메뉴 건너뛰기




Volumn 290, Issue 23, 2015, Pages 14626-14636

Interaction with single-stranded DNA-binding protein stimulates escherichia coli ribonuclease HI enzymatic activity

Author keywords

[No Author keywords available]

Indexed keywords

BINS; COMPLEXATION; DNA; ENZYMES; ESCHERICHIA COLI; GENES; MOBILE SECURITY; NUCLEIC ACIDS; REACTION INTERMEDIATES; RNA;

EID: 84930632519     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.655134     Document Type: Article
Times cited : (60)

References (88)
  • 1
    • 0003890119 scopus 로고
    • 2nd Ed. W. H. Freeman, New York
    • Kornberg, A., and Baker, T. A. (1992) DNA Replication, 2nd Ed., pp. 275-283, W. H. Freeman, New York
    • (1992) DNA Replication , pp. 275-283
    • Kornberg, A.1    Baker, T.A.2
  • 2
    • 25144434608 scopus 로고    scopus 로고
    • (Higgins, N. P., ed) ASM Press, Washington, D. C
    • Hingorani, M. M., and O'Donnell, M. (2005) in The Bacterial Chromosome (Higgins, N. P., ed) pp. 193-216, ASM Press, Washington, D. C.
    • (2005) The Bacterial Chromosome , pp. 193-216
    • Hingorani, M.M.1    O'Donnell, M.2
  • 3
    • 0032584643 scopus 로고    scopus 로고
    • Anintegrated model of the transcription complex in elongation, termination, and editing
    • von Hippel, P. H.(1998) Anintegrated model of the transcription complex in elongation, termination, and editing. Science 281, 660-665
    • (1998) Science , vol.281 , pp. 660-665
    • Von Hippel, P.H.1
  • 4
    • 84891145437 scopus 로고    scopus 로고
    • Replication of the escherichia coli chromosome in RNase HI-deficient cells: Multiple initiation regions and fork dynamics
    • Maduike, N. Z., and Tehranchi., A. K., Wang, J. D., and Kreuzer, K. N. (2014) Replication of the Escherichia coli chromosome in RNase HI-deficient cells: multiple initiation regions and fork dynamics. Mol. Microbiol. 91, 39-56
    • (2014) Mol. Microbiol. , vol.91 , pp. 39-56
    • Maduike, N.Z.1    Tehranchi, A.K.2    Wang, J.D.3    Kreuzer, K.N.4
  • 5
    • 84871946865 scopus 로고    scopus 로고
    • Rhodependent transcription termination is essential to prevent excessive genome-wide R-loops in escherichia coli
    • Leela, J. K., and Syeda., A. H., Anupama, K., and Gowrishankar, J. (2013) Rhodependent transcription termination is essential to prevent excessive genome-wide R-loops in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 110, 258-263
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 258-263
    • Leela, J.K.1    Syeda, A.H.2    Anupama, K.3    Gowrishankar, J.4
  • 6
    • 84860338675 scopus 로고    scopus 로고
    • R loops: From transcription byproducts to threats to genome stability
    • Aguilera, A., and García-Muse, T. (2012) R loops: from transcription byproducts to threats to genome stability. Mol. Cell 46, 115-124
    • (2012) Mol. Cell , vol.46 , pp. 115-124
    • Aguilera, A.1    García-Muse, T.2
  • 7
    • 84859087611 scopus 로고    scopus 로고
    • R-loop formation is a distinctive characteristic of unmethylated human CpG island promoters
    • Ginno, P. A., and Lott., P. L., Christensen, H. C., Korf, I., and Chédin, F. (2012) R-loop formation is a distinctive characteristic of unmethylated human CpG island promoters. Mol. Cell 45, 814-825
    • (2012) Mol. Cell , vol.45 , pp. 814-825
    • Ginno, P.A.1    Lott, P.L.2    Christensen, H.C.3    Korf, I.4    Chédin, F.5
  • 8
    • 77954841539 scopus 로고    scopus 로고
    • Loss of topoisomerase I leads to R-loop-mediated transcriptional blocks during ribosomal RNA synthesis
    • El Hage, A., French, S. L., and Beyer., A. L., and Tollervey, D. (2010) Loss of Topoisomerase I leads to R-loop-mediated transcriptional blocks during ribosomal RNA synthesis. Genes Dev. 24, 1546-1558
