., EBRIGHT, Y. W. & EBRIGHT, R. H. (2001). Translocation of sigma(70) with RNA polymerase during transcription: fluorescence resonance energy transfer assay for movement relative to DNA. Cell 106, 453-463.
    • (2001) Cell , vol.106 , pp. 453-463
    • Mukhopadhyay, J.1    Kapanidis, A.N.2    Mekler, V.3    Kort-Khonjia, E.4    Ebright, Y.W.5    Ebright, R.H.6
  • 170
    • 0035859954 scopus 로고    scopus 로고
    • Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction
    • MULUGU, S., POTNIS, A., SHAMSUZZAMAN, TAYLOR, J., ALEXANDER, K. & BASTIA, D. (2001). Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction. Proc. natn. Acad. Sci. USA 98, 9569-9574.
    • (2001) Proc. Natn. Acad. Sci. USA , vol.98 , pp. 9569-9574
    • Mulugu, S.1    Potnis, A.2    Shamsuzzaman3    Taylor, J.4    Alexander, K.5    Bastia, D.6
  • 171
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • MURAKAMI, K. S., MASUDA, S., CAMPSELL, E. A., MUZZIN, O. & DARST, S. A. (2002a). Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science 296, 1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campsell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 172
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • MURAKAMI, K. S., MASUDA, S. & DARST, S. A. (2002b). Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science 296, 1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 173
    • 0021759104 scopus 로고
    • Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome
    • NAKAYAMA, N., ARAI, N., KAZIRO, Y. & ARAI, K. (1984). Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome. J. biol. Chem. 259, 88-96.
    • (1984) J. Biol. Chem. , vol.259 , pp. 88-96
    • Nakayama, N.1    Arai, N.2    Kaziro, Y.3    Arai, K.4
  • 175
    • 0034601780 scopus 로고    scopus 로고
    • Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: A model derived from DNA-binding studies of mutant proteins by surface plasmon resonance
    • NEYLON, C., BROWN, S. E., KRALICEK, A. V., MILES, C. S., LOVE, C. A. & DIXON, N. E. (2000). Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance. Biochemistry 39, 11989-11999.
    • (2000) Biochemistry , vol.39 , pp. 11989-11999
    • Neylon, C.1    Brown, S.E.2    Kralicek, A.V.3    Miles, C.S.4    Love, C.A.5    Dixon, N.E.6
  • 176
    • 0036161499 scopus 로고    scopus 로고
    • The spliceosome: No assembly required?
    • NILSEN, T. W. (2002). The spliceosome: no assembly required? Molec. Cell 9, 8-9.
    • (2002) Molec. Cell , vol.9 , pp. 8-9
    • Nilsen, T.W.1
  • 177
    • 0035102131 scopus 로고    scopus 로고
    • Bacteriophage T4 proteins replicate plasmids with a preformed R loop at the T4 ori(uvsY) replication origin in vitro
    • NOSSAL, N. G., DUDAS, K. C. & KREUZER, K. N. (2001). Bacteriophage T4 proteins replicate plasmids with a preformed R loop at the T4 ori(uvsY) replication origin in vitro. Molec. Cell 7, 31-41.
    • (2001) Molec. Cell , vol.7 , pp. 31-41
    • Nossal, N.G.1    Dudas, K.C.2    Kreuzer, K.N.3
  • 178
    • 0032541021 scopus 로고    scopus 로고
    • Spatial organization of transcription elongation complex in Escherichia coli
    • NUDLER, E., GUSAROV, I., AVETISSOVA, E., KOZLOV, M. & GOLDFARB, A. (1998). Spatial organization of transcription elongation complex in Escherichia coli. Science 281, 424-428.
    • (1998) Science , vol.281 , pp. 424-428
    • Nudler, E.1    Gusarov, I.2    Avetissova, E.3    Kozlov, M.4    Goldfarb, A.5
  • 179
    • 0019993713 scopus 로고
    • The uvrD gene of E. coli encodes a DNA-dependent ATPase
    • OEDA, K., HORIUCHI, T. & SEKIGUCHI, M. (1982). The uvrD gene of E. coli encodes a DNA-dependent ATPase. Nature 298, 98-100.
    • (1982) Nature , vol.298 , pp. 98-100
    • Oeda, K.1    Horiuchi, T.2    Sekiguchi, M.3
  • 180
    • 0024357127 scopus 로고
    • ATPase activity of the UvrA and UvrAB protein complexes of the Escherichia coli UvrABC endonuclease
    • OH, E. Y., CLAASSEN, L., THIAGALINGAM, S., MAZUR, S. & GROSSMAN, L. (1989). ATPase activity of the UvrA and UvrAB protein complexes of the Escherichia coli UvrABC endonuclease. Nucleic Acids Res. 17, 4145-4159.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4145-4159
    • Oh, E.Y.1    Claassen, L.2    Thiagalingam, S.3    Mazur, S.4    Grossman, L.5
  • 181
    • 1842396307 scopus 로고
    • Helicase properties of the Escherichia coli UvrAB protein complex
    • OH, E. Y. & GROSSMAN, L. (1987). Helicase properties of the Escherichia coli UvrAB protein complex. Proc. natn. Acad. Sci. USA 84, 3638-3642.
    • (1987) Proc. Natn. Acad. Sci. USA , vol.84 , pp. 3638-3642
    • Oh, E.Y.1    Grossman, L.2
  • 182
    • 0024570144 scopus 로고
    • Characterization of the helicase activity of the Escherichia coli UvrAB protein complex
    • OH, E. Y. & GROSSMAN, L. (1989). Characterization of the helicase activity of the Escherichia coli UvrAB protein complex. J. biol. Chem. 264, 1336-1343.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1336-1343
    • Oh, E.Y.1    Grossman, L.2
  • 183
    • 0024371067 scopus 로고
    • The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex
    • ORREN, D. K. & SANCAR, A. (1989). The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex. Proc. natn. Acad. Sci. USA 86, 5237-5241.
    • (1989) Proc. Natn. Acad. Sci. USA , vol.86 , pp. 5237-5241
    • Orren, D.K.1    Sancar, A.2
  • 184
    • 0025150833 scopus 로고
    • Formation and enzymatic properties of the UvrB DNA complex
    • ORREN, D. K. & SANCAR, A. (1990). Formation and enzymatic properties of the UvrB DNA complex. J. biol. Chem. 265, 15796-15803.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15796-15803
    • Orren, D.K.1    Sancar, A.2
  • 185
    • 0026595890 scopus 로고
    • Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I
    • ORREN, D. K., SELBY, C. P., HEARST, J. E. & SANCAR, A. (1992). Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I. J. biol. Chem. 267, 780-788.
