메뉴 건너뛰기




Volumn 4, Issue 1, 2005, Pages 23-31

Conservation of RecG activity from pathogens to hyperthermophiles

Author keywords

DNA repair; Genomic instability; Holliday junction; Recombination

Indexed keywords

ADENOSINE TRIPHOSPHATE; ESCHERICHIA COLI PROTEIN; HELICASE; PROTEIN DERIVATIVE; RECG HELICASE; UNCLASSIFIED DRUG;

EID: 7944236522     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2004.07.008     Document Type: Article
Times cited : (14)

References (49)
  • 1
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialization in superfamily 1 and 2 helicases
    • M.R. Singleton, and D.B. Wigley Modularity and specialization in superfamily 1 and 2 helicases J. Bacteriol. 184 2002 1819 1826
    • (2002) J. Bacteriol. , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 2
    • 0032873606 scopus 로고    scopus 로고
    • Holliday junction processing in bacteria: Insights from the evolutionary conservation of RuvABC, RecG, and RusA
    • G.J. Sharples, S.M. Ingleston, and R.G. Lloyd Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA J. Bacteriol. 181 1999 5543 5550
    • (1999) J. Bacteriol. , vol.181 , pp. 5543-5550
    • Sharples, G.J.1    Ingleston, S.M.2    Lloyd, R.G.3
  • 3
    • 0025924538 scopus 로고
    • Genetic analysis of the recG locus of Escherichia coli K-12 and of its role in recombination and DNA repair
    • R.G. Lloyd, and C. Buckman Genetic analysis of the recG locus of Escherichia coli K-12 and of its role in recombination and DNA repair J. Bacteriol. 173 1991 1004 1011
    • (1991) J. Bacteriol. , vol.173 , pp. 1004-1011
    • Lloyd, R.G.1    Buckman, C.2
  • 5
    • 0030852247 scopus 로고    scopus 로고
    • The DNA replication protein PriA and the recombination protein RecG bind D-loops
    • P. McGlynn, A.A. Al-Deib, J. Liu, K.J. Marians, and R.G. Lloyd The DNA replication protein PriA and the recombination protein RecG bind D-loops J. Mol. Biol. 270 1997 212 221
    • (1997) J. Mol. Biol. , vol.270 , pp. 212-221
    • McGlynn, P.1    Al-Deib, A.A.2    Liu, J.3    Marians, K.J.4    Lloyd, R.G.5
  • 6
    • 0033178272 scopus 로고    scopus 로고
    • RecG helicase activity at three- and four-strand DNA structures
    • P. McGlynn, and R.G. Lloyd RecG helicase activity at three- and four-strand DNA structures Nucleic Acids Res. 27 1999 3049 3056
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3049-3056
    • McGlynn, P.1    Lloyd, R.G.2
  • 7
    • 0027397630 scopus 로고
    • Dissociation of synthetic Holliday junctions by E. coli RecG protein
    • R.G. Lloyd, and G.J. Sharples Dissociation of synthetic Holliday junctions by E. coli RecG protein EMBO J. 12 1993 17 22
    • (1993) EMBO J. , vol.12 , pp. 17-22
    • Lloyd, R.G.1    Sharples, G.J.2
  • 8
    • 0032584598 scopus 로고    scopus 로고
    • Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli
    • M.C. Whitby, and R.G. Lloyd Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli J. Biol. Chem. 273 1998 19729 19739
    • (1998) J. Biol. Chem. , vol.273 , pp. 19729-19739
    • Whitby, M.C.1    Lloyd, R.G.2
  • 9
    • 0027438781 scopus 로고
    • Reverse branch migration of Holliday junctions by RecG protein: A new mechanism for resolution of intermediates in recombination and DNA repair
    • M.C. Whitby, L. Ryder, and R.G. Lloyd Reverse branch migration of Holliday junctions by RecG protein: a new mechanism for resolution of intermediates in recombination and DNA repair Cell 75 1993 341 350
    • (1993) Cell , vol.75 , pp. 341-350
    • Whitby, M.C.1    Ryder, L.2    Lloyd, R.G.3
  • 10