    • (2010) Genes Dev. , vol.24 , pp. 1546-1558
    • El Hage, A.1    French, S.L.2    Beyer, A.L.3    Tollervey, D.4
  • 9
    • 3042550193 scopus 로고    scopus 로고
    • Effects of RNA polymerase modifications on transcription-induced negative supercoiling and associated R-loop formation
    • Broccoli, S., Rallu, F., Sanscartier, P., Cerritelli, S. M., Crouch, R. J., and Drolet, M. (2004) Effects of RNA polymerase modifications on transcription-induced negative supercoiling and associated R-loop formation. Mol. Microbiol. 52, 1769-1779
    • (2004) Mol. Microbiol. , vol.52 , pp. 1769-1779
    • Broccoli, S.1    Rallu, F.2    Sanscartier, P.3    Cerritelli, S.M.4    Crouch, R.J.5    Drolet, M.6
  • 10
    • 84876188716 scopus 로고    scopus 로고
    • Transcription-replication encounters, consequences and genomic instability
    • Helmrich, A., Ballarino, M., Nudler, E., and Tora, L. (2013) Transcription-replication encounters, consequences and genomic instability. Nat. Struct. Mol. Biol. 20, 412-418
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 412-418
    • Helmrich, A.1    Ballarino, M.2    Nudler, E.3    Tora, L.4
  • 12
    • 84862763199 scopus 로고    scopus 로고
    • The conflict between DNA replication and transcription
    • McGlynn, P., and Savery., N. J., and Dillingham, M. S. (2012) The conflict between DNA replication and transcription. Mol. Microbiol. 85, 12-20
    • (2012) Mol. Microbiol. , vol.85 , pp. 12-20
    • McGlynn, P.1    Savery, N.J.2    Dillingham, M.S.3
  • 13
    • 84255198334 scopus 로고    scopus 로고
    • Collisions between replication and transcription complexes cause common fragile site instability at the longest human genes
    • Helmrich, A., Ballarino, M., and Tora, L. (2011) Collisions between replication and transcription complexes cause common fragile site instability at the longest human genes. Mol. Cell 44, 966-977
    • (2011) Mol. Cell , vol.44 , pp. 966-977
    • Helmrich, A.1    Ballarino, M.2    Tora, L.3
  • 14
    • 84255177502 scopus 로고    scopus 로고
    • RNase H and multiple RNA biogenesis factors cooperate to prevent RNA: DNA hybrids from generating genome instability
    • Wahba, L., and Amon., J. D., Koshland, D., and Vuica-Ross, M. (2011) RNase H and multiple RNA biogenesis factors cooperate to prevent RNA: DNA hybrids from generating genome instability. Mol. Cell 44, 978-988
    • (2011) Mol. Cell , vol.44 , pp. 978-988
    • Wahba, L.1    Amon, J.D.2    Koshland, D.3    Vuica-Ross, M.4
  • 15
    • 84859042868 scopus 로고    scopus 로고
    • Preventing replication stress to maintain genome stability: Resolving conflicts between replication and transcription
    • Bermejo, R., and Lai., M. S., and Foiani, M. (2012) Preventing replication stress to maintain genome stability: resolving conflicts between replication and transcription. Mol. Cell 45, 710-718
    • (2012) Mol. Cell , vol.45 , pp. 710-718
    • Bermejo, R.1    Lai, M.S.2    Foiani, M.3
  • 16
    • 79958724964 scopus 로고    scopus 로고
    • The replication-transcription conflict
    • Soultanas, P. (2011) The replication-transcription conflict. Transcription 2, 140-144
    • (2011) Transcription , vol.2 , pp. 140-144
    • Soultanas, P.1
  • 17
    • 77952527102 scopus 로고    scopus 로고
    • The transcription factor DksA prevents conflicts between DNA replication and transcription machinery
    • Tehranchi, A. K., and Blankschien., M. D., Zhang, Y., Halliday, J. A., Srivatsan, A., Peng, J., Herman, C., and Wang, J. D. (2010) The transcription factor DksA prevents conflicts between DNA replication and transcription machinery. Cell 141, 595-605
    • (2010) Cell , vol.141 , pp. 595-605