    • (1992) J. Biol. Chem. , vol.267 , pp. 780-788
    • Orren, D.K.1    Selby, C.P.2    Hearst, J.E.3    Sancar, A.4
  • 186
    • 0032568637 scopus 로고    scopus 로고
    • Mapping the promoter DNA sites proximal to conserved regions of sigma 70 in an Escherichia coli RNA polymerase-lacUV5 open promoter complex
    • OWENS, J. T., CHMURA, A. J., MURAKAMI, K., FUJITA, N., ISHIHAMA, A. & MEARES, C. F. (1998a). Mapping the promoter DNA sites proximal to conserved regions of sigma 70 in an Escherichia coli RNA polymerase-lacUV5 open promoter complex. Biochemistry 37, 7670-7675.
    • (1998) Biochemistry , vol.37 , pp. 7670-7675
    • Owens, J.T.1    Chmura, A.J.2    Murakami, K.3    Fujita, N.4    Ishihama, A.5    Meares, C.F.6
  • 187
    • 0032568456 scopus 로고    scopus 로고
    • Mapping the sigma70 subunit contact sites on Escherichia coli RNA polymerase with a sigma70-conjugated chemical protease
    • OWENS, J. T., MIYAKE, R., MURAKAMI, K., CHMURA, A. J., FUJITA, N., ISHIHAMA, A. & MEARES, C. F. (1998b). Mapping the sigma70 subunit contact sites on Escherichia coli RNA polymerase with a sigma70-conjugated chemical protease. Proc. natn. Acad. Sci. USA 95, 6021-6026.
    • (1998) Proc. Natn. Acad. Sci. USA , vol.95 , pp. 6021-6026
    • Owens, J.T.1    Miyake, R.2    Murakami, K.3    Chmura, A.J.4    Fujita, N.5    Ishihama, A.6    Meares, C.F.7
  • 188
    • 0037077154 scopus 로고    scopus 로고
    • E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation
    • PARK, J. S., MARR, M. T. & ROBERTS, J. W. (2002). E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. Cell 109, 757-767.
    • (2002) Cell , vol.109 , pp. 757-767
    • Park, J.S.1    Marr, M.T.2    Roberts, J.W.3
  • 189
    • 0028968305 scopus 로고
    • Structure of a multisubunit complex that promotes DNA branch migration
    • PARSONS, C. A., STASIAK, A., BENNETT, R. J. & WEST, S. C. (1995). Structure of a multisubunit complex that promotes DNA branch migration. Nature 374, 375-378.
    • (1995) Nature , vol.374 , pp. 375-378
    • Parsons, C.A.1    Stasiak, A.2    Bennett, R.J.3    West, S.C.4
  • 190
    • 0034625124 scopus 로고    scopus 로고
    • Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex
    • PASMAN, Z. & VON HIPPEL, P. H. (2000). Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex. Biochemistry 39, 5573-5585.
    • (2000) Biochemistry , vol.39 , pp. 5573-5585
    • Pasman, Z.1    Von Hippel, P.H.2
  • 191
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • PATEL, S. S. & PICHA, K. M. (2000). Structure and function of hexameric helicases. Annu. Rev. Biochem. 69, 651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 192
    • 0036307672 scopus 로고    scopus 로고
    • FIS modulates the kinetics of successive interactions of RNA polymerase with the core and upstream regions of the tyrT promoter
    • PEMBERTON, I. K., MUSKHELISHVILI, G., TRAVERS, A. A. & BUCKLE, M. (2002). FIS modulates the kinetics of successive interactions of RNA polymerase with the core and upstream regions of the tyrT promoter. J. molec. Biol. 318, 651-663.
    • (2002) J. Molec. Biol. , vol.318 , pp. 651-663
    • Pemberton, I.K.1    Muskhelishvili, G.2    Travers, A.A.3    Buckle, M.4
  • 193
    • 0034732885 scopus 로고    scopus 로고
    • DNA binding in the central channel of bacteriophage T7 helicase-primase is a multistep process. Nucleotide hydrolysis is not required
    • PICHA, K. M., AHNERT, P. & PATEL, S. S. (2000). DNA binding in the central channel of bacteriophage T7 helicase-primase is a multistep process. Nucleotide hydrolysis is not required. Biochemistry 39, 6401-6409.
    • (2000) Biochemistry , vol.39 , pp. 6401-6409
    • Picha, K.M.1    Ahnert, P.2    Patel, S.S.3
  • 196
    • 0032537739 scopus 로고    scopus 로고
    • RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2
    • RAGHUNATHAN, P. L. & GUTHRIE, C. (1998a). RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2. Curr. Biol. 8, 847-855.
    • (1998) Curr. Biol. , vol.8 , pp. 847-855
    • Raghunathan, P.L.1    Guthrie, C.2
  • 197
    • 0032488860 scopus 로고    scopus 로고
    • A spliceosomal recycling factor that reanneals U4 and U6 small nuclear ribonucleoprotein particles
    • RAGHUNATHAN, P. L. & GUTHRIE, C. (1998b). A spliceosomal recycling factor that reanneals U4 and U6 small nuclear ribonucleoprotein particles. Science 279, 857-860.
