메뉴 건너뛰기




Volumn 38, Issue 19, 2010, Pages 6433-6446

The RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DNA; DNA BINDING PROTEIN; PROTEIN RDGC; RECA PROTEIN; UNCLASSIFIED DRUG;

EID: 78049397469     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq509     Document Type: Article
Times cited : (6)

References (45)
  • 1
    • 0033053014 scopus 로고    scopus 로고
    • Identification of two new proteins in spermidine nucleoids isolated from Escherichia coli
    • Murphy,L.D., Rosner,J.L., Zimmerman,S.B. and Esposito,D. (1999) Identification of two new proteins in spermidine nucleoids isolated from Escherichia coli. J. Bacteriol., 181, 3842-3844.
    • (1999) J. Bacteriol. , vol.181 , pp. 3842-3844
    • Murphy, L.D.1    Rosner, J.L.2    Zimmerman, S.B.3    Esposito, D.4
  • 2
    • 0030000241 scopus 로고    scopus 로고
    • Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12
    • Ryder,L., Sharples,G.J. and Lloyd,R.G. (1996) Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12. Genetics, 143, 1101-1114.
    • (1996) Genetics , vol.143 , pp. 1101-1114
    • Ryder, L.1    Sharples, G.J.2    Lloyd, R.G.3
  • 3
    • 0037415736 scopus 로고    scopus 로고
    • The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA
    • Moore,T., McGlynn,P., Ngo,H.P., Sharples,G.J. and Lloyd,R.G. (2003) The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA. EMBO J., 22, 735-745.
    • (2003) EMBO J. , vol.22 , pp. 735-745
    • Moore, T.1    McGlynn, P.2    Ngo, H.P.3    Sharples, G.J.4    Lloyd, R.G.5
  • 4
    • 1642500115 scopus 로고    scopus 로고
    • DNA binding by the meningococcal RdgC protein, associated with pilin antigenic variation
    • Moore,T., Sharples,G.J. and Lloyd,R.G. (2004) DNA binding by the meningococcal RdgC protein, associated with pilin antigenic variation. J. Bacteriol., 186, 870-874.
    • (2004) J. Bacteriol. , vol.186 , pp. 870-874
    • Moore, T.1    Sharples, G.J.2    Lloyd, R.G.3
  • 5
    • 33646200335 scopus 로고    scopus 로고
    • Inhibition of RecA protein function by the RdgC protein from Escherichia coli
    • Drees,J.C., Chitteni-Pattu,S., McCaslin,D.R., Inman,R.B. and Cox,M.M. (2006) Inhibition of RecA protein function by the RdgC protein from Escherichia coli. J. Biol. Chem., 281, 4708-4717.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4708-4717
    • Drees, J.C.1    Chitteni-Pattu, S.2    McCaslin, D.R.3    Inman, R.B.4    Cox, M.M.5
  • 6
    • 33847778234 scopus 로고    scopus 로고
    • Motoring along with the bacterial RecA protein
    • Cox,M.M. (2007) Motoring along with the bacterial RecA protein. Nat. Rev. Mol. Cell Biol., 8, 127-138.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 127-138
    • Cox, M.M.1
  • 8
    • 66249147580 scopus 로고    scopus 로고
    • Why do bacteria engage in homologous recombination?
    • Vos,M. (2009) Why do bacteria engage in homologous recombination? Trends Microbiol., 17, 226-232.
    • (2009) Trends Microbiol. , vol.17 , pp. 226-232
    • Vos, M.1
  • 9
    • 64349102519 scopus 로고    scopus 로고
    • Pilin gene variation in Neisseria gonorrhoeae: reassessing the old paradigms
    • Hill,S.A. and Davies,J.K. (2009) Pilin gene variation in Neisseria gonorrhoeae: reassessing the old paradigms. FEMS Microbiol. Rev., 33, 521-530.