    • Tehranchi, A.K.1    Blankschien, M.D.2    Zhang, Y.3    Halliday, J.A.4    Srivatsan, A.5    Peng, J.6    Herman, C.7    Wang, J.D.8
  • 18
    • 84902081933 scopus 로고    scopus 로고
    • The contribution of co-transcriptional RNA: DNA hybrid structures to DNA damage and genome instability
    • Hamperl, S., and Cimprich, K. A. (2014) The contribution of co-transcriptional RNA: DNA hybrid structures to DNA damage and genome instability. DNA Repair 19, 84-94
    • (2014) DNA Repair , vol.19 , pp. 84-94
    • Hamperl, S.1    Cimprich, K.A.2
  • 20
    • 0025084228 scopus 로고
    • Ribonuclease H: From discovery to 3D structure
    • Crouch, R. J. (1990) Ribonuclease H: from discovery to 3D structure. New Biol. 2, 771-777
    • (1990) New Biol. , vol.2 , pp. 771-777
    • Crouch, R.J.1
  • 21
    • 0014801394 scopus 로고
    • Ribonuclease H. Anenzyme degrading the RNA moiety of DNA-RNA hybrids
    • Hausen, P., and Stein, H. (1970) Ribonuclease H. Anenzyme degrading the RNA moiety of DNA-RNA hybrids. Eur. J. Biochem. 14, 278-283
    • (1970) Eur. J. Biochem. , vol.14 , pp. 278-283
    • Hausen, P.1    Stein, H.2
  • 22
    • 0021859620 scopus 로고
    • Evidence that discontinuous DNA replication in escherichia coli is primed by approximately 10 to 12 residues of RNA starting with a purine
    • Kitani, T., Yoda, K., Ogawa, T., and Okazaki, T. (1985) Evidence that discontinuous DNA replication in Escherichia coli is primed by approximately 10 to 12 residues of RNA starting with a purine. J. Mol. Biol. 184, 45-52
    • (1985) J. Mol. Biol. , vol.184 , pp. 45-52
    • Kitani, T.1    Yoda, K.2    Ogawa, T.3    Okazaki, T.4
  • 23
    • 0021357260 scopus 로고
    • Function of RNase H in DNA replication revealed by RNase H defective mutants of escherichia coli
    • Ogawa, T., and Okazaki, T. (1984) Function of RNase H in DNA replication revealed by RNase H defective mutants of Escherichia coli. Mol. Gen. Genet. 193, 231-237
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 231-237
    • Ogawa, T.1    Okazaki, T.2
  • 24
    • 33645185950 scopus 로고    scopus 로고
    • Critical role of R-loops in processing replication blocks
    • Camps, M., and Loeb, L. A. (2005) Critical role of R-loops in processing replication blocks. Front. Biosci. 10, 689-698
    • (2005) Front. Biosci. , vol.10 , pp. 689-698
    • Camps, M.1    Loeb, L.A.2
  • 25
    • 0023663897 scopus 로고
    • Multiple mechanisms for initiation of ColE1 DNA replication: DNA synthesis in the presence and absence of ribonuclease H
    • Dasgupta, S., Masukata, H., and Tomizawa, J. (1987) Multiple mechanisms for initiation of ColE1 DNA replication: DNA synthesis in the presence and absence of ribonuclease H. Cell 51, 1113-1122
    • (1987) Cell , vol.51 , pp. 1113-1122
    • Dasgupta, S.1    Masukata, H.2    Tomizawa, J.3
  • 26
    • 1842391776 scopus 로고
    • Formation of an RNA primer for initiation of replication of ColE1 DNA by ribonuclease H
    • Itoh, T., and Tomizawa, J. (1980) Formation of an RNA primer for initiation of replication of ColE1 DNA by ribonuclease H. Proc. Natl. Acad. Sci. 77, 2450-2454
    • (1980) Proc. Natl. Acad. Sci. , vol.77 , pp. 2450-2454
    • Itoh, T.1    Tomizawa, J.2
  • 27
    • 0030737725 scopus 로고    scopus 로고
    • Stable DNA replication: Interplay between DNA replication, homologous recombination, and transcription
    • Kogoma, T. (1997) Stable DNA replication: interplay between DNA replication, homologous recombination, and transcription. Microbiol. Mol. Biol. Rev. 61, 212-238
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 212-238
    • Kogoma, T.1
  • 28
    • 0030426021 scopus 로고    scopus 로고
    • Mechanisms of primer RNA synthesis and D-loop/R-loop-dependent DNA replication in escherichia coli
