메뉴 건너뛰기




Volumn 31, Issue 14, 2003, Pages 4024-4030

Processing of DNA lesions by archaeal DNA polymerases from Sulfolobus solfataricus

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; ARCHAEAL DNA; DEOXYURIDINE TRIPHOSPHATE DERIVATIVE; DNA BASE; DNA POLYMERASE; ENZYME PRECURSOR; HYPOXANTHINE; OLIGONUCLEOTIDE; URACIL; ARCHAEAL PROTEIN; DNA BINDING PROTEIN; DNA DIRECTED DNA POLYMERASE; SINGLE STRANDED DNA;

EID: 0242317687     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg447     Document Type: Article
Times cited : (50)

References (30)
  • 1
    • 0037085734 scopus 로고    scopus 로고
    • Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA
    • Bruskov,V.I., Malakhova,L.V., Masalimov,Z.K. and Chernikov,A.V. (2002) Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA. Nucleic Acids Res., 30, 1354-1363.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1354-1363
    • Bruskov, V.I.1    Malakhova, L.V.2    Masalimov, Z.K.3    Chernikov, A.V.4
  • 2
    • 0037124349 scopus 로고    scopus 로고
    • A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site
    • Sartori,A.A., Fitz-Gibbon,S., Yang,H., Miller,J.H. and Jiricny,J. (2002) A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site. EMBO J., 21, 3182-3191.
    • (2002) EMBO J. , vol.21 , pp. 3182-3191
    • Sartori, A.A.1    Fitz-Gibbon, S.2    Yang, H.3    Miller, J.H.4    Jiricny, J.5
  • 3
    • 0036894880 scopus 로고    scopus 로고
    • Structural basis for uracil recognition by archaeal family B DNA polymerases
    • Fogg,M.J., Pearl,L.H. and Connolly,B.A. (2002) Structural basis for uracil recognition by archaeal family B DNA polymerases. Nature Struct. Biol., 9, 922-927.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 922-927
    • Fogg, M.J.1    Pearl, L.H.2    Connolly, B.A.3
  • 5
    • 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,F.M., Shimizu,M., Yamada,M., Hayashi,I., Morikawa,K. and 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
  • 6
    • 0036682979 scopus 로고    scopus 로고
    • Translesion DNA synthesis in eukaryotes: A one- or two-polymerase affair
    • Prakash,S. and Prakash,L. (2002) Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair. Genes Dev., 16, 1872-1883.
    • (2002) Genes Dev. , vol.16 , pp. 1872-1883
    • Prakash, S.1    Prakash, L.2
  • 8
    • 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. and 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
  • 9
    • 0034762679 scopus 로고    scopus 로고
    • Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus
    • Silvian,L.F., Toth,E.A., Pham,P., Goodman,M.F. and Ellenberger,T. (2001) Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nature Struct. Biol., 8, 984-989.
    • (2001) Nature 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
  • 10
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • Zhou,B.L., Pata,J.D. and Steitz,T.A. (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
  • 11
    • 0037205402 scopus 로고    scopus 로고
    • Low fidelity DNA synthesis by a y family DNA polymerase due to misalignment in the active site
    • Kokoska,R.J., Bebenek,K., Boudsocq,F., Woodgate,R. and Kunkel,T.A. (2002) Low fidelity DNA synthesis by a y family DNA polymerase due to misalignment in the active site. J. Biol. Chem., 277, 19633-19638.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19633-19638
    • Kokoska, R.J.1    Bebenek, K.2    Boudsocq, F.3    Woodgate, R.4    Kunkel, T.A.5
  • 12
    • 0037008746 scopus 로고    scopus 로고
    • The mutational specificity of the Dbh lesion bypass polymerase and its implications
    • Potapova,O., Grindley,N.D. and Joyce,C.M. (2002) The mutational specificity of the Dbh lesion bypass polymerase and its implications. J. Biol. Chem., 277, 28157-28166.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28157-28166
    • Potapova, O.1    Grindley, N.D.2    Joyce, C.M.3
  • 14
    • 0032552893 scopus 로고    scopus 로고
    • Amino acid residues involved in determining the processivity of the 3′-5′ exonuclease activity in a family B DNA polymerase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • Pisani,F.M., De Felice,M. and Rossi,M. (1998) Amino acid residues involved in determining the processivity of the 3′-5′ exonuclease activity in a family B DNA polymerase from the thermoacidophilic archaeon Sulfolobus solfataricus. Biochemistry, 37, 15005-15012.
    • (1998) Biochemistry , vol.37 , pp. 15005-15012
    • Pisani, F.M.1    De Felice, M.2    Rossi, M.3
  • 16
    • 0015275944 scopus 로고
    • Sulfolobus: A new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock,T.D., Brock,K.M., Belly,R.T. and Weiss,R.L. (1972) Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch. Mikrobiol., 84, 54-68.
    • (1972) Arch. Mikrobiol. , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weiss, R.L.4
  • 17
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): An archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic poleta
    • Boudsocq,F., Iwai,S., Hanaoka,F. and Woodgate,R. (2001) Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic poleta. Nucleic Acids Res., 29, 4607-4616.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4607-4616
    • Boudsocq, F.1    Iwai, S.2    Hanaoka, F.3    Woodgate, R.4
  • 20
    • 0029929717 scopus 로고    scopus 로고
    • Archaebacterial DNA polymerases tightly bind uracil-containing DNA
    • Lasken,R.S., Schuster,D.M. and 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
  • 21
    • 0003890119 scopus 로고
    • Prokaryotