메뉴 건너뛰기




Volumn 293, Issue 3, 1999, Pages 505-519

Helicase-defective RUVB(D113E) promotes RuvAB-mediated branch migration in vitro

Author keywords

ATPase; DNA repair; DNA unwinding; Holliday junction; Recombination

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; HELICASE; MUTANT PROTEIN;

EID: 0344069591     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3187     Document Type: Article
Times cited : (11)

References (76)
  • 2
    • 0028970354 scopus 로고
    • Unwinding of closed circular DNA by the Escherichia coli RuvA and RuvB recombination/repair proteins
    • Adams D. E., West S. C. Unwinding of closed circular DNA by the Escherichia coli RuvA and RuvB recombination/repair proteins. J. Mol. Biol. 247:1995;404-417.
    • (1995) J. Mol. Biol. , vol.247 , pp. 404-417
    • Adams, D.E.1    West, S.C.2
  • 3
    • 0030575805 scopus 로고    scopus 로고
    • Bypass of DNA heterologies during RuvAB-mediated three- And four-strand branch migration
    • Adams D. E., West S. C. Bypass of DNA heterologies during RuvAB-mediated three- and four-strand branch migration. J. Mol. Biol. 263:1996;582-596.
    • (1996) J. Mol. Biol. , vol.263 , pp. 582-596
    • Adams, D.E.1    West, S.C.2
  • 4
    • 1842328563 scopus 로고    scopus 로고
    • Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein
    • Bird L. E., Håkansson K., Pan H., Wigley D. B. Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein. Nucl. Acids Res. 25:1997;2620-2626.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 2620-2626
    • Bird, L.E.1    Håkansson, K.2    Pan, H.3    Wigley, D.B.4
  • 5
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - some probabilities and possibilities
    • Boyer P. D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta. 1140:1993;215-250.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 6
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
    • Bujalowski W., Klonowska M. M. Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs. Biochemistry. 32:1993;5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 7
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole S. T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S. V. et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 393:1998;537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6    Gordon, S.V.7
  • 8
    • 0032482446 scopus 로고    scopus 로고
    • Formation of RuvABC-Holliday junction complexes in vitro
    • Davies A. A., West S. C. Formation of RuvABC-Holliday junction complexes in vitro. Curr. Biol. 8:1998;725-727.
    • (1998) Curr. Biol. , vol.8 , pp. 725-727
    • Davies, A.A.1    West, S.C.2
  • 9
    • 0024270328 scopus 로고
    • Site-directed alterations in the ATP-binding domain of Rho protein affect its activities as a termination factor
    • Dombroski A. J., Brennan C. A., Spear P., Platt T. Site-directed alterations in the ATP-binding domain of Rho protein affect its activities as a termination factor. J. Biol. Chem. 263:1988;18802-18809.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18802-18809
    • Dombroski, A.J.1    Brennan, C.A.2    Spear, P.3    Platt, T.4
  • 10
    • 0030586054 scopus 로고    scopus 로고
    • Homomorphous hexameric helicases: Tales from the ring cycle
    • Egelman E. H. Homomorphous hexameric helicases: tales from the ring cycle. Structure. 4:1996;759-762.
    • (1996) Structure , vol.4 , pp. 759-762
    • Egelman, E.H.1
  • 11
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase- primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman E. H., Yu X., Wild R., Hingorani M. M., Patel S. S. Bacteriophage T7 helicase- primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc. Natl Acad. Sci. USA. 92:1995;3869-3873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 12
    • 0030727120 scopus 로고    scopus 로고
    • In vitro reconstitution of the late steps of genetic recombination in E. coli
    • Eggleston A. K., Mitchell A. H., West S. C. In vitro reconstitution of the late steps of genetic recombination in E. coli. Cell. 89:1997;607-617.
    • (1997) Cell , vol.89 , pp. 607-617
    • Eggleston, A.K.1    Mitchell, A.H.2    West, S.C.3
  • 14
    • 0033548196 scopus 로고    scopus 로고
    • Biochemical and electron microscopic image analysis of the hexameric E1 helicase
    • Fouts E. T., Yu X., Egelman E. H., Botchan M. R. Biochemical and electron microscopic image analysis of the hexameric E1 helicase. J. Biol. Chem. 274:1999;4447-4458.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4447-4458
    • Fouts, E.T.1    Yu, X.2    Egelman, E.H.3    Botchan, M.R.4
  • 16
    • 0027049248 scopus 로고
    • Functional interactions of ligand cofactors with Escherichia coli transcription termination factor Rho. I. Binding of ATP
    • Geiselmann J., von Hippel P. H. Functional interactions of ligand cofactors with Escherichia coli transcription termination factor Rho. I. Binding of ATP. Protein Sci. 1:1992;850-860.