    • 0028005448 scopus 로고
    • Branch migration of Holliday junctions: Identification of RecG protein as a junction specific DNA helicase
    • M.C. Whitby, S. Vincent, and R.G. Lloyd 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.2    Lloyd, R.G.3
  • 11
    • 0029072794 scopus 로고
    • Branch migration of three-strand recombination intermediates by RecG, a possible pathway for securing exchanges initiated by 3′-tailed duplex DNA
    • M.C. Whitby, and R.G. Lloyd Branch migration of three-strand recombination intermediates by RecG, a possible pathway for securing exchanges initiated by 3′-tailed duplex DNA EMBO J. 14 1995 3302 3310
    • (1995) EMBO J. , vol.14 , pp. 3302-3310
    • Whitby, M.C.1    Lloyd, R.G.2
  • 12
    • 0036683338 scopus 로고    scopus 로고
    • Genome stability and the processing of damaged replication forks by RecG
    • P. McGlynn, and R.G. Lloyd Genome stability and the processing of damaged replication forks by RecG Trends Genet. 18 2002 413 419
    • (2002) Trends Genet. , vol.18 , pp. 413-419
    • McGlynn, P.1    Lloyd, R.G.2
  • 13
    • 0034737294 scopus 로고    scopus 로고
    • Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression
    • P. McGlynn, and R.G. Lloyd Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression Cell 101 2000 35 45
    • (2000) Cell , vol.101 , pp. 35-45
    • McGlynn, P.1    Lloyd, R.G.2
  • 14
    • 0035902591 scopus 로고    scopus 로고
    • Rescue of stalled replication forks by RecG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation
    • P. McGlynn, and R.G. Lloyd Rescue of stalled replication forks by RecG: simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation Proc. Natl. Acad. Sci. U.S.A. 98 2001 8227 8234
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8227-8234
    • McGlynn, P.1    Lloyd, R.G.2
  • 15
    • 0035902573 scopus 로고    scopus 로고
    • Formation of Holliday junctions by regression of stalled replication forks: RecG stimulates fork regression even when the DNA is negatively supercoiled
    • P. McGlynn, R.G. Lloyd, and K.J. Marians Formation of Holliday junctions by regression of stalled replication forks: RecG stimulates fork regression even when the DNA is negatively supercoiled Proc. Natl. Acad. Sci. U.S.A. 98 2001 8235 8240
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8235-8240
    • McGlynn, P.1    Lloyd, R.G.2    Marians, K.J.3
  • 16
    • 0036844340 scopus 로고    scopus 로고
    • Recombinational repair and restart of damaged replication forks
    • P. McGlynn, and R.G. Lloyd Recombinational repair and restart of damaged replication forks Nat. Rev. Mol. Cell Biol. 3 2002 859 870
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 859-870
    • McGlynn, P.1    Lloyd, R.G.2
  • 17
    • 0035653448 scopus 로고    scopus 로고
    • Requirement of DNA repair mechanisms for survival of Burkholderia cepacia G4 upon degradation of trichloroethylene
    • C.M. Yeager, P.J. Bottomley, and D.J. Arp Requirement of DNA repair mechanisms for survival of Burkholderia cepacia G4 upon degradation of trichloroethylene Appl. Environ. Microbiol. 67 2001 5384 5391
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 5384-5391
    • Yeager, C.M.1    Bottomley, P.J.2    Arp, D.J.3
  • 18
    • 0033874090 scopus 로고    scopus 로고
    • Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF
    • U.A. Ochsner, M.L. Vasil, E. Alsabbagh, K. Parvatiyar, and D.J. Hassett Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF J. Bacteriol. 182 2000 4533 4544
    • (2000) J. Bacteriol. , vol.182 , pp. 4533-4544