    • (1998) Science , vol.279 , pp. 857-860
    • Raghunathan, P.L.1    Guthrie, C.2
  • 198
    • 17544363810 scopus 로고    scopus 로고
    • Stoichiometry and DNA unwinding by the bacteriophage T4 41:59 helicase
    • RANEY, K. D., CARVER, T. E. & BENKOVIC, S. J. (1996). Stoichiometry and DNA unwinding by the bacteriophage T4 41:59 helicase. J. biol. Chem. 271, 14074-14081.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14074-14081
    • Raney, K.D.1    Carver, T.E.2    Benkovic, S.J.3
  • 199
    • 0034814802 scopus 로고    scopus 로고
    • A novel single-molecule study to determine protein-protein association constants
    • RATCLIFF, G. C. & ERJE, D. A. (2001). A novel single-molecule study to determine protein-protein association constants. J. Am. Chem. Soc. 123, 5632-5635.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5632-5635
    • Ratcliff, G.C.1    Erje, D.A.2
  • 200
    • 0032939521 scopus 로고    scopus 로고
    • mRNA degradation in bacteria
    • RAUHUT, R. & KLUG, G. (1999). mRNA degradation in bacteria. FEMS Microbiol. Rev. 23, 353-370.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 353-370
    • Rauhut, R.1    Klug, G.2
  • 201
    • 0030745912 scopus 로고    scopus 로고
    • In vitro repair of oxidative DNA damage by human nucleotide excision repair system: Possible explanation for neurodegeneration in xeroderma pigmentosum patients
    • REARDON, J. T., BESSHO, T., KUNG, H. C., BOLTON, P. H. & SANCAR, A. (1997). In vitro repair of oxidative DNA damage by human nucleotide excision repair system: possible explanation for neurodegeneration in xeroderma pigmentosum patients. Proc. Natl. Acad. Sci. USA 94, 9463-9468.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9463-9468
    • Reardon, J.T.1    Bessho, T.2    Kung, H.C.3    Bolton, P.H.4    Sancar, A.5
  • 202
    • 0027244844 scopus 로고
    • Evidence of DNA bending in transcription complexes imaged by scanning force microscopy
    • REES, W. A., KELLER, R. W., VESENKA, J. P., YANG, G. & BUSTAMANTE, C. (1993). Evidence of DNA bending in transcription complexes imaged by scanning force microscopy. Science 260, 1646-1649.
    • (1993) Science , vol.260 , pp. 1646-1649
    • Rees, W.A.1    Keller, R.W.2    Vesenka, J.P.3    Yang, G.4    Bustamante, C.5
  • 203
    • 0242400018 scopus 로고    scopus 로고
    • Degradation of mRNA in bacteria: Emergence of ubiquitous features
    • REGNIER, P. & ARRAIANO, C. M. (2000). Degradation of mRNA in bacteria: emergence of ubiquitous features. Bioessays 22, 235-244.
    • (2000) Bioessays , vol.22 , pp. 235-244
    • Regnier, P.1    Arraiano, C.M.2
  • 204
    • 0030748519 scopus 로고    scopus 로고
    • Transcriptional activation via DNA-looping: Visualization of intermediates in the activation pathway of E. coli RNA polymerase-sigma54 holoenzyme by scanning force microscopy
    • RIPPE, K., GUTHOLD, M., VON HIPPEL, P. H. & BUSTAMANTE, C. (1997). Transcriptional activation via DNA-looping: visualization of intermediates in the activation pathway of E. coli RNA polymerase-sigma54 holoenzyme by scanning force microscopy. J. molec. Biol. 270, 125-138.
    • (1997) J. Molec. Biol. , vol.270 , pp. 125-138
    • Rippe, K.1    Guthold, M.2    Von Hippel, P.H.3    Bustamante, C.4
  • 205
    • 0033575742 scopus 로고    scopus 로고
    • Wrapping of DNA around the E. coli RNA polymerase open promoter complex
    • RIVETTI, C., GUTHOLD, M. & BUSTAMANTE, C. (1999). Wrapping of DNA around the E. coli RNA polymerase open promoter complex. EMBO J. 18, 4464-4475.
    • (1999) EMBO J. , vol.18 , pp. 4464-4475
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 207
    • 0024512057 scopus 로고
    • Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay
    • ROMAN, L. J. & KOWALCZYKOWSKI, S. C. (1989). Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay. Biochemistry 28, 2863-2873.
    • (1989) Biochemistry , vol.28 , pp. 2863-2873
    • Roman, L.J.1    Kowalczykowski, S.C.2
  • 208
    • 0021285415 scopus 로고
    • Analysis of bacteriophage phi X174 gene A protein-mediated termination and reinitiation of phi X DNA synthesis. II. Structural characterization of the covalent phi X A protein-DNA complex
    • ROTH, M. J., BROWN, D. R. & HURWITZ, J. (1984). Analysis of bacteriophage phi X174 gene A protein-mediated termination and reinitiation of phi X DNA synthesis. II. Structural characterization of the covalent phi X A protein-DNA complex. J. biol. Chem. 259, 10556-10568.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10556-10568
    • Roth, M.J.1    Brown, D.R.2    Hurwitz, J.3
  • 209
    • 0025127419 scopus 로고
    • Escherichia coli helicase II (UvrD) protein initiates DNA unwinding at nicks and blunt ends
    • RUNYON, G. T., BEAR, D. G. & LOHMAN, T. M. (1990). Escherichia coli helicase II (UvrD) protein initiates DNA unwinding at nicks and blunt ends. Proc. natn. Acad. Sci. USA 87, 6383-6387.
    • (1990) Proc. Natn. Acad. Sci. USA , vol.87 , pp. 6383-6387
    • Runyon, G.T.1    Bear, D.G.2    Lohman, T.M.3
  • 210
    • 0024407628 scopus 로고
    • Escherichia coli helicase II (uvrD) protein can completely unwind fully duplex linear and nicked circular DNA
    • RUNYON, G. T. & LOHMAN, T. M. (1989). Escherichia coli helicase II (uvrD) protein can completely unwind fully duplex linear and nicked circular DNA. J. biol. Chem. 264, 17502-17512.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17502-17512
    • Runyon, G.T.1    Lohman, T.M.2
  • 211
    • 0027222764 scopus 로고
    • Kinetics of Escherichia coli helicase II-catalyzed unwinding of fully duplex and nicked circular DNA
    • RUNYON, G. T. & LOHMAN, T. M. (1993). Kinetics of Escherichia coli helicase II-catalyzed unwinding of fully duplex and nicked circular DNA. Biochemistry 32, 4128-4138.
    • (1993) Biochemistry , vol.32 , pp. 4128-4138
    • Runyon, G.T.1    Lohman, T.M.2
  • 212
    • 0027455421 scopus 로고
    • Overexpression, purification, DNA binding, and dimerization of the Escherichia coli uvrD gene product (helicase II)
    • RUNYON, G. T., WONG, I. & LOHMAN, T.M. (1993). Overexpression, purification, DNA binding, and dimerization of the Escherichia coli uvrD gene product (helicase II). Biochemistry 32, 602-612.