    • (1992) Protein Sci. , vol.1 , pp. 850-860
    • Geiselmann, J.1    Von Hippel, P.H.2
  • 17
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya A. E., Koonin E. V. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3:1993;419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 18
    • 0031054522 scopus 로고    scopus 로고
    • Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding
    • Graves-Woodward K. L., Gottlieb J., Challberg M. D., Weller S. K. Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding. J. Biol. Chem. 272:1997;4623-4630.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4623-4630
    • Graves-Woodward, K.L.1    Gottlieb, J.2    Challberg, M.D.3    Weller, S.K.4
  • 19
    • 0029079703 scopus 로고
    • Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase
    • Gross C. H., Shuman S. Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase. J. Virol. 69:1995;4727-4736.
    • (1995) J. Virol. , vol.69 , pp. 4727-4736
    • Gross, C.H.1    Shuman, S.2
  • 20
    • 0030670510 scopus 로고    scopus 로고
    • A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding
    • Hacker K. J., Johnson K. A. A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding. Biochemistry. 36:1997;14080-14087.
    • (1997) Biochemistry , vol.36 , pp. 14080-14087
    • Hacker, K.J.1    Johnson, K.A.2
  • 23
    • 0030045742 scopus 로고    scopus 로고
    • Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases
    • Hingorani M. M., Patel S. S. Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases. Biochemistry. 35:1996;2218-2228.
    • (1996) Biochemistry , vol.35 , pp. 2218-2228
    • Hingorani, M.M.1    Patel, S.S.2
  • 25
    • 0030571508 scopus 로고    scopus 로고
    • Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and ruvC, involved in processing of homologous recombination intermediates
    • Hishida T., Iwasaki H., Ishioka K., Shinagawa H. Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and ruvC, involved in processing of homologous recombination intermediates. Gene. 182:1996;63-70.
    • (1996) Gene , vol.182 , pp. 63-70
    • Hishida, T.1    Iwasaki, H.2    Ishioka, K.3    Shinagawa, H.4
  • 26
    • 0024447720 scopus 로고
    • Overproduction, purification, and ATPase activity of the Escherichia coli RuvB protein involved in DNA repair
    • Iwasaki H., Shiba T., Makino K., Nakata A., Shinagawa H. Overproduction, purification, and ATPase activity of the Escherichia coli RuvB protein involved in DNA repair. J. Bacteriol. 171:1989a;5276-5280.
    • (1989) J. Bacteriol. , vol.171 , pp. 5276-5280
    • Iwasaki, H.1    Shiba, T.2    Makino, K.3    Nakata, A.4    Shinagawa, H.5
  • 27
    • 0024436511 scopus 로고
    • Involvement in DNA repair of the ruvA gene of Escherichia coli
    • Iwasaki H., Shiba T., Nakata A., Shinagawa H. Involvement in DNA repair of the ruvA gene of Escherichia coli. Mol. Gen. Genet. 219:1989b;328-331.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 328-331
    • Iwasaki, H.1    Shiba, T.2    Nakata, A.3    Shinagawa, H.4
  • 28
    • 0026482604 scopus 로고
    • Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration
    • Iwasaki H., Takahagi M., Nakata A., Shinagawa H. Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration. Genes Dev. 6:1992;2214-2220.
    • (1992) Genes Dev. , vol.6 , pp. 2214-2220
    • Iwasaki, H.1    Takahagi, M.2    Nakata, A.3    Shinagawa, H.4
  • 29
    • 0028067935 scopus 로고
    • RuvA and RuvB proteins facilitate the bypass of heterologous DNA insertions during RecA protein-mediated DNA strand exchange
    • Iype L. E., Wood E. A., Inman R. B., Cox M. M. RuvA and RuvB proteins facilitate the bypass of heterologous DNA insertions during RecA protein-mediated DNA strand exchange. J. Biol. Chem. 269:1994;24967-24978.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24967-24978
    • Iype, L.E.1    Wood, E.A.2    Inman, R.B.3    Cox, M.M.4
  • 30
    • 0030747747 scopus 로고    scopus 로고
    • Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with a replication fork
    • Jezewska M. J., Rajendran S., Bujalowski W. Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with a replication fork. Biochemistry. 36:1997;10320-10326.