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 521-530
    • Hill, S.A.1    Davies, J.K.2
  • 10
    • 1642417542 scopus 로고    scopus 로고
    • Strong positive selection and recombination drive the antigenic variation of the PilE protein of the human pathogen Neisseria meningitidis
    • Andrews,T.D. and Gojobori,T. (2004) Strong positive selection and recombination drive the antigenic variation of the PilE protein of the human pathogen Neisseria meningitidis. Genetics, 166, 25-32.
    • (2004) Genetics , vol.166 , pp. 25-32
    • Andrews, T.D.1    Gojobori, T.2
  • 12
    • 0033968143 scopus 로고    scopus 로고
    • A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation
    • Mehr,I.J., Long,C.D., Serkin,C.D. and Seifert,H.S. (2000) A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation. Genetics, 154, 523-532.
    • (2000) Genetics , vol.154 , pp. 523-532
    • Mehr, I.J.1    Long, C.D.2    Serkin, C.D.3    Seifert, H.S.4
  • 13
    • 0036303443 scopus 로고    scopus 로고
    • Concerted evolution between duplicated genetic elements in Helicobacter pylori
    • Pride,D.T. and Blaser,M.J. (2002) Concerted evolution between duplicated genetic elements in Helicobacter pylori. J. Mol. Biol., 316, 629-642.
    • (2002) J. Mol. Biol. , vol.316 , pp. 629-642
    • Pride, D.T.1    Blaser, M.J.2
  • 14
    • 0030700288 scopus 로고    scopus 로고
    • Molecular mechanisms of Campylobacter fetus surface layer protein expression
    • Dworkin,J. and Blaser,M.J. (1997) Molecular mechanisms of Campylobacter fetus surface layer protein expression. Mol. Microbiol., 26, 433-440.
    • (1997) Mol. Microbiol. , vol.26 , pp. 433-440
    • Dworkin, J.1    Blaser, M.J.2
  • 15
    • 0033754273 scopus 로고    scopus 로고
    • Analysis of the role of recA in phenotypic switching of Pseudomonas tolaasii
    • Sinha,H., Pain,A. and Johnstone,K. (2000) Analysis of the role of recA in phenotypic switching of Pseudomonas tolaasii. J. Bacteriol., 182, 6532-6535.
    • (2000) J. Bacteriol. , vol.182 , pp. 6532-6535
    • Sinha, H.1    Pain, A.2    Johnstone, K.3
  • 16
    • 0022508853 scopus 로고
    • Genes involved in Haemophilus influenzae type b capsule expression are part of an 18-kilobase tandem duplication
    • Hoiseth,S.K., Moxon,E.R. and Silver,R.P. (1986) Genes involved in Haemophilus influenzae type b capsule expression are part of an 18-kilobase tandem duplication. Proc. Natl Acad. Sci. USA, 83, 1106-1110.
    • (1986) Proc. Natl Acad. Sci. USA. , vol.83 , pp. 1106-1110
    • Hoiseth, S.K.1    Moxon, E.R.2    Silver, R.P.3
  • 17
    • 0032723013 scopus 로고    scopus 로고
    • A role for RAD51 and homologous recombination in Trypanosoma brucei antigenic variation
    • McCulloch,R. and Barry,J.D. (1999) A role for RAD51 and homologous recombination in Trypanosoma brucei antigenic variation. Genes Dev., 13, 2875-2888.
    • (1999) Genes Dev. , vol.13 , pp. 2875-2888
    • McCulloch, R.1    Barry, J.D.2
  • 18
    • 33847795537 scopus 로고    scopus 로고
    • Regulation of bacterial RecA protein function
    • Cox,M.M. (2007) Regulation of bacterial RecA protein function. Crit. Rev. Biochem. Mol. Biol., 42, 41-63.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 41-63
    • Cox, M.M.1
  • 19
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West,S.C. (2003) Molecular views of recombination proteins and their control. Nat. Rev. Mol. Cell Biol., 4, 435-445.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 435-445
    • West, S.C.1
  • 20
    • 70349775652 scopus 로고    scopus 로고
    • An SOS inhibitor that binds to free RecA protein: the PsiB protein
    • Petrova,V., Chitteni-Pattu,S., Drees,J.C., Inman,R.B. and Cox,M.M. (2009) An SOS inhibitor that binds to free RecA protein: the PsiB protein. Mol. Cell, 36, 121-130.