    • (1993) Biochemistry , vol.32 , pp. 602-612
    • Runyon, G.T.1    Wong, I.2    Lohman, T.M.3
  • 213
    • 0032522423 scopus 로고    scopus 로고
    • Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC
    • SAN MARTIN, C., RADERMACHER, M., WOLPENSINGER, B., ENGEL, A., MILES, C. S., DIXON, N. E. & CARAZO, J. M. (1998). Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC. Structure 6, 501-509.
    • (1998) Structure , vol.6 , pp. 501-509
    • San Martin, C.1    Radermacher, M.2    Wolpensinger, B.3    Engel, A.4    Miles, C.S.5    Dixon, N.E.6    Carazo, J.M.7
  • 214
    • 0029892790 scopus 로고    scopus 로고
    • DNA excision repair
    • SANCAR, A. (1996). DNA excision repair. Annu. Rev. Biochem. 65, 43-81.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 43-81
    • Sancar, A.1
  • 215
    • 0027522357 scopus 로고
    • Molecular matchmakers
    • SANCAR, A. & HEARST, J. E. (1993). Molecular matchmakers. Science 259, 1415-1420.
    • (1993) Science , vol.259 , pp. 1415-1420
    • Sancar, A.1    Hearst, J.E.2
  • 217
    • 0032055765 scopus 로고    scopus 로고
    • Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing
    • SCHWER, B. & GROSS, C. H. (1998). Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. EMBO J. 17, 2086-2094.
    • (1998) EMBO J. , vol.17 , pp. 2086-2094
    • Schwer, B.1    Gross, C.H.2
  • 218
    • 0026019713 scopus 로고
    • PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
    • SCHWER, B. & GUTHRIE, C. (1991). PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349, 494-499.
    • (1991) Nature , vol.349 , pp. 494-499
    • Schwer, B.1    Guthrie, C.2
  • 219
    • 0017332435 scopus 로고
    • A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: Catalytic strand separation in advance of replication
    • SCOTT, J. F., EISENBERG, S., BERTSCH, L. L. & KORNBERG, A. (1977). A mechanism of duplex DNA replication revealed by enzymatic studies of phage phi X174: catalytic strand separation in advance of replication. Proc. natn. Acad. Sci. USA 74, 193-197.
    • (1977) Proc. Natn. Acad. Sci. USA , vol.74 , pp. 193-197
    • Scott, J.F.1    Eisenberg, S.2    Bertsch, L.L.3    Kornberg, A.4
  • 220
    • 0020053107 scopus 로고
    • Purification and properties of the uvrA protein from Escherichia coli
    • SEEBERG, E. & STEINUM, A.-L. (1982). Purification and properties of the uvrA protein from Escherichia coli. Proc. natn. Acad. Sci. USA 79, 988-992.
    • (1982) Proc. Natn. Acad. Sci. USA , vol.79 , pp. 988-992
    • Seeberg, E.1    Steinum, A.-L.2
  • 221
    • 0025774049 scopus 로고
    • Gene- and strand-specific repair in vitro: Partial purification of a transcription-repair coupling factor
    • SELBY, C. P. & SANCAR, A. (1991). Gene- and strand-specific repair in vitro: partial purification of a transcription-repair coupling factor. Proc. natn. Acad. Sci. USA 88, 8232-8236.
    • (1991) Proc. Natn. Acad. Sci. USA , vol.88 , pp. 8232-8236
    • Selby, C.P.1    Sancar, A.2
  • 222
    • 0027905034 scopus 로고
    • Molecular mechanism of transcription-repair coupling
    • SELBY, C. P. & SANCAR, A. (1993). Molecular mechanism of transcription-repair coupling. Science 260, 53-58.
    • (1993) Science , vol.260 , pp. 53-58
    • Selby, C.P.1    Sancar, A.2
  • 223
    • 0028969976 scopus 로고
    • Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties
    • SELBY, C. P. & SANCAR, A. (1995a). Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties. J. biol. Chem. 270, 4882-4889.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4882-4889
    • Selby, C.P.1    Sancar, A.2
  • 224
    • 0028949551 scopus 로고
    • Structure and function of transcription-repair coupling factor. II. Catalytic properties
    • SELBY, C. P. & SANCAR, A. (1995b). Structure and function of transcription-repair coupling factor. II. Catalytic properties. J. biol. Chem. 270, 4890-4895.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4890-4895
    • Selby, C.P.1    Sancar, A.2
  • 225
    • 0026354699 scopus 로고
    • Escherichia coli mfd mutant deficient in 'mutation frequency decline' lacks strand-specific repair: In vitro complementation with purified coupling factor
    • SELBY, C. P., WITKIN, E. M. & SANCAR, A. (1991). Escherichia coli mfd mutant deficient in 'mutation frequency decline' lacks strand-specific repair: in vitro complementation with purified coupling factor. Proc. natn. Acad. Sci. USA 88, 11574-11578.
    • (1991) Proc. Natn. Acad. Sci. USA , vol.88 , pp. 11574-11578
    • Selby, C.P.1    Witkin, E.M.2    Sancar, A.3
  • 226
    • 0027982114 scopus 로고
    • The sigma subunit conserved region 3 is part of '5′-face' of active center of Escherichia coli RNA polymerase
    • SEVERINOV, K., FENYO, D., SEVERINOVA, E., MUSTAEV, A., CHAIT, B. T., GOLDFARB A. & DARST, S. A. (1994). The sigma subunit conserved region 3 is part of '5′-face' of active center of Escherichia coli RNA polymerase. J. biol. Chem. 269, 20826-20828.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20826-20828
    • Severinov, K.1    Fenyo, D.2    Severinova, E.3    Mustaev, A.4    Chait, B.T.5    Goldfarb, A.6    Darst, S.A.7
  • 227
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution
    • SHAMOO, Y., KRUEGER, U., RICE, L. M., WILLIAMS, K. R. & STEITZ, T. A. (1997). Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution. Nature struct. Biol. 4, 215-222.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 215-222
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 228
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • SHAMOO, Y. & STEITZ, T. A. (1999). Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell 99, 155-166.
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 229
    • 0026654184 scopus 로고
    • Electron microscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex
    • SHI, Q., THRESHER, R., SANCAR, A. & GRIFFITH, J. (1992). Electron microscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex. J. molec. Biol. 226, 425-432.