    • (1997) Biochemistry , vol.36 , pp. 10320-10326
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 31
    • 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. Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 273:1998;9058-9069.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 32
    • 0028136544 scopus 로고
    • Mutations in the NTP-binding motif of minute virus of mice (MVM) NS-1 protein uncouple ATPase and DNA helicase functions
    • Jindal H. K., Yong C. B., Wilson G. M., Tam P., Astell C. R. Mutations in the NTP-binding motif of minute virus of mice (MVM) NS-1 protein uncouple ATPase and DNA helicase functions. J. Biol. Chem. 269:1994;3283-3289.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3283-3289
    • Jindal, H.K.1    Yong, C.B.2    Wilson, G.M.3    Tam, P.4    Astell, C.R.5
  • 33
    • 0029655167 scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64 % to 92 % of the genome
    • Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64 % to 92 % of the genome. DNA Res. 2:1995;153-166.
    • (1995) DNA Res. , vol.2 , pp. 153-166
    • Kaneko, T.1    Tanaka, A.2    Sato, S.3    Kotani, H.4    Sazuka, T.5    Miyajima, N.6    Sugiura, M.7    Tabata, S.8
  • 34
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman T. M., Bjornson K. P. Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65:1996;169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 35
    • 0024814206 scopus 로고
    • Peptide sequencing and site-directed mutagenesis identify tyrosine-319 as the active site tyrosine of Escherichia coli DNA topoisomerase I
    • Lynn R. M., Wang J. C. Peptide sequencing and site-directed mutagenesis identify tyrosine-319 as the active site tyrosine of Escherichia coli DNA topoisomerase I. Proteins: Struct. Funct. Genet. 6:1989;231-239.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 231-239
    • Lynn, R.M.1    Wang, J.C.2
  • 36
    • 0029154926 scopus 로고
    • RuvB protein-mediated ATP hydrolysis: Functional asymmetry in the RuvB hexamer
    • Marrione P. E., Cox M. M. RuvB protein-mediated ATP hydrolysis: functional asymmetry in the RuvB hexamer. Biochemistry. 34:1995;9809-9818.
    • (1995) Biochemistry , vol.34 , pp. 9809-9818
    • Marrione, P.E.1    Cox, M.M.2
  • 37
    • 0031554722 scopus 로고    scopus 로고
    • D113N: A mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities
    • D113N: a mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities. J. Mol. Biol. 271:1997;704-717.
    • (1997) J. Mol. Biol. , vol.271 , pp. 704-717
    • Mézard, C.1    Davies, A.A.2    Stasiak, A.3    West, S.C.4
  • 39
    • 0029783042 scopus 로고    scopus 로고
    • Role of RuvA in branch migration reactions catalyzed by the RuvA and RuvB proteins of Escherichia coli
    • Mitchell A. H., West S. C. Role of RuvA in branch migration reactions catalyzed by the RuvA and RuvB proteins of Escherichia coli. J. Biol. Chem. 271:1996;19497-19502.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19497-19502
    • Mitchell, A.H.1    West, S.C.2
  • 40
    • 0027184479 scopus 로고
    • Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins: II. Interaction of RuvB with DNA
    • Müller B., Tsaneva I. R., West S. C. Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins: II. Interaction of RuvB with DNA. J. Biol. Chem. 268:1993;17185-17189.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17185-17189
    • Müller, B.1    Tsaneva, I.R.2    West, S.C.3
  • 41
    • 0015954847 scopus 로고
    • Isolation and characterization of an Escherichia coli ruv mutant which forms non-septate filaments after low doses of ultraviolet light irradiation
    • Otsuji N., Iyehara H., Hideshima Y. Isolation and characterization of an Escherichia coli ruv mutant which forms non-septate filaments after low doses of ultraviolet light irradiation. J. Bacteriol. 117:1974;337-344.
    • (1974) J. Bacteriol. , vol.117 , pp. 337-344
    • Otsuji, N.1    Iyehara, H.2    Hideshima, Y.3
  • 42
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai E. F., Krengel U., Petsko G. A., Goody R. S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:1990;2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 43
    • 0027261464 scopus 로고
    • Formation of a RuvAB-Holliday junction complex in vitro
    • Parsons C. A., West S. C. Formation of a RuvAB-Holliday junction complex in vitro. J. Mol. Biol. 232:1993;397-405.