    • Masai, H., and Arai, K. (1996) Mechanisms of primer RNA synthesis and D-loop/R-loop-dependent DNA replication in Escherichia coli. Biochimie 78, 1109-1117
    • (1996) Biochimie , vol.78 , pp. 1109-1117
    • Masai, H.1    Arai, K.2
  • 29
    • 0025147609 scopus 로고
    • Isolation and characterization of a second RNase H (RNase HII) of escherichia coli K-12 encoded by the rnhB gene
    • Itaya, M. (1990) Isolation and characterization of a second RNase H (RNase HII) of Escherichia coli K-12 encoded by the rnhB gene. Proc. Natl. Acad. Sci. U.S.A. 87, 8587-8591
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8587-8591
    • Itaya, M.1
  • 32
    • 84866462296 scopus 로고    scopus 로고
    • Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity
    • Hiller, B., Achleitner, M., Glage, S., Naumann, R., Behrendt, R., and Roers, A. (2012) Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity. J. Exp. Med. 209, 1419-1426
    • (2012) J. Exp. Med. , vol.209 , pp. 1419-1426
    • Hiller, B.1    Achleitner, M.2    Glage, S.3    Naumann, R.4    Behrendt, R.5    Roers, A.6
  • 34
    • 78650691470 scopus 로고    scopus 로고
    • The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks
    • Costes, A., Lecointe, F., McGovern, S., Quevillon-Cheruel, S., and Polard, P. (2010) The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks. PLoS Genet. 6, e1001238
    • (2010) PLoS Genet. , vol.6
    • Costes, A.1    Lecointe, F.2    McGovern, S.3    Quevillon-Cheruel, S.4    Polard, P.5
  • 35
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of escherichia coli
    • Meyer, R. R., and Laine, P. S. (1990) The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 54, 342-380
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 36
    • 0032479370 scopus 로고    scopus 로고
    • Identification of amino acids stabilizing the tetramerization of the single stranded DNA binding protein from escherichia coli
    • Carlini, L., Curth, U., Kindler, B., Urbanke, C., and Porter, R. D. (1998) Identification of amino acids stabilizing the tetramerization of the single stranded DNA binding protein from Escherichia coli. FEBS Lett. 430, 197-200
    • (1998) FEBS Lett. , vol.430 , pp. 197-200
    • Carlini, L.1    Curth, U.2    Kindler, B.3    Urbanke, C.4    Porter, R.D.5
  • 37
    • 0016771382 scopus 로고
    • Properties of the escherichia coli DNA-binding (unwinding) protein interaction with nucleolytic enzymes and DNA
    • Molineux, I. J., and Gefter, M. L. (1975) Properties of the Escherichia coli DNA-binding (unwinding) protein interaction with nucleolytic enzymes and DNA. J. Mol. Biol. 98, 811-825
    • (1975) J. Mol. Biol. , vol.98 , pp. 811-825
    • Molineux, I.J.1    Gefter, M.L.2
  • 39
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E. Coli singlestranded DNA binding protein (SSB) with exonuclease I. The carboxyterminus of SSB is the recognition site for the nuclease
    • Genschel, J., Curth, U., and Urbanke, C. (2000) Interaction of E. coli singlestranded DNA binding protein (SSB) with exonuclease I. The carboxyterminus of SSB is the recognition site for the nuclease. Biol. Chem. 381, 183-192
    • (2000) Biol. Chem. , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 40
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand - The subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman, Z., Yuzhakov, A., Andjelkovic, J., and O'Donnell, M. (1998) Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J. 17, 2436-2449
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1    Yuzhakov, A.2    Andjelkovic, J.3    O'Donnell, M.4
  • 41
    • 0032483511 scopus 로고    scopus 로고