    • (1992) J. Molec. Biol. , vol.226 , pp. 425-432
    • Shi, Q.1    Thresher, R.2    Sancar, A.3    Griffith, J.4
  • 230
    • 0024371540 scopus 로고
    • Altered promoter recognition by mutant forms of the sigma 70 subunit of Escherichia coli RNA polymerase
    • SIEGELE, D. A., HU, J. C., WALTER, W.A. & GROSS, C. A. (1989). Altered promoter recognition by mutant forms of the sigma 70 subunit of Escherichia coli RNA polymerase. J. molec. Biol. 206, 591-603.
    • (1989) J. Molec. Biol. , vol.206 , pp. 591-603
    • Siegele, D.A.1    Hu, J.C.2    Walter, W.A.3    Gross, C.A.4
  • 231
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • SINGLETON, M. R., SAWAYA, M. R., ELLENBERGER, T. & WIGLEY, D. B. (2000). Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101, 589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 232
    • 3142512132 scopus 로고    scopus 로고
    • The stretched DNA geometry, of recombination and repair nucleoprotein filaments
    • SINGLETON, S. F. & XIAO, J. (2001). The stretched DNA geometry, of recombination and repair nucleoprotein filaments. Biopolymers 61, 145-158.
    • (2001) Biopolymers , vol.61 , pp. 145-158
    • Singleton, S.F.1    Xiao, J.2
  • 233
    • 0037059785 scopus 로고    scopus 로고
    • The beta-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions
    • SKORVAGA, M., THEIS, K., MANDAVILLI, B. S., KISKER, C. & VAN HOUTEN, B. (2002). The beta-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. J. biol. Chem. 277, 1553-1559.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1553-1559
    • Skorvaga, M.1    Theis, K.2    Mandavilli, B.S.3    Kisker, C.4    Van Houten, B.5
  • 234
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: Motors, clocks, springs, and things
    • STALEY, J. P. & GUTHRIE, C. (1998). Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92, 315-326.
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 235
    • 0033010430 scopus 로고    scopus 로고
    • An RNA switch at the 5′ splice site requires ATP and the DEAD box protein Prp28p
    • STALEY, J. P. & GUTHRIE, C. (1999). An RNA switch at the 5′ splice site requires ATP and the DEAD box protein Prp28p. Molec. Cell 3, 55-64.
    • (1999) Molec. Cell , vol.3 , pp. 55-64
    • Staley, J.P.1    Guthrie, C.2
  • 236
    • 0036308760 scopus 로고    scopus 로고
    • The intercalating β-hairpin of T7 RNA polymerase plays a role in promoter DNA melting and in stabilizing the melted DNA for efficient RNA synthesis
    • STANO, N. M. & PATEL, S. S. (2002). The intercalating β-hairpin of T7 RNA polymerase plays a role in promoter DNA melting and in stabilizing the melted DNA for efficient RNA synthesis. J. molec. Biol. 315, 1009-1025.
    • (2002) J. Molec. Biol. , vol.315 , pp. 1009-1025
    • Stano, N.M.1    Patel, S.S.2
  • 237
    • 0028050051 scopus 로고
    • The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA
    • STASIAK, A., TSANEVA, I. R., WEST, S. C., BENSON, C. J., YU, X. & EGELMA, E. H. (1994). The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA. Proc. natn. Acad. Sci. USA 91, 7618-7622.
    • (1994) Proc. Natn. Acad. Sci. USA , vol.91 , pp. 7618-7622
    • Stasiak, A.1    Tsaneva, I.R.2    West, S.C.3    Benson, C.J.4    Yu, X.5    Egelma, E.H.6
  • 238
  • 239
    • 0344271983 scopus 로고
    • Prokaryotic and eukaryotic RNA polymerases have homologous core subunits
    • SWEETSER, D., NONET, M. & YOUNG, R.A. (1987). Prokaryotic and eukaryotic RNA polymerases have homologous core subunits. Proc. natn. Acad. Sci. USA 84, 1192-1196.
    • (1987) Proc. Natn. Acad. Sci. USA , vol.84 , pp. 1192-1196
    • Sweetser, D.1    Nonet, M.2    Young, R.A.3
  • 240
    • 0028798513 scopus 로고
    • Functional interactions of gene 32, 41, and 59 proteins of bacteriophage T4
    • TARUMI, K. & YONESAKI, T. (1995). Functional interactions of gene 32, 41, and 59 proteins of bacteriophage T4. J. biol. Chem. 270, 2614-2619.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2614-2619
    • Tarumi, K.1    Yonesaki, T.2
  • 241
    • 0028158655 scopus 로고
    • The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNA
    • TEIGELKAMP, S., McGARVEY, M., & BEGGS, J. D. (1994). The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNA. EMBO J. 13, 888-897.
    • (1994) EMBO J. , vol.13 , pp. 888-897
    • Teigelkamp, S.1    McGarvey, M.2    Beggs, J.D.3
  • 242
    • 0033573066 scopus 로고    scopus 로고
    • Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair
    • THEIS, K., CHEN, P. J., SKORVAGA, M., VAN HOUTEN, B. & KISKER, C. (1999). Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair. EMBO J. 18, 6899-6907.
    • (1999) EMBO J. , vol.18 , pp. 6899-6907
    • Theis, K.1    Chen, P.J.2    Skorvaga, M.3    Van Houten, B.4    Kisker, C.5
  • 243
    • 0027198345 scopus 로고
    • The multiple roles for ATP in the Escherichia coli UvrABC endonuclease-catalyzed incision reaction
    • THIAGALINGAM, S. & GROSSMAN, L. (1993). The multiple roles for ATP in the Escherichia coli UvrABC endonuclease-catalyzed incision reaction. J. biol. Chem. 268, 18382-18389.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18382-18389
    • Thiagalingam, S.1    Grossman, L.2
  • 244
    • 0035957687 scopus 로고    scopus 로고
    • Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins
    • TOULOKHONOV, I., ARSTIMOVITCH, I. & LANDICK, R. (2001). Allosteric control of RNA polymerase by a site that contacts nascent RNA hairpins. Science 292, 730-733.