    • Ochsner, U.A.1    Vasil, M.L.2    Alsabbagh, E.3    Parvatiyar, K.4    Hassett, D.J.5
  • 19
    • 0030741937 scopus 로고    scopus 로고
    • Cloning and sequencing of a novel gene (recG) that affects the quinolone susceptibility of Staphylococcus aureus
    • T. Niga, H. Yoshida, H. Hattori, S. Nakamura, and H. Ito Cloning and sequencing of a novel gene (recG) that affects the quinolone susceptibility of Staphylococcus aureus Antimicrob. Agents Chemother. 41 1997 1770 1774
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1770-1774
    • Niga, T.1    Yoshida, H.2    Hattori, H.3    Nakamura, S.4    Ito, H.5
  • 20
    • 0029981318 scopus 로고    scopus 로고
    • The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination
    • B. Martin, G.J. Sharples, O. Humbert, R.G. Lloyd, and J. Claverys The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein involved in DNA repair and in three-strand recombination Mol. Microbiol. 19 1996 1035 1045
    • (1996) Mol. Microbiol. , vol.19 , pp. 1035-1045
    • Martin, B.1    Sharples, G.J.2    Humbert, O.3    Lloyd, R.G.4    Claverys, J.5
  • 21
    • 0037067774 scopus 로고    scopus 로고
    • Effect of the Streptococcus pneumoniae MmsA protein on the RecA protein-promoted three-strand exchange reaction. Implications for the mechanism of transformational recombination
    • M.A. Hedayati, S.E. Steffen, and F.R. Bryant Effect of the Streptococcus pneumoniae MmsA protein on the RecA protein-promoted three-strand exchange reaction. Implications for the mechanism of transformational recombination J. Biol. Chem. 277 2002 24863 24869
    • (2002) J. Biol. Chem. , vol.277 , pp. 24863-24869
    • Hedayati, M.A.1    Steffen, S.E.2    Bryant, F.R.3
  • 22
    • 0036228158 scopus 로고    scopus 로고
    • RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions
    • G.J. Sharples, E.L. Bolt, and R.G. Lloyd RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions Mol. Microbiol. 44 2002 549 559
    • (2002) Mol. Microbiol. , vol.44 , pp. 549-559
    • Sharples, G.J.1    Bolt, E.L.2    Lloyd, R.G.3
  • 25
    • 0029850005 scopus 로고    scopus 로고
    • Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12
    • A.A. Al-Deib, A.A. Mahdi, and R.G. Lloyd Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12 J. Bacteriol. 178 1996 6782 6789
    • (1996) J. Bacteriol. , vol.178 , pp. 6782-6789
    • Al-Deib, A.A.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 26
    • 0030885346 scopus 로고    scopus 로고
    • DNA binding and helicase domains of the Escherichia coli recombination protein RecG
    • A.A. Mahdi, P. McGlynn, S.D. Levett, and R.G. Lloyd DNA binding and helicase domains of the Escherichia coli recombination protein RecG Nucleic Acids Res. 25 1997 3875 3880
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3875-3880
    • Mahdi, A.A.1    McGlynn, P.2    Levett, S.D.3    Lloyd, R.G.4
  • 27
    • 0030582737 scopus 로고    scopus 로고
    • The RecG branch migration protein of Escherichia coli dissociates R-loops
    • S.D. Vincent, A.A. Mahdi, and R.G. Lloyd The RecG branch migration protein of Escherichia coli dissociates R-loops J. Mol. Biol. 264 1996 713 721
    • (1996) J. Mol. Biol. , vol.264 , pp. 713-721
    • Vincent, S.D.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 29
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • J.A. Cuff, and G.J. Barton Application of multiple sequence alignment profiles to improve protein secondary structure prediction Proteins 40 2000 502 511
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 30