    • The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template
    • Glover, B. P., and McHenry, C. S. (1998) The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template. J. Biol. Chem. 273, 23476-23484
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 42
    • 0030014904 scopus 로고    scopus 로고
    • In vitro and in vivo function of the C-terminus of escherichia coli single-stranded DNA binding protein
    • Curth, U., Genschel, J., Urbanke, C., and Greipel, J. (1996) In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein. Nucleic Acids Res. 24, 2706-2711
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2706-2711
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4
  • 43
    • 0016296093 scopus 로고
    • Properties of the escherichia coli in DNA binding (unwinding) protein: Interaction with DNA polymerase and DNA
    • Molineux, I. J., and Gefter, M.L. (1974) Properties of the Escherichia coli in DNA binding (unwinding) protein: interaction with DNA polymerase and DNA. Proc. Natl. Acad. Sci. U.S.A. 71, 3858-3862
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 3858-3862
    • Molineux, I.J.1    Gefter, M.L.2
  • 44
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA - A three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov, A., Kelman, Z., and O'Donnell, M. (1999) Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96, 153-163
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 46
    • 0003903343 scopus 로고    scopus 로고
    • 3rd Ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J., and Russell, D. W. (2001) Molecular Cloning: A Laboratory Manual, 3rd Ed., pp. A2.2, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2001) Molecular Cloning: A Laboratory Manual , pp. A22
    • Sambrook, J.1    Russell, D.W.2
  • 47
    • 84879034275 scopus 로고    scopus 로고
    • PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein
    • Wessel, S.R., Marceau, A. H., Massoni, S.C., Zhou, R., Ha, T., Sandler, S. J., and Keck, J. L. (2013) PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein. J. Biol. Chem. 288, 17569-17578
    • (2013) J. Biol. Chem. , vol.288 , pp. 17569-17578
    • Wessel, S.R.1    Marceau, A.H.2    Massoni, S.C.3    Zhou, R.4    Ha, T.5    Sandler, S.J.6    Keck, J.L.7
  • 48
    • 0242567791 scopus 로고    scopus 로고
    • Metal activation and regulation of E. Coli RNase H
    • (Marshak, D. R., ed) Academic Press, San Diego, CA
    • Keck, J. L., and Marqusee, S. (1997) Metal activation and regulation of E. coli RNase H. in Techniques in Protein Chemistry VIII (Marshak, D. R., ed), pp. 409-416, Academic Press, San Diego, CA
    • (1997) Techniques in Protein Chemistry VIII , pp. 409-416
    • Keck, J.L.1    Marqusee, S.2
  • 49
    • 0029811784 scopus 로고    scopus 로고
    • Structure of the acid state of escherichia coli ribonuclease HI
    • Dabora, J. M., and Pelton., J. G., and Marqusee, S. (1996) Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry 35, 11951-11958
    • (1996) Biochemistry , vol.35 , pp. 11951-11958
    • Dabora, J.M.1    Pelton, J.G.2    Marqusee, S.3
  • 50
    • 84862702956 scopus 로고    scopus 로고
    • Structure and cellular dynamics of deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes
    • George, N. P., and Ngo., K. V., Chitteni-Pattu, S., Norais, C. A., and Battista., J. R., Cox, M. M., and Keck, J. L. (2012) Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes. J. Biol. Chem. 287, 22123-22132
    • (2012) J. Biol. Chem. , vol.287 , pp. 22123-22132
    • George, N.P.1    Ngo, K.V.2    Chitteni-Pattu, S.3    Norais, C.A.4    Battista, J.R.5    Cox, M.M.6    Keck, J.L.7
  • 51
    • 48249095036 scopus 로고    scopus 로고