    • (2001) Science , vol.292 , pp. 730-733
    • Toulokhonov, I.1    Arstimovitch, I.2    Landick, R.3
  • 245
    • 0027158626 scopus 로고
    • RecQ DNA helicase of Escherichia coli. Characterization of the helix-unwinding activity with emphasis on the effect of single-stranded DNA-binding protein
    • UMEZU, K. & NAKAYAMA, H. (1993). RecQ DNA helicase of Escherichia coli. Characterization of the helix-unwinding activity with emphasis on the effect of single-stranded DNA-binding protein. J. molec. Biol. 230, 1145-1150.
    • (1993) J. Molec. Biol. , vol.230 , pp. 1145-1150
    • Umezu, K.1    Nakayama, H.2
  • 247
    • 0035909835 scopus 로고    scopus 로고
    • A zinc ribbon protein in DNA replication: Primer synthesis and macromolecular interactions by the bacteriophage T4 primase
    • VALENTINE, A. M., ISHMAEL, F. T., SHIER, V. K. & BENKOVIC, S. J. (2001). A zinc ribbon protein in DNA replication: primer synthesis and macromolecular interactions by the bacteriophage T4 primase. Biochemistry 40, 15074-15085.
    • (2001) Biochemistry , vol.40 , pp. 15074-15085
    • Valentine, A.M.1    Ishmael, F.T.2    Shier, V.K.3    Benkovic, S.J.4
  • 248
    • 0035979798 scopus 로고    scopus 로고
    • The primase active site is on the outside of the hexameric bacteriophage T7 gene 4 helicase-primase ring
    • VANLOOCK, M. S., CHEN, Y. J., YU, X., PATEL, S. S. & EGELMAN, E. H. (2001). The primase active site is on the outside of the hexameric bacteriophage T7 gene 4 helicase-primase ring. J. molec. Biol. 311, 951-956.
    • (2001) J. Molec. Biol. , vol.311 , pp. 951-956
    • Vanloock, M.S.1    Chen, Y.J.2    Yu, X.3    Patel, S.S.4    Egelman, E.H.5
  • 249
    • 0020364657 scopus 로고
    • Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase
    • VENKATESAN, M., SILVER, L. L. & NOSSAL, N. G. (1982). Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase. J. biol. Chem. 257, 12426-12434.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12426-12434
    • Venkatesan, M.1    Silver, L.L.2    Nossal, N.G.3
  • 250
    • 0034681350 scopus 로고    scopus 로고
    • Catalytic sites for 3′ and 5′ incision of Escherichia coli nucleotide excision repair are both located in UvrC
    • VERHOEVEN, E. E., VAN KESTEREN, M., MOOLENAAR, G. F., VISSE, R. & GOOSEN, N. (2000). Catalytic sites for 3′ and 5′ incision of Escherichia coli nucleotide excision repair are both located in UvrC. J. biol. Chem. 275, 5120-5123.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5120-5123
    • Verhoeven, E.E.1    Van Kesteren, M.2    Moolenaar, G.F.3    Visse, R.4    Goosen, N.5
  • 251
    • 0036682613 scopus 로고    scopus 로고
    • The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands
    • VERHOEVEN, E. E., WYMAN, C., MOOLENAAR, G. F. & GOOSEN, N. (2002). The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands. EMBO J. 21, 4196-4205.
    • (2002) EMBO J. , vol.21 , pp. 4196-4205
    • Verhoeven, E.E.1    Wyman, C.2    Moolenaar, G.F.3    Goosen, N.4
  • 252
    • 0035254673 scopus 로고    scopus 로고
    • Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition
    • VERHOEVEN, E. E., WYMAN, C., MOOLENAAR, G. F., HOEIJMAKERS, J. H. & GOOSEN, N. (2001). Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition. EMBO J. 20, 601-611.
    • (2001) EMBO J. , vol.20 , pp. 601-611
    • Verhoeven, E.E.1    Wyman, C.2    Moolenaar, G.F.3    Hoeijmakers, J.H.4    Goosen, N.5
  • 253
    • 0037133955 scopus 로고    scopus 로고
    • 2+-dependent chemistry at the catalytic core?
    • 2+-dependent chemistry at the catalytic core? Cell 109, 149-152.
    • (2002) Cell , vol.109 , pp. 149-152
    • Villa, T.1    Pleiss, J.A.2    Guthrie, C.3
  • 254
    • 0037059797 scopus 로고    scopus 로고
    • Influence of DNA sequence on the positioning of RecA monomers in RecA-DNA cofilaments
    • VOLODIN, A. A. & CAMERINI-OTERO, R. D. (2002). Influence of DNA sequence on the positioning of RecA monomers in RecA-DNA cofilaments. J. biol. Chem. 277, 1614-1618.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1614-1618
    • Volodin, A.A.1    Camerini-Otero, R.D.2
  • 255
    • 0021154435 scopus 로고
    • Protein-nucleic acid interactions in transcription: A molecular analysis
    • VON HIPPEL, P. H., BEAR, D. G., MORGAN, W. D. & MCSWIGGEN, J. A. (1984). Protein-nucleic acid interactions in transcription: a molecular analysis. Annu. Rev. Biochem. 53, 389-446.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 389-446
    • Von Hippel, P.H.1    Bear, D.G.2    Morgan, W.D.3    Mcswiggen, J.A.4
  • 256
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their 'coupling' within macromolecular machines
    • VON HIPPEL, P. H. & DELAGOUTTE, E. (2001). A general model for nucleic acid helicases and their 'coupling' within macromolecular machines. Cell 104, 177-190.
    • (2001) Cell , vol.104 , pp. 177-190
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 257
    • 0037058904 scopus 로고    scopus 로고
    • Reaction pathways in transcript elongation
    • VON HIPPEL, P. H. & PASMAN, Z. (2002). Reaction pathways in transcript elongation. Biophys. Chem. 101-102, 401-423.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 401-423
    • Von Hippel, P.H.1    Pasman, Z.2
  • 258
    • 0025976369 scopus 로고
    • Transcript elongation and termination are competitive kinetic processes
    • VON HIPPEL, P.H. & YAGER, T.D. (1991). Transcript elongation and termination are competitive kinetic processes. Proc. natn. Acad. Sci. USA 88, 2307-2311.
    • (1991) Proc. Natn. Acad. Sci. USA , vol.88 , pp. 2307-2311
    • Von Hippel, P.H.1    Yager, T.D.2
  • 259
    • 0026556058 scopus 로고
    • The elongation-termination decision in transcription
    • VON HIPPEL, P.H. & YAGER, T.D. (1992). The elongation-termination decision in transcription. Science 255, 809-812.
