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Volumn 11, Issue 2, 2007, Pages 277-282

Biochemical evidence of a physical interaction between Sulfolobus solfataricus B-family and Y-family DNA polymerases

Author keywords

Archaea; DNA polymerase; DNA replication; Genome stability; Sulfolobus solfataricus; Translesion synthesis

Indexed keywords

ARCHAEAL PROTEIN; DBH PROTEIN, SULFOLOBUS SOLFATARICUS; DNA DIRECTED DNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 33847255445     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-006-0038-x     Document Type: Article
Times cited : (12)

References (28)
  • 1
    • 33645847242 scopus 로고    scopus 로고
    • Visualization of the interaction between archaeal DNA polymerase and uracil-containing DNA by atomic force microscopy
    • Asami Y, Murakami M, Shimizu M, Pisani FM, Hayata I, Nohmi T (2006) Visualization of the interaction between archaeal DNA polymerase and uracil-containing DNA by atomic force microscopy. Genes Cells 11:3-11
    • (2006) Genes Cells , vol.11 , pp. 3-11
    • Asami, Y.1    Murakami, M.2    Shimizu, M.3    Pisani, F.M.4    Hayata, I.5    Nohmi, T.6
  • 2
    • 1842334927 scopus 로고
    • A general structure for DNA-dependent DNA polymerases
    • Blanco L, Bernad A, Blasco MA, Salas M (1991) A general structure for DNA-dependent DNA polymerases. Gene 108:165
    • (1991) Gene , vol.108 , pp. 165
    • Blanco, L.1    Bernad, A.2    Blasco, M.A.3    Salas, M.4
  • 4
    • 18844434472 scopus 로고    scopus 로고
    • Characterization of an archaeal family 4 uracil DNA glycosylase and its interaction with PCNA and chromatin proteins
    • Dionne I, Bell SD (2005) Characterization of an archaeal family 4 uracil DNA glycosylase and its interaction with PCNA and chromatin proteins. Biochem J 387:859-863
    • (2005) Biochem J , vol.387 , pp. 859-863
    • Dionne, I.1    Bell, S.D.2
  • 5
    • 0036894880 scopus 로고    scopus 로고
    • Structural basis for uracil recognition by archaeal family B DNA polymerases
    • Fogg MJ, Pearl LH, Connolly BA (2002) Structural basis for uracil recognition by archaeal family B DNA polymerases. Nat Struct Biol 9:922-927
    • (2002) Nat Struct Biol , vol.9 , pp. 922-927
    • Fogg, M.J.1    Pearl, L.H.2    Connolly, B.A.3
  • 6
    • 0037205001 scopus 로고    scopus 로고
    • Specialized DNA polymerases, cellular survival, and the genesis of mutations
    • Friedberg EC, Wagner R, Radman M (2002) Specialized DNA polymerases, cellular survival, and the genesis of mutations. Science 296:1627-1630
    • (2002) Science , vol.296 , pp. 1627-1630
    • Friedberg, E.C.1    Wagner, R.2    Radman, M.3
  • 8
    • 0034940811 scopus 로고    scopus 로고
    • Genetic fidelity under harsh conditions: Analysis of spontaneous mutation in the thermoacidophilic archaeon Sulfolobus acidocaldarius
    • Grogan DW, Carver GT, Drake JW (2001) Genetic fidelity under harsh conditions: analysis of spontaneous mutation in the thermoacidophilic archaeon Sulfolobus acidocaldarius. Proc Natl Acad Sci USA 98:7928-7933
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7928-7933
    • Grogan, D.W.1    Carver, G.T.2    Drake, J.W.3
  • 10
    • 0035861667 scopus 로고    scopus 로고
    • Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C
    • Gruz P, Pisani FM, Shimizu M, Yamada M, Hayashi I, Morikawa K, Nohmi T (2001) Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C. J Biol Chem 276:47394-47401
    • (2001) J Biol Chem , vol.276 , pp. 47394-47401
    • Gruz, P.1    Pisani, F.M.2    Shimizu, M.3    Yamada, M.4    Hayashi, I.5    Morikawa, K.6    Nohmi, T.7
  • 13
    • 0029929717 scopus 로고    scopus 로고
    • Archaebacterial DNA polymerases tightly bind uracil-containing DNA
    • Lasken RS, Schuster DM, Rashtchian A (1996) Archaebacterial DNA polymerases tightly bind uracil-containing DNA. J Biol Chem 271:17692-17696
    • (1996) J Biol Chem , vol.271 , pp. 17692-17696
    • Lasken, R.S.1    Schuster, D.M.2    Rashtchian, A.3
  • 14
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T (1993) Instability and decay of the primary structure of DNA. Nature 362:709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 15