    • Structural basis of escherichia coli singlestranded DNA-binding protein stimulation of exonuclease I
    • Lu, D., and Keck, J. L. (2008) Structural basis of Escherichia coli singlestranded DNA-binding protein stimulation of exonuclease I. Proc. Natl. Acad. Sci. U.S.A. 105, 9169-9174
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9169-9174
    • Lu, D.1    Keck, J.L.2
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • (Carter, C. W., and Sweet, R. M., eds) Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) in Methods in Enzymology (Carter, C. W., and Sweet, R. M., eds) pp. 307-326, Academic Press, New York
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 55
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein
    • Yang, W., and Hendrickson., W. A., Crouch, R. J., and Satow, Y. (1990) Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein. Science 249, 1398-1405
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4
  • 56
  • 57
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., and Isupov., M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 58
    • 77954257799 scopus 로고    scopus 로고
    • Con-surf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) Con-Surf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 61
    • 44949225070 scopus 로고    scopus 로고
    • Resolution of converging replication forks by RecQ and topoisomerase III
    • Suski, C., and Marians, K. J. (2008) Resolution of converging replication forks by RecQ and topoisomerase III. Mol. Cell 30, 779-789
    • (2008) Mol. Cell , vol.30 , pp. 779-789
    • Suski, C.1    Marians, K.J.2
  • 62
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman, C. J., and McGlynn, P. (2004) PriA helicase and SSB interact physically and functionally. Nucleic Acids Res. 32, 6378-6387
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 63
    • 0029929392 scopus 로고    scopus 로고
    • Protein-protein interactions between the escherichia coli single-stranded DNA-binding protein and exonuclease I
    • Sandigursky, M., Mendez, F., Bases, R. E., Matsumoto, T., and Franklin, W. A. (1996) Protein-protein interactions between the Escherichia coli single-stranded DNA-binding protein and exonuclease I. Radiat. Res. 145, 619-623
    • (1996) Radiat. Res. , vol.145 , pp. 619-623
    • Sandigursky, M.1    Mendez, F.2    Bases, R.E.3    Matsumoto, T.4    Franklin, W.A.5
  • 64
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in escherichia coli RecQ DNA helicase function
    • Shereda, R. D., and Bernstein., D. A., and Keck, J. L. (2007) A central role for SSB in Escherichia coli RecQ DNA helicase function. J. Biol. Chem. 282, 19247-19258
    • (2007) J. Biol. Chem. , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 66
    • 34248647207 scopus 로고    scopus 로고
    • SSB protein limits RecOR binding onto single-stranded DNA
    • Hobbs, M. D., Sakai, A., and Cox, M. M. (2007) SSB protein limits RecOR binding onto single-stranded DNA. J. Biol. Chem. 282, 11058-11067
    • (2007) J. Biol. Chem. , vol.282 , pp. 11058-11067
    • Hobbs, M.D.1    Sakai, A.2    Cox, M.M.3
  • 67
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between singlestranded DNA-binding proteins from escherichia coli and mycobacterium tuberculosisreveal that their C-terminal domains interact with uracil DNA glycosylases
    • Handa, P., Acharya, N., and Varshney, U. (2001) Chimeras between singlestranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosisreveal that their C-terminal domains interact with uracil DNA glycosylases. J. Biol. Chem. 276, 16992-16997
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 69
    • 59649104376 scopus 로고    scopus 로고
    • Identification of the SSB binding site on E. Coli RecQ reveals a conserved surface for binding SSB's C terminus