    • (1992) Science , vol.255 , pp. 809-812
    • Von Hippel, P.H.1    Yager, T.D.2
  • 260
    • 0032525149 scopus 로고    scopus 로고
    • The DEAH-box protein PRP22 is an ATPase that mediates ATP-dependent mRNA release from the spliceosome and unwinds RNA duplexes
    • WAGNER, J. D., JANKOWSKY, E., COMPANY, M., PYLE, A. M. & ABELSON, J.H. (1998). The DEAH-box protein PRP22 is an ATPase that mediates ATP-dependent mRNA release from the spliceosome and unwinds RNA duplexes. EMBO J. 17, 2926-2937.
    • (1998) EMBO J. , vol.17 , pp. 2926-2937
    • Wagner, J.D.1    Jankowsky, E.2    Company, M.3    Pyle, A.M.4    Abelson, J.H.5
  • 261
    • 0025066083 scopus 로고
    • Changes in conserved region 2 of Escherichia coli sigma 70 affecting promoter recognition
    • WALDBURGER, C., GARDELLA, T., WONG, R. & SUSSKIND, M. M. (1990). Changes in conserved region 2 of Escherichia coli sigma 70 affecting promoter recognition. J. molec. Biol. 215, 267-276.
    • (1990) J. Molec. Biol. , vol.215 , pp. 267-276
    • Waldburger, C.1    Gardella, T.2    Wong, R.3    Susskind, M.M.4
  • 262
    • 0030847146 scopus 로고    scopus 로고
    • Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 1. Characterization and analysis of the reaction
    • WALSTROM, K. M., DOZONO, J. M., ROBIC, S. & VON HIPPEL, P. H. (1997a). Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 1. Characterization and analysis of the reaction. Biochemistry 36, 7980-7992.
    • (1997) Biochemistry , vol.36 , pp. 7980-7992
    • Walstrom, K.M.1    Dozono, J.M.2    Robic, S.3    Von Hippel, P.H.4
  • 263
    • 0030848285 scopus 로고    scopus 로고
    • Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding
    • WALSTROM, K. M., DOZONO, J. M. & VON HIPPEL, P. H. (1997b). Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding. Biochemistry 36, 7993-8004.
    • (1997) Biochemistry , vol.36 , pp. 7993-8004
    • Walstrom, K.M.1    Dozono, J.M.2    Von Hippel, P.H.3
  • 264
    • 0027156376 scopus 로고
    • Escherichia coli transcription termination factor rho. I. ATPase activation by oligonucleotide cofactors
    • WANG, Y. & VON HIPPEL P.H. (1993). Escherichia coli transcription termination factor rho. I. ATPase activation by oligonucleotide cofactors. J. biol. Chem. 268, 13940-13946.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13940-13946
    • Wang, Y.1    Von Hippel, P.H.2
  • 265
    • 0032499075 scopus 로고    scopus 로고
    • The DEAH-box splicing factor Prp16 unwinds RNA duplexes in vitro
    • WANG, Y., WAGNER, J. D. & GUTHRIE, C. (1998). The DEAH-box splicing factor Prp16 unwinds RNA duplexes in vitro. Curr. Biol. 8, 441-451.
    • (1998) Curr. Biol. , vol.8 , pp. 441-451
    • Wang, Y.1    Wagner, J.D.2    Guthrie, C.3
  • 266
    • 10244263498 scopus 로고    scopus 로고
    • Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding
    • WASHINGTON, M. T., ROSENBERG, A.H., GRIFFIN, K., STUDIER, F. W. & PATEL, S. S. (1996). Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding. J. biol. Chem. 271, 26825-26834.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26825-26834
    • Washington, M.T.1    Rosenberg, A.H.2    Griffin, K.3    Studier, F.W.4    Patel, S.S.5
  • 267
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DnaB helicase: Implications for structure rearrangements in the helicase hexamer
    • WEIGELT, J., BROWN, S. E., MILES, C. S., DIXON, N. E. & OTTING, G. (1999). NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Struct. Folding Design 7, 681-690.
    • (1999) Struct. Folding Design , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4    Otting, G.5
  • 268
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • WEST, S. C. (1997). Processing of recombination intermediates by the RuvABC proteins. Annu. Rev. Genet. 31, 213-244.
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 269
    • 0032544610 scopus 로고    scopus 로고
    • RuvA gets X-rayed on holliday
    • WEST, S. C. (1998). RuvA gets X-rayed on holliday. Cell 94, 699-701.
    • (1998) Cell , vol.94 , pp. 699-701
    • West, S.C.1
  • 271
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • WILL, C. L. & LUHRMANN, R. (2001). Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell Biol. 13, 290-301.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 272
    • 0028091898 scopus 로고
    • Stability of Escherichia coli transcription complexes near an intrinsic terminator
    • WILSON, K. S. & VON HIPPEL, P. H. (1994). Stability of Escherichia coli transcription complexes near an intrinsic terminator. J. molec. Biol. 244, 36-51.
    • (1994) J. Molec. Biol. , vol.244 , pp. 36-51
    • Wilson, K.S.1    Von Hippel, P.H.2
  • 273
    • 0029073396 scopus 로고
    • Transcription termination at intrinsic terminators: The role of the RNA hairpin
    • WILSON, K. S. & VON HIPPEL, P. H. (1995). Transcription termination at intrinsic terminators: the role of the RNA hairpin. Proc. natn. Acad. Sci. USA 92, 8793-8797.
    • (1995) Proc. Natn. Acad. Sci. USA , vol.92 , pp. 8793-8797
    • Wilson, K.S.1    Von Hippel, P.H.2
  • 274
    • 0036310983 scopus 로고    scopus 로고
    • Elucidating a key intermediate in homologous DNA strand exchange: Structural characterization of the RecA-triple-stranded DNA complex using fluorescence resonance energy transfer
    • XIAO, J. & SINGLETON, S. F. (2002). Elucidating a key intermediate in homologous DNA strand exchange: structural characterization of the RecA-triple-stranded DNA complex using fluorescence resonance energy transfer. J. molec. Biol. 320, 529-558.