    • (2009) Mol. Cell , vol.36 , pp. 121-130
    • Petrova, V.1    Chitteni-Pattu, S.2    Drees, J.C.3    Inman, R.B.4    Cox, M.M.5
  • 21
    • 34250345700 scopus 로고    scopus 로고
    • Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair
    • Briggs,G.S., McEwan,P.A., Yu,J., Moore,T., Emsley,J. and Lloyd,R.G. (2007) Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair. J. Biol. Chem., 282, 12353-12357.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12353-12357
    • Briggs, G.S.1    McEwan, P.A.2    Yu, J.3    Moore, T.4    Emsley, J.5    Lloyd, R.G.6
  • 24
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp
    • Kong,X.P., Onrust,R., O'Donnell,M. and Kuriyan,J. (1992) Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell, 69, 425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 25
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna,T.S., Kong,X.P., Gary,S., Burgers,P.M. and Kuriyan,J. (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell, 79, 1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 26
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey,S., Eliason,W.K. and Steitz,T.A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science, 318, 459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 27
    • 0033519722 scopus 로고    scopus 로고
    • Oligomeric ring structure of the Bloom's syndrome helicase
    • Karow,J.K., Newman,R.H., Freemont,P.S. and Hickson,I.D. (1999) Oligomeric ring structure of the Bloom's syndrome helicase. Curr. Biol., 9, 597-600.
    • (1999) Curr. Biol. , vol.9 , pp. 597-600
    • Karow, J.K.1    Newman, R.H.2    Freemont, P.S.3    Hickson, I.D.4
  • 28
  • 30
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell,S.P. and Dutta,A. (2002) DNA replication in eukaryotic cells. Annu. Rev. Biochem., 71, 333-374.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 31
    • 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. and 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
  • 32
    • 2942538589 scopus 로고    scopus 로고
    • Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity
    • Bernhardt,T.G. and de Boer,P.A. (2004) Screening for synthetic lethal mutants in Escherichia coli and identification of EnvC (YibP) as a periplasmic septal ring factor with murein hydrolase activity. Mol. Microbiol., 52, 1255-1269.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1255-1269
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 33
    • 33746629428 scopus 로고    scopus 로고
    • Rep and PriA helicase activities prevent RecA from provoking unnecessary recombination during replication fork repair
    • Mahdi,A.A., Buckman,C., Harris,L. and Lloyd,R.G. (2006) Rep and PriA helicase activities prevent RecA from provoking unnecessary recombination during replication fork repair. Genes Dev., 20, 2135-2147.
    • (2006) Genes Dev. , vol.20 , pp. 2135-2147
    • Mahdi, A.A.1    Buckman, C.2    Harris, L.3    Lloyd, R.G.4
  • 34
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko,K.A. and Wanner,B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl Acad. Sci. USA, 97, 6640-6645.
    • (2000) Proc. Natl Acad. Sci. USA. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 35
    • 0029850005 scopus 로고    scopus 로고
    • Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12
    • Al-Deib,A.A., Mahdi,A.A. and Lloyd,R.G. (1996) Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12. J. Bacteriol., 178, 6782-6789.
    • (1996) J. Bacteriol. , vol.178 , pp. 6782-6789
    • Al-Deib, A.A.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 36
    • 17144385089 scopus 로고    scopus 로고
    • DNA binding by the substrate specificity (wedge) domain of RecG helicase suggests a role in processivity
    • Briggs,G.S., Mahdi,A.A., Wen,Q. and Lloyd,R.G. (2005) DNA binding by the substrate specificity (wedge) domain of RecG helicase suggests a role in processivity. J. Biol. Chem., 280, 13921-13927.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13921-13927
    • Briggs, G.S.1    Mahdi, A.A.2    Wen, Q.3    Lloyd, R.G.4
  • 39
    • 0347755624 scopus 로고    scopus 로고
    • DSDBASE: a consortium of native and modelled disulphide bonds in proteins
    • Vinayagam,A., Pugalenthi,G., Rajesh,R. and Sowdhamini,R. (2004) DSDBASE: a consortium of native and modelled disulphide bonds in proteins. Nucleic Acids Res., 32, D200-D202.
    • (2004) Nucleic Acids Res. , vol.32
    • Vinayagam, A.1    Pugalenthi, G.2    Rajesh, R.3    Sowdhamini, R.4
  • 40
    • 0029960337 scopus 로고    scopus 로고
    • Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC
    • Sandler,S.J., Samra,H.S. and Clark,A.J. (1996) Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC. Genetics, 143, 5-13.
    • (1996) Genetics , vol.143 , pp. 5-13
    • Sandler, S.J.1    Samra, H.S.2    Clark, A.J.3
  • 41
    • 0032870793 scopus 로고    scopus 로고
    • dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12
    • Sandler,S.J., Marians,K.J., Zavitz,K.H., Coutu,J., Parent,M.A. and Clark,A.J. (1999) dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12. Mol. Microbiol., 34, 91-101.
    • (1999) Mol. Microbiol. , vol.34 , pp. 91-101
    • Sandler, S.J.1    Marians, K.J.2    Zavitz, K.H.3    Coutu, J.4    Parent, M.A.5    Clark, A.J.6
  • 42
    • 0036184234 scopus 로고    scopus 로고
    • Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities
    • Gregg,A.V., McGlynn,P., Jaktaji,R.P. and Lloyd,R.G. (2002) Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. Mol. Cell, 9, 241-251.
    • (2002) Mol. Cell , vol.9 , pp. 241-251
    • Gregg, A.V.1    McGlynn, P.2    Jaktaji, R.P.3    Lloyd, R.G.4
  • 43
    • 0028148226 scopus 로고
    • Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication
    • Masai,H., Asai,T., Kubota,Y., Arai,K. and Kogoma,T. (1994) Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication. EMBO J., 13, 5338-5345.
    • (1994) EMBO J. , vol.13 , pp. 5338-5345
    • Masai, H.1    Asai, T.2    Kubota, Y.3    Arai, K.4    Kogoma, T.5
  • 44
    • 0002739483 scopus 로고    scopus 로고
    • Derivations and genotypes of some mutant derivatives of Escherichia coli K-12
    • Neidardt,F.C.E.A. (ed.) 2nd edn. ASM Press, Washington DC
    • Bachmann,B.J. (1996) Derivations and genotypes of some mutant derivatives of Escherichia coli K-12. In Neidardt,F.C.E.A. (ed.), Escherichia coli and Salmonella Cellular and Molecular Biology, Vol. 2, 2nd edn. ASM Press, Washington DC, pp. 2460-2488.
    • (1996) Escherichia coli and Salmonella Cellular and Molecular Biology , vol.2 , pp. 2460-2488
    • Bachmann, B.J.1
  • 45
    • 0025836589 scopus 로고
    • Inactivation of the Escherichia coli PriA DNA replication protein induces the SOS response
    • Nurse,P., Zavitz,K.H. and Marians,K.J. (1991) Inactivation of the Escherichia coli PriA DNA replication protein induces the SOS response. J. Bacteriol., 173, 6686-6693.
    • (1991) J. Bacteriol. , vol.173 , pp. 6686-6693
    • Nurse, P.1    Zavitz, K.H.2    Marians, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.