    • Shereda, R. D., and Reiter., N. J., Butcher, S. E., and Keck, J. L. (2009) Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus. J. Mol. Biol. 386, 612-625
    • (2009) J. Mol. Biol. , vol.386 , pp. 612-625
    • Shereda, R.D.1    Reiter, N.J.2    Butcher, S.E.3    Keck, J.L.4
  • 71
    • 79960790784 scopus 로고    scopus 로고
    • Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein
    • Ryzhikov, M., Koroleva, O., Postnov, D., Tran, A., and Korolev, S. (2011) Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein. Nucleic Acids Res. 39, 6305-6314
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6305-6314
    • Ryzhikov, M.1    Koroleva, O.2    Postnov, D.3    Tran, A.4    Korolev, S.5
  • 73
    • 0036693201 scopus 로고    scopus 로고
    • Chimeric RNA-DNA molecular beacon assay for ribonuclease H activity
    • Rizzo, J., and Gifford., L. K., Zhang, X., Gewirtz, A. M., and Lu, P. (2002) Chimeric RNA-DNA molecular beacon assay for ribonuclease H activity. Mol. Cell. Probes 16, 277-283
    • (2002) Mol. Cell. Probes , vol.16 , pp. 277-283
    • Rizzo, J.1    Gifford, L.K.2    Zhang, X.3    Gewirtz, A.M.4    Lu, P.5
  • 74
    • 80055089237 scopus 로고    scopus 로고
    • Mechanism of exonuclease I stimulation by the single-strand DNA-binding protein
    • Lu, D., and Myers., A. R., George, N. P., and Keck, J. L. (2011) Mechanism of exonuclease I stimulation by the single-strand DNA-binding protein. Nucleic Acids Res. 39, 6536-6545
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6536-6545
    • Lu, D.1    Myers, A.R.2    George, N.P.3    Keck, J.L.4
  • 75
    • 33745224311 scopus 로고    scopus 로고
    • Detection and structural analysis of R-loops
    • Yu, K., Roy, D., Huang, F. T., and Lieber, M. R. (2006) Detection and structural analysis of R-loops. Methods Enzymol. 409, 316-329
    • (2006) Methods Enzymol. , vol.409 , pp. 316-329
    • Yu, K.1    Roy, D.2    Huang, F.T.3    Lieber, M.R.4
  • 76
    • 84898841862 scopus 로고    scopus 로고
    • The yeast and human FACT chromatin-reorganizing complexes solve R-loop-mediated transcription-replication conflicts
    • Herrera-Moyano, E., Mergui, X., García-Rubio, M. L., Barroso, S., and Aguilera, A. (2014) The yeast and human FACT chromatin-reorganizing complexes solve R-loop-mediated transcription-replication conflicts. Genes Dev. 28, 735-748
    • (2014) Genes Dev. , vol.28 , pp. 735-748
    • Herrera-Moyano, E.1    Mergui, X.2    García-Rubio, M.L.3    Barroso, S.4    Aguilera, A.5
  • 77
    • 84887410764 scopus 로고    scopus 로고
    • Dealing with transcriptional outbursts during S phase to protect genomic integrity
    • Duch, A., de Nadal, E., and Posas, F. (2013) Dealing with transcriptional outbursts during S phase to protect genomic integrity. J. Mol. Biol. 425, 4745-4755
    • (2013) J. Mol. Biol. , vol.425 , pp. 4745-4755
    • Duch, A.1    De Nadal, E.2    Posas, F.3
  • 78
    • 84863023752 scopus 로고    scopus 로고
    • Interference between DNA replication and transcription as a cause of genomic instability
    • Lin, Y. L., and Pasero, P. (2012) Interference between DNA replication and transcription as a cause of genomic instability. Curr. Genomics 13, 65-73
    • (2012) Curr. Genomics , vol.13 , pp. 65-73
    • Lin, Y.L.1    Pasero, P.2
  • 79
    • 79952257414 scopus 로고    scopus 로고
    • Transcription and replication: Breaking the rules of the road causes genomic instability
    • Poveda, A. M., Le Clech, M., and Pasero, P. (2010) Transcription and replication: breaking the rules of the road causes genomic instability. Transcription 1, 99-102
    • (2010) Transcription , vol.1 , pp. 99-102