    • (1993) J. Mol. Biol. , vol.232 , pp. 397-405
    • Parsons, C.A.1    West, S.C.2
  • 44
    • 0026741832 scopus 로고
    • Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
    • Parsons C. A., Tsaneva I., Lloyd R. G., West S. C. Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions. Proc. Natl Acad. Sci. USA. 89:1992;5452-5456.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5452-5456
    • Parsons, C.A.1    Tsaneva, I.2    Lloyd, R.G.3    West, S.C.4
  • 45
    • 0028968305 scopus 로고
    • Structure of a multisubunit complex that promotes DNA branch migration
    • Parsons C. A., Stasiak A., Bennett R. J., West S. C. Structure of a multisubunit complex that promotes DNA branch migration. Nature. 374:1995a;375-378.
    • (1995) Nature , vol.374 , pp. 375-378
    • Parsons, C.A.1    Stasiak, A.2    Bennett, R.J.3    West, S.C.4
  • 46
    • 0028788048 scopus 로고
    • The E. coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB
    • Parsons C. A., Stasiak A., West S. C. The E. coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB. EMBO J. 14:1995b;5736-5744.
    • (1995) EMBO J. , vol.14 , pp. 5736-5744
    • Parsons, C.A.1    Stasiak, A.2    West, S.C.3
  • 47
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause A., Sonenberg N. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11:1992;2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 48
    • 0029588669 scopus 로고
    • A mutation in the ATP binding domain of Rho alters its RNA binding properties and uncouples ATP hydrolysis from helicase activity
    • Pereira S., Platt T. A mutation in the ATP binding domain of Rho alters its RNA binding properties and uncouples ATP hydrolysis from helicase activity. J. Biol. Chem. 270:1995;30401-30407.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30401-30407
    • Pereira, S.1    Platt, T.2
  • 50
    • 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. Stoichiometry and DNA unwinding by the bacteriophage T4 41:59 helicase. J. Biol. Chem. 271:1996;14074-14081.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14074-14081
    • Raney, K.D.1    Carver, T.E.2    Benkovic, S.J.3
  • 52
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin M. C., Stamford N. P. J., Dammerova N., Dixon N. E., Carazo J. M. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J. Struct. Biol. 114:1995;167-176.
    • (1995) J. Struct. Biol. , vol.114 , pp. 167-176
    • San Martin, M.C.1    Stamford, N.P.J.2    Dammerova, N.3    Dixon, N.E.4    Carazo, J.M.5
  • 54
    • 0028272139 scopus 로고
    • Activation of RuvC Holliday junction resolvase in vitro
    • Shah R., Bennett R. J., West S. C. Activation of RuvC Holliday junction resolvase in vitro. Nucl. Acids Res. 22:1994;2490-2497.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 2490-2497
    • Shah, R.1    Bennett, R.J.2    West, S.C.3
  • 55
    • 0025332556 scopus 로고
    • Molecular and functional analysis of the ruv region of Escherichia coli K-12 reveals three genes involved in DNA repair and recombination
    • Sharples G. J., Benson F. E., Illing G. T., Lloyd R. G. Molecular and functional analysis of the ruv region of Escherichia coli K-12 reveals three genes involved in DNA repair and recombination. Mol. Gen. Genet. 221:1990;219-226.
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 219-226
    • Sharples, G.J.1    Benson, F.E.2    Illing, G.T.3    Lloyd, R.G.4
  • 58
    • 0023770755 scopus 로고
    • Escherichia coli transcription termination protein Rho has three hydrolytic sites for ATP
    • Stitt B. L. Escherichia coli transcription termination protein Rho has three hydrolytic sites for ATP. J. Biol. Chem. 263:1988;11130-11137.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11130-11137
    • Stitt, B.L.1
  • 59
    • 0026584599 scopus 로고
    • Structure of the RecA protein-ADP complex
    • Story R. M., Steitz T. A. Structure of the RecA protein-ADP complex. Nature. 355:1992;374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 62
    • 0029981226 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of ruvB and characterization of RuvB proteins from two distantly related thermophilic eubacteria
    • Tong J., Wetmur J. G. Cloning, sequencing, and expression of ruvB and characterization of RuvB proteins from two distantly related thermophilic eubacteria. J. Bacteriol. 178:1996;2695-2700.
    • (1996) J. Bacteriol. , vol.178 , pp. 2695-2700
    • Tong, J.1    Wetmur, J.G.2
  • 63
    • 0026444104 scopus 로고
    • Purification and properties of the RuvA and RuvB proteins of Escherichia coli
    • Tsaneva I. R., Illing G. T., Lloyd R. G., West S. C. Purification and properties of the RuvA and RuvB proteins of Escherichia coli. Mol. Gen. Genet. 235:1992a;1-10.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 1-10
    • Tsaneva, I.R.1    Illing, G.T.2    Lloyd, R.G.3    West, S.C.4
  • 64
    • 0026633047 scopus 로고
    • ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli
    • Tsaneva I. R., Müller B., West S. C. ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli. Cell. 69:1992b;1171-1180.
