메뉴 건너뛰기




Volumn 367, Issue 3, 2008, Pages 523-529

Physical and functional interaction between archaeal single-stranded DNA-binding protein and the 5′-3′ nuclease NurA

Author keywords

Archaea; DNA repair; Homologous recombination; StoNurA; StoSSB; Sulfolobus tokodaii

Indexed keywords

EXONUCLEASE; NURA ENZYME; SINGLE STRANDED DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 38649140681     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.019     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl T., and Wood R.D. Quality control by DNA repair. Science 286 (1999) 1897-1905
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 2
    • 0037115920 scopus 로고    scopus 로고
    • Structure and function of nucleases in DNA repair: shape, grip and blade of the DNA scissors
    • Nishino T., and Morikawa K. Structure and function of nucleases in DNA repair: shape, grip and blade of the DNA scissors. Oncogene 21 (2002) 9022-9032
    • (2002) Oncogene , vol.21 , pp. 9022-9032
    • Nishino, T.1    Morikawa, K.2
  • 3
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae
    • Paques F., and Haber J.E. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63 (1999) 349-404
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 349-404
    • Paques, F.1    Haber, J.E.2
  • 4
    • 0029892791 scopus 로고    scopus 로고
    • DNA repair in eukaryotes
    • Wood R.D. DNA repair in eukaryotes. Annu. Rev. Biochem. 65 (1996) 135-167
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 135-167
    • Wood, R.D.1
  • 6
    • 0036305477 scopus 로고    scopus 로고
    • NurA, a novel 5′-3′ nuclease gene liked to rad50 and mre11 homologs of thermophilic Archaea
    • Constantinesco F., Forterre P., and Elie C. NurA, a novel 5′-3′ nuclease gene liked to rad50 and mre11 homologs of thermophilic Archaea. EMBO Rep. 3 (2002) 537-542
    • (2002) EMBO Rep. , vol.3 , pp. 537-542
    • Constantinesco, F.1    Forterre, P.2    Elie, C.3
  • 7
    • 2442670846 scopus 로고    scopus 로고
    • A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea
    • Constantinesco F., Forterre P., Koonin E.V., Aravind L., and Elie C. A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea. Nucleic Acids Res. 32 (2004) 1439-1447
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1439-1447
    • Constantinesco, F.1    Forterre, P.2    Koonin, E.V.3    Aravind, L.4    Elie, C.5
  • 8
    • 0032567041 scopus 로고    scopus 로고
    • The many interfaces of Mrell
    • Haber J.E. The many interfaces of Mrell. Cell 95 (1998) 583-586
    • (1998) Cell , vol.95 , pp. 583-586
    • Haber, J.E.1
  • 9
    • 0344541947 scopus 로고    scopus 로고
    • Novel homologs of replication protein A in archaea: implications for the evolution of ssDNA-binding proteins
    • Chedin F., Seitz E.M., and Kowalczykowski S.C. Novel homologs of replication protein A in archaea: implications for the evolution of ssDNA-binding proteins. Trends Biochem. Sci. 23 (1998) 273-277
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 273-277
    • Chedin, F.1    Seitz, E.M.2    Kowalczykowski, S.C.3
  • 10
    • 2942597631 scopus 로고    scopus 로고
    • Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage
    • Bernstein D.A., Eggington J.M., Killoran M.P., Misic A.M., Cox M.M., and Keck J.L. Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage. Proc. Natl. Acad. Sci. USA 101 (2004) 8575-8580
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8575-8580
    • Bernstein, D.A.1    Eggington, J.M.2    Killoran, M.P.3    Misic, A.M.4    Cox, M.M.5    Keck, J.L.6
  • 11
    • 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. In vitro and in vivo function of the C-terminus of Escherichia coli single-stranded DNA binding protein. Nucleic Acids Res. 24 (1996) 2706-2711
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2706-2711
    • Curth, U.1    Genschel, J.2    Urbanke, C.3    Greipel, J.4
  • 12
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences
    • Murzin A.G. OB (oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12 (1993) 861-867
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 13
    • 0043163774 scopus 로고    scopus 로고
    • DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery
    • Witte G., Urbanke C., and Curth U. DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery. Nucleic Acid Res. 31 (2003) 4434-4440
    • (2003) Nucleic Acid Res. , vol.31 , pp. 4434-4440
    • Witte, G.1    Urbanke, C.2    Curth, U.3
  • 14
    • 2342516683 scopus 로고    scopus 로고
    • Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase
    • Richard D.J., Bell S.D., and White M.F. Physical and functional interaction of the archaeal single-stranded DNA-binding protein SSB with RNA polymerase. Nucleic Acids Res. 32 (2004) 1065-1074
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1065-1074
    • Richard, D.J.1    Bell, S.D.2    White, M.F.3
  • 15
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E.coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease
    • Genschel J., Curth U., and Urbanke C. Interaction of E.coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease. Biol. Chem. 381 (2000) 183-192
    • (2000) Biol. Chem. , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 16
    • 0035907374 scopus 로고    scopus 로고
    • Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with Uracil DNA Glycosylases
    • Handa P., Acharya N., and Varshney U. Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with Uracil DNA Glycosylases. J. Biol. Chem. 276 (2001) 16992-16997
    • (2001) J. Biol. Chem. , vol.276 , pp. 16992-16997
    • Handa, P.1    Acharya, N.2    Varshney, U.3
  • 17
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in E. coli RecQ DNA helicase function
    • Shereda R.D., Bernstein D.A., and Keck J.L. A central role for SSB in E. coli RecQ DNA helicase function. J. Biol. Chem. 282 (2007) 19247-19258
    • (2007) J. Biol. Chem. , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 18
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman C.J., and Mcglynn P. PriA helicase and SSB interact physically and functionally. Nucleic Acids Res. 32 (2004) 6378-6387
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    Mcglynn, P.2
  • 19
    • 0035865799 scopus 로고    scopus 로고
    • Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus
    • Wadsworth R.I.M., and White M.F. Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus. Nucleic Acids Res. 29 (2001) 914-920
    • (2001) Nucleic Acids Res. , vol.29 , pp. 914-920
    • Wadsworth, R.I.M.1    White, M.F.2
  • 20
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold M.S. Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu. Eev. Biochem. 66 (1997) 61-92
    • (1997) Annu. Eev. Biochem. , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 21
    • 0035793718 scopus 로고    scopus 로고
    • Functional cooperation between topoisomerase I and single strand DNA-binding protein
    • Sikder D., Unniraman S., Bhaduri T., and Nagaraja V. Functional cooperation between topoisomerase I and single strand DNA-binding protein. J. Mol. Biol. 306 (2001) 669-679
    • (2001) J. Mol. Biol. , vol.306 , pp. 669-679
    • Sikder, D.1    Unniraman, S.2    Bhaduri, T.3    Nagaraja, V.4
  • 22
    • 10544227300 scopus 로고    scopus 로고
    • Interaction of Escherichia coli primase with a phage G4ori(c)-E. coli SSB complex
    • Sun W., and Godson G.N. Interaction of Escherichia coli primase with a phage G4ori(c)-E. coli SSB complex. J. Bacteriol. 178 (1996) 6701-6705
    • (1996) J. Bacteriol. , vol.178 , pp. 6701-6705
    • Sun, W.1    Godson, G.N.2
  • 23
    • 0032544662 scopus 로고    scopus 로고
    • SSB protein controls RecBCD enzyme nuclease activity during unwinding: a new role for looped intermediates
    • Anderson D.G., and Kowalczykowski S.C. SSB protein controls RecBCD enzyme nuclease activity during unwinding: a new role for looped intermediates. J. Mol. Biol. 282 (1998) 275-285
    • (1998) J. Mol. Biol. , vol.282 , pp. 275-285
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 24
    • 33749022503 scopus 로고    scopus 로고
    • Methanosarcina acetivorans flap endonuclease 1 activity is inhibited by a cognate single-stranded-DNA-Binding protein
    • Lin Y., Guzman C.E., McKinney M.C., Nair S.K., Ha T., and Cann I.K.O. Methanosarcina acetivorans flap endonuclease 1 activity is inhibited by a cognate single-stranded-DNA-Binding protein. J. Bacteriol. 188 (2006) 6153-6167
    • (2006) J. Bacteriol. , vol.188 , pp. 6153-6167
    • Lin, Y.1    Guzman, C.E.2    McKinney, M.C.3    Nair, S.K.4    Ha, T.5    Cann, I.K.O.6
  • 25
    • 33645225808 scopus 로고    scopus 로고
    • Nucleotide sequence and DNA secondary structure, as well as replication A, modulate the single-stranded abasic endonuclease activity of APE1
    • Fan J., Matsumoto Y., and Wilson D.M. Nucleotide sequence and DNA secondary structure, as well as replication A, modulate the single-stranded abasic endonuclease activity of APE1. J. Biol. Chem. 281 (2006) 3889-3898
    • (2006) J. Biol. Chem. , vol.281 , pp. 3889-3898
    • Fan, J.1    Matsumoto, Y.2    Wilson, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.