    • (2002) J. Molec. Biol. , vol.320 , pp. 529-558
    • Xiao, J.1    Singleton, S.F.2
  • 275
    • 0035954387 scopus 로고    scopus 로고
    • Helicase assembly protein Gp59 of bacteriophage T4: Fluorescence anisotropy and sedimentation studies of complexes formed with derivatives of Gp32, the phage ssDNA binding protein
    • XU, H., WANG, Y., BLEUIT, J. S. & MORRICAL, S. W. (2001). Helicase assembly protein Gp59 of bacteriophage T4: fluorescence anisotropy and sedimentation studies of complexes formed with derivatives of Gp32, the phage ssDNA binding protein. Biochemistry 40, 7651-7661.
    • (2001) Biochemistry , vol.40 , pp. 7651-7661
    • Xu, H.1    Wang, Y.2    Bleuit, J.S.3    Morrical, S.W.4
  • 276
    • 0034677944 scopus 로고    scopus 로고
    • Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function
    • XU, L. & MARIANS, K. J. (2000). Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function. J. biol. Chem. 275, 8196-8205.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8196-8205
    • Xu, L.1    Marians, K.J.2
  • 277
    • 0031569797 scopus 로고    scopus 로고
    • Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs
    • XU, R. M., JOKHAN, L., CHENG, X., MAYEDA, A. & KRAINER, A. R. (1997). Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs. Structure 5, 559-570.
    • (1997) Structure , vol.5 , pp. 559-570
    • Xu, R.M.1    Jokhan, L.2    Cheng, X.3    Mayeda, A.4    Krainer, A.R.5
  • 278
    • 0026084789 scopus 로고
    • A thermodynamic analysis of RNA transcript elongation and termination in Escherichia coli
    • YAGER, T. D. & VON HIPPEL, P. H. (1991). A thermodynamic analysis of RNA transcript elongation and termination in Escherichia coli. Biochemistry 30, 1097-1118.
    • (1991) Biochemistry , vol.30 , pp. 1097-1118
    • Yager, T.D.1    Von Hippel, P.H.2
  • 280
    • 0029379540 scopus 로고
    • The search for DNA homology does not limit stable homologous pairing promoted by RecA protein
    • YANCEY-WRONA, J. E. & CAMERINI-OTERO, R. D. (1995). The search for DNA homology does not limit stable homologous pairing promoted by RecA protein. Curr. Biol. 5, 1149-1158.
    • (1995) Curr. Biol. , vol.5 , pp. 1149-1158
    • Yancey-Wrona, J.E.1    Camerini-Otero, R.D.2
  • 281
    • 0033597435 scopus 로고    scopus 로고
    • Mechanism of intrinsic transcription termination and and termination
    • YARNELL, W. S. & ROBERTS, J. W. (1999). Mechanism of intrinsic transcription termination and and termination. Science 284, 611-615.
    • (1999) Science , vol.284 , pp. 611-615
    • Yarnell, W.S.1    Roberts, J.W.2
  • 282
    • 0037123763 scopus 로고    scopus 로고
    • Views of transcription initiation
    • YOUNG, B. A., GRUBER, T. M. & GROSS, C. A. (2002). Views of transcription initiation. Cell 109, 417-420.
    • (2002) Cell , vol.109 , pp. 417-420
    • Young, B.A.1    Gruber, T.M.2    Gross, C.A.3
  • 283
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary states
    • YU, X., JEZEWSKA M. J., BUJALOWSKI, W. & EGELMAN, E. H. (1996). The hexameric E. coli DnaB helicase can exist in different quaternary states. J. molec. Biol. 259, 7-14.
    • (1996) J. Molec. Biol. , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4
  • 284
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • ZHANG, G., CAMPBELL, E. A., MINAKHIN, L., RICHTER, C., SEVERINOV, K. & DARST, S. A. (1999). Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell 98, 811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 285
    • 0031936257 scopus 로고    scopus 로고
    • Identification and characterization of Escherichia coli DNA helicase II mutants that exhibit increased unwinding efficiency
    • ZHANG, G., DENG, E., BAUGH, L. & KUSHNER, S. R. (1998). Identification and characterization of Escherichia coli DNA helicase II mutants that exhibit increased unwinding efficiency. J. Bacteriol. 180, 377-387.
    • (1998) J. Bacteriol. , vol.180 , pp. 377-387
    • Zhang, G.1    Deng, E.2    Baugh, L.3    Kushner, S.R.4
  • 286
    • 0035946915 scopus 로고    scopus 로고
    • Appropriate initiation of the strand exchange reaction promoted by RecA protein requires ATP hydrolysis
    • ZHANG, Z., YOON, D., LAPORTE, J. R. & CHEN, J. (2001). Appropriate initiation of the strand exchange reaction promoted by RecA protein requires ATP hydrolysis. J. molec. Biol. 309, 29-43.
    • (2001) J. Molec. Biol. , vol.309 , pp. 29-43
    • Zhang, Z.1    Yoon, D.2    Laporte, J.R.3    Chen, J.4
  • 287
    • 0032508378 scopus 로고    scopus 로고
    • Rho-dependent termination within the trp t′ terminator. I. Effects of rho loading and template sequence
    • ZHU, A. Q. & von HIPPEL, P. H. (1998). Rho-dependent termination within the trp t′ terminator. I. Effects of rho loading and template sequence. Biochemistry 37, 11202-11214.
    • (1998) Biochemistry , vol.37 , pp. 11202-11214
    • Zhu, A.Q.1    Von Hippel, P.H.2
  • 288
    • 0035814936 scopus 로고    scopus 로고
    • Hierarchy of DNA damage recognition in Escherichia coli nucleotide excision repair
    • ZOU, Y., LUO, C. & GEACINTOV, N. E. (2001). Hierarchy of DNA damage recognition in Escherichia coli nucleotide excision repair. Biochemistry 40, 2923-2931.
    • (2001) Biochemistry , vol.40 , pp. 2923-2931
    • Zou, Y.1    Luo, C.2    Geacintov, N.E.3
  • 289
    • 0033199492 scopus 로고    scopus 로고
    • Strand opening by the UvrA(2)B complex allows dynamic recognition of DNA damage
    • ZOU, Y. & VAN HOUTEN, B. (1999). Strand opening by the UvrA(2)B complex allows dynamic recognition of DNA damage. EMBO J. 18, 4889-4901.
    • (1999) EMBO J. , vol.18 , pp. 4889-4901
    • Zou, Y.1    Van Houten, B.2


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