    • 0037415719 scopus 로고    scopus 로고
    • A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins
    • A.A. Mahdi, G.S. Briggs, G.J. Sharples, Q. Wen, and R.G. Lloyd A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins EMBO J. 22 2003 724 734
    • (2003) EMBO J. , vol.22 , pp. 724-734
    • Mahdi, A.A.1    Briggs, G.S.2    Sharples, G.J.3    Wen, Q.4    Lloyd, R.G.5
  • 31
    • 0030940299 scopus 로고    scopus 로고
    • Sequence-specificity and biochemical characterization of the RusA Holliday junction resolvase of Escherichia coli
    • S.N. Chan, L. Harris, E.L. Bolt, M.C. Whitby, and R.G. Lloyd Sequence-specificity and biochemical characterization of the RusA Holliday junction resolvase of Escherichia coli J. Biol. Chem. 272 1997 14873 14882
    • (1997) J. Biol. Chem. , vol.272 , pp. 14873-14882
    • Chan, S.N.1    Harris, L.2    Bolt, E.L.3    Whitby, M.C.4    Lloyd, R.G.5
  • 32
    • 0037121936 scopus 로고    scopus 로고
    • Modulation of DNA repair by mutations flanking the DNA channel through RNA polymerase
    • B.W. Trautinger, and R.G. Lloyd Modulation of DNA repair by mutations flanking the DNA channel through RNA polymerase EMBO J. 21 2002 6944 6953
    • (2002) EMBO J. , vol.21 , pp. 6944-6953
    • Trautinger, B.W.1    Lloyd, R.G.2
  • 33
    • 0033600866 scopus 로고    scopus 로고
    • Functional and biochemical characterization of a recombinant 3-Deoxy-d-manno-octulosonic acid 8-phosphate synthase from the hyperthermophilic bacterium Aquifex aeolicus
    • H.S. Duewel, G.Y. Sheflyan, and R.W. Woodard Functional and biochemical characterization of a recombinant 3-Deoxy-d-manno-octulosonic acid 8-phosphate synthase from the hyperthermophilic bacterium Aquifex aeolicus Biochem. Biophys. Res. Commun. 263 1999 346 351
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 346-351
    • Duewel, H.S.1    Sheflyan, G.Y.2    Woodard, R.W.3
  • 35
    • 0031028107 scopus 로고    scopus 로고
    • ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase
    • A. Fukuoh, H. Iwasaki, K. Ishioka, and H. Shinagawa ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase EMBO J. 16 1997 203 209
    • (1997) EMBO J. , vol.16 , pp. 203-209
    • Fukuoh, A.1    Iwasaki, H.2    Ishioka, K.3    Shinagawa, H.4
  • 37
    • 0034659679 scopus 로고    scopus 로고
    • Characterisation of the catalytically active form of RecG helicase
    • P. McGlynn, A.A. Mahdi, and R.G. Lloyd Characterisation of the catalytically active form of RecG helicase Nucleic Acids Res. 28 2000 2324 2332
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2324-2332
    • McGlynn, P.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 38
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • M.R. Singleton, S. Scaife, and D.B. Wigley Structural analysis of DNA replication fork reversal by RecG Cell 107 2001 79 89
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 39
    • 0016155830 scopus 로고
    • Role of a deoxyribonuclease in the genetic transformation of Diplococcus pneumoniae
    • S. Lacks, B. Greenberg, and M. Neuberger Role of a deoxyribonuclease in the genetic transformation of Diplococcus pneumoniae Proc. Natl. Acad. Sci. U.S.A. 71 1974 2305 2309
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 2305-2309
    • Lacks, S.1    Greenberg, B.2    Neuberger, M.3
  • 40
    • 0025315488 scopus 로고
    • Genetic and structural characterisation of EndA, a membrane-bound nuclease required for transformation of Streptococcus pneumoniae