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl T, Nyberg B (1974) Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry 13:3405-3410
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 16
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling H, Boudsocq F, Woodgate R, Yang W (2001) Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell 107:91-102
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 17
    • 0346422480 scopus 로고    scopus 로고
    • Modulation of hyperthermophilic DNA polymerase activity by archaeal chromatin proteins
    • Lou H, Duan Z, Huo X, Huang L (2004) Modulation of hyperthermophilic DNA polymerase activity by archaeal chromatin proteins. J Biol Chem 279:127-132
    • (2004) J Biol Chem , vol.279 , pp. 127-132
    • Lou, H.1    Duan, Z.2    Huo, X.3    Huang, L.4
  • 18
    • 33750344433 scopus 로고    scopus 로고
    • Environmental stress and lesion-bypass DNA polymerases
    • Nohmi T (2006) Environmental stress and lesion-bypass DNA polymerases. Annu Rev Microbiol 60:231-253
    • (2006) Annu Rev Microbiol , vol.60 , pp. 231-253
    • Nohmi, T.1
  • 20
    • 0028176299 scopus 로고
    • Evidence that an archaeal alpha-like DNA polymerase has a modular organization of its associated catalytic activities
    • Pisani FM, Rossi M (1994) Evidence that an archaeal alpha-like DNA polymerase has a modular organization of its associated catalytic activities. J Biol Chem 269:7887-7892
    • (1994) J Biol Chem , vol.269 , pp. 7887-7892
    • Pisani, F.M.1    Rossi, M.2
  • 21
    • 0029951380 scopus 로고    scopus 로고
    • Domain organization and DNA-induced conformational changes of an archaeal family B DNA polymerase
    • Pisani FM, Manco G, Carratore V, Rossi M (1996) Domain organization and DNA-induced conformational changes of an archaeal family B DNA polymerase. Biochemistry 35:9158-9166
    • (1996) Biochemistry , vol.35 , pp. 9158-9166
    • Pisani, F.M.1    Manco, G.2    Carratore, V.3    Rossi, M.4
  • 22
    • 0041589201 scopus 로고    scopus 로고
    • Enzymology of base excision repair in the hyperthermophilic archaeon Pyrobaculum aerophilum
    • Sartori AA, Jiricny J (2003) Enzymology of base excision repair in the hyperthermophilic archaeon Pyrobaculum aerophilum. J Biol Chem 278:24563-24576
    • (2003) J Biol Chem , vol.278 , pp. 24563-24576
    • Sartori, A.A.1    Jiricny, J.2
  • 25
    • 0034762679 scopus 로고    scopus 로고
    • Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus
    • Silvian LF, Toth EA, Pham P, Goodman MF, Ellenberger T (2001) Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nat Struct. Biol 8:984-989
    • (2001) Nat Struct. Biol , vol.8 , pp. 984-989
    • Silvian, L.F.1    Toth, E.A.2    Pham, P.3    Goodman, M.F.4    Ellenberger, T.5
  • 26
    • 0035850235 scopus 로고    scopus 로고
    • Translesion synthesis by the UmuC family of DNA polymerases
    • Wang Z (2001) Translesion synthesis by the UmuC family of DNA polymerases. Mutat Res 486:59-70
    • (2001) Mutat Res , vol.486 , pp. 59-70
    • Wang, Z.1
  • 27
    • 0037151021 scopus 로고    scopus 로고
    • Direct interaction between uracil-DNA glycosylase and a proliferating cell nuclear antigen homolog in the crenarchaeon Pyrobaculum aerophilum
    • Yang H, Chiang JH, Fitz-Gibbon S, Lebel M, Sartori AA, Jiricny J, Slupska MM, Miller JH (2002) Direct interaction between uracil-DNA glycosylase and a proliferating cell nuclear antigen homolog in the crenarchaeon Pyrobaculum aerophilum. J Biol Chem 277:22271-22278
    • (2002) J Biol Chem , vol.277 , pp. 22271-22278
    • Yang, H.1    Chiang, J.H.2    Fitz-Gibbon, S.3    Lebel, M.4    Sartori, A.A.5    Jiricny, J.6    Slupska, M.M.7    Miller, J.H.8
  • 28
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • Zhou BL, Pata JD, Steitz TA (2001) Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol Cell 8:427-437
    • (2001) Mol Cell , vol.8 , pp. 427-437
    • Zhou, B.L.1    Pata, J.D.2    Steitz, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.