    • Poveda, A.M.1    Le Clech, M.2    Pasero, P.3
  • 80
    • 0141819093 scopus 로고    scopus 로고
    • Cotranscriptionally formed DNA: RNA hybrids mediate transcription elongation impairment and transcription-associated recombination
    • Huertas, P., and Aguilera, A. (2003) Cotranscriptionally formed DNA: RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol. Cell 12, 711-721
    • (2003) Mol. Cell , vol.12 , pp. 711-721
    • Huertas, P.1    Aguilera, A.2
  • 81
    • 77954371207 scopus 로고    scopus 로고
    • RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases
    • Baharoglu, Z., Lestini, R., Duigou, S., and Michel, B. (2010) RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases. Mol. Microbiol. 77, 324-336
    • (2010) Mol. Microbiol. , vol.77 , pp. 324-336
    • Baharoglu, Z.1    Lestini, R.2    Duigou, S.3    Michel, B.4
  • 82
    • 75649142564 scopus 로고    scopus 로고
    • The helicases din G, rep and UvrD cooperate to promote replication across transcription units in vivo
    • Boubakri, H., de Septenville, A. L., Viguera, E., and Michel, B. (2010) The helicases Din G, Rep and UvrD cooperate to promote replication across transcription units in vivo. EMBO J. 29, 145-157
    • (2010) EMBO J. , vol.29 , pp. 145-157
    • Boubakri, H.1    De Septenville, A.L.2    Viguera, E.3    Michel, B.4
  • 84
    • 84862673628 scopus 로고    scopus 로고
    • RNA polymerase backtracking in gene regulation and genome instability
    • Nudler, E. (2012) RNA polymerase backtracking in gene regulation and genome instability. Cell 149, 1438-1445
    • (2012) Cell , vol.149 , pp. 1438-1445
    • Nudler, E.1
  • 85
    • 80052008241 scopus 로고    scopus 로고
    • Linking RNA polymerase backtracking to genome instability in E. Coli
    • Dutta, D., Shatalin, K., Epshtein, V., Gottesman, M. E., and Nudler, E. (2011) Linking RNA polymerase backtracking to genome instability in E. coli. Cell 146, 533-543
    • (2011) Cell , vol.146 , pp. 533-543
    • Dutta, D.1    Shatalin, K.2    Epshtein, V.3    Gottesman, M.E.4    Nudler, E.5
  • 86
    • 77951589688 scopus 로고    scopus 로고
    • Cooperation between translating ribosomes and RNA polymerase in transcription elongation
    • Proshkin, S., and Rahmouni., A. R., Mironov, A., and Nudler, E. (2010) Cooperation between translating ribosomes and RNA polymerase in transcription elongation. Science 328, 504-508
    • (2010) Science , vol.328 , pp. 504-508
    • Proshkin, S.1    Rahmouni, A.R.2    Mironov, A.3    Nudler, E.4
  • 87
    • 0028966185 scopus 로고
    • Overexpression of RNase H partially complements the growth defect of an escherichia coli ΔtopA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase I
    • Drolet, M., Phoenix, P., Menzel, R., Massé, E., Liu, L. F., and Crouch, R. J. (1995) Overexpression of RNase H partially complements the growth defect of an Escherichia coli ΔtopA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase I. Proc. Natl. Acad. Sci. U.S.A. 92, 3526-3530
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3526-3530
    • Drolet, M.1    Phoenix, P.2    Menzel, R.3    Massé, E.4    Liu, L.F.5    Crouch, R.J.6
  • 88
    • 84892895021 scopus 로고    scopus 로고
    • PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry
    • Maréchal, A., and Li., J. M., Ji, X. Y., Wu, C. S., Yazinski, S. A., Nguyen, H. D., Liu, S., Jimenez, A. E., Jin, J., and Zou, L. (2014) PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry. Mol. Cell 53, 235-246
    • (2014) Mol. Cell , vol.53 , pp. 235-246
    • Maréchal, A.1    Li, J.M.2    Ji, X.Y.3    Wu, C.S.4    Yazinski, S.A.5    Nguyen, H.D.6    Liu, S.7    Jimenez, A.E.8    Jin, J.9    Zou, L.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.