    • A. Puyet, B. Greenberg, and S.A. Lacks Genetic and structural characterisation of EndA, a membrane-bound nuclease required for transformation of Streptococcus pneumoniae J. Mol. Biol. 213 1990 727 738
    • (1990) J. Mol. Biol. , vol.213 , pp. 727-738
    • Puyet, A.1    Greenberg, B.2    Lacks, S.A.3
  • 41
    • 0035117855 scopus 로고    scopus 로고
    • The X philes: Structure-specific endonucleases that resolve Holliday junctions
    • G.J. Sharples The X philes: structure-specific endonucleases that resolve Holliday junctions Mol. Microbiol. 39 2001 823 834
    • (2001) Mol. Microbiol. , vol.39 , pp. 823-834
    • Sharples, G.J.1
  • 42
    • 0346374827 scopus 로고    scopus 로고
    • Bacillus subtilis RecU protein cleaves Holliday junctions and anneals single-stranded DNA
    • S. Ayora, B. Carrasco, E. Doncel, R. Lurz, and J.C. Alonso Bacillus subtilis RecU protein cleaves Holliday junctions and anneals single-stranded DNA Proc. Natl. Acad. Sci. U.S.A. 101 2004 452 457
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 452-457
    • Ayora, S.1    Carrasco, B.2    Doncel, E.3    Lurz, R.4    Alonso, J.C.5
  • 43
    • 0028468549 scopus 로고
    • Bacterial sporulation: An ATP/ADP switch
    • C. Stephens, M. Singer, and L. Shapiro Bacterial sporulation: an ATP/ADP switch Curr. Biol. 4 1994 630 632
    • (1994) Curr. Biol. , vol.4 , pp. 630-632
    • Stephens, C.1    Singer, M.2    Shapiro, L.3
  • 44
    • 0026009412 scopus 로고
    • Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG
    • R.G. Lloyd Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG J. Bacteriol. 173 1991 5414 5418
    • (1991) J. Bacteriol. , vol.173 , pp. 5414-5418
    • Lloyd, R.G.1
  • 45
    • 0027236687 scopus 로고
    • Resolution of Holliday intermediates in recombination and DNA repair: Indirect suppression of ruvA, ruvB and ruvC mutations
    • T.N. Mandal, A.A. Mahdi, G.J. Sharples, and R.G. Lloyd Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB and ruvC mutations J. Bacteriol. 175 1993 4325 4334
    • (1993) J. Bacteriol. , vol.175 , pp. 4325-4334
    • Mandal, T.N.1    Mahdi, A.A.2    Sharples, G.J.3    Lloyd, R.G.4
  • 46
    • 0036348154 scopus 로고    scopus 로고
    • Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo
    • E.L. Bolt, and R.G. Lloyd Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo Mol. Cell. 10 2002 187 198
    • (2002) Mol. Cell. , vol.10 , pp. 187-198
    • Bolt, E.L.1    Lloyd, R.G.2
  • 47
    • 0029871788 scopus 로고    scopus 로고
    • Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82
    • A.A. Mahdi, G.J. Sharples, T.N. Mandal, and R.G. Lloyd Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82 J. Mol. Biol. 257 1996 561 573
    • (1996) J. Mol. Biol. , vol.257 , pp. 561-573
    • Mahdi, A.A.1    Sharples, G.J.2    Mandal, T.N.3    Lloyd, R.G.4
  • 48
    • 0036384368 scopus 로고    scopus 로고
    • Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization
    • D. Sahoo, P.M. Weers, R.O. Ryan, and V. Narayanaswami Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization J. Mol. Biol. 321 2002 201 214
    • (2002) J. Mol. Biol. , vol.321 , pp. 201-214
    • Sahoo, D.1    Weers, P.M.2    Ryan, R.O.3    Narayanaswami, V.4
  • 49
    • 0037022281 scopus 로고    scopus 로고
    • Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein
    • J. Wang, B.D. Sykes, and R.O. Ryan Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein Proc. Natl. Acad. Sci. U.S.A. 99 2002 1188 1193
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1188-1193
    • Wang, J.1    Sykes, B.D.2    Ryan, R.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.