    • (1992) Cell , vol.69 , pp. 1171-1180
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 65
    • 0027476446 scopus 로고
    • RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
    • Tsaneva I. R., Müller B., West S. C. RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc. Natl Acad. Sci. USA. 90:1993;1315-1319.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1315-1319
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 66
    • 0032509147 scopus 로고    scopus 로고
    • Visualisation of human Rad52 protein and its complexes with hRad51 and DNA
    • Van Dyck E., Hajibagheri N. M. A., Stasiak A., West S. C. Visualisation of human Rad52 protein and its complexes with hRad51 and DNA. J. Mol. Biol. 284:1998;1027-1038.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1027-1038
    • Van Dyck, E.1    Hajibagheri, N.M.A.2    Stasiak, A.3    West, S.C.4
  • 67
    • 0032536901 scopus 로고    scopus 로고
    • Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli
    • van Gool A. J., Shah R., Mézard C., West S. C. Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli. EMBO J. 17:1998;1838-1845.
    • (1998) EMBO J. , vol.17 , pp. 1838-1845
    • Van Gool, A.J.1    Shah, R.2    Mézard, C.3    West, S.C.4
  • 68
    • 0033565930 scopus 로고    scopus 로고
    • Assembly of the Escherichia coli RuvABC resolvasome directs the orientation of Holliday junction resolution
    • van Gool A. J., Hajibagheri N. M. A., Stasiak A., West S. C. Assembly of the Escherichia coli RuvABC resolvasome directs the orientation of Holliday junction resolution. Genes Dev. 13:1999;1861-1870.
    • (1999) Genes Dev. , vol.13 , pp. 1861-1870
    • Van Gool, A.J.1    Hajibagheri, N.M.A.2    Stasiak, A.3    West, S.C.4
  • 69
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar S. S., Soultanas P., Dillingham M. S., Subramanya H. S., Wigley D. B. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell. 97:1999;75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 70
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- And β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 71
    • 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. 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. 271:1996;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
  • 72
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • West S. C. Processing of recombination intermediates by the RuvABC proteins. Annu. Rev. Genet. 31:1997;213-244.
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 73
    • 0028005448 scopus 로고
    • Branch migration of Holliday junctions: Identification of RecG protein as a junction specific DNA helicase
    • Whitby M. C., Vincent S. D., Lloyd R. G. Branch migration of Holliday junctions: identification of RecG protein as a junction specific DNA helicase. EMBO J. 13:1994;5220-5228.
    • (1994) EMBO J. , vol.13 , pp. 5220-5228
    • Whitby, M.C.1    Vincent, S.D.2    Lloyd, R.G.3
  • 74
    • 0030596061 scopus 로고    scopus 로고
    • Interactions between RuvA and RuvC at Holliday junctions: Inhibition of junction cleavage and formation of a RuvA-RuvC-DNA complex
    • Whitby M. C., Bolt E. L., Chan S. N., Lloyd R. G. Interactions between RuvA and RuvC at Holliday junctions: inhibition of junction cleavage and formation of a RuvA-RuvC-DNA complex. J. Mol. Biol. 264:1996;878-890.
    • (1996) J. Mol. Biol. , vol.264 , pp. 878-890
    • Whitby, M.C.1    Bolt, E.L.2    Chan, S.N.3    Lloyd, R.G.4
  • 75
    • 0031581811 scopus 로고    scopus 로고
    • Structure and subunit composition of the RuvAB-Holliday junction complex
    • Yu X., West S. C., Egelman E. H. Structure and subunit composition of the RuvAB-Holliday junction complex. J. Mol. Biol. 266:1997;217-222.
    • (1997) J. Mol. Biol. , vol.266 , pp. 217-222
    • Yu, X.1    West, S.C.2    Egelman, E.H.3
  • 76
    • 0032575757 scopus 로고    scopus 로고
    • Coordinated actions of RuvABC in Holliday junction processing
    • Zerbib D., Mézard C., George H., West S. C. Coordinated actions of RuvABC in Holliday junction processing. J. Mol. Biol. 281:1998;621-630.
    • (1998) J. Mol. Biol. , vol.281 , pp. 621-630
    • Zerbib, D.1    Mézard, C.2    George, H.3    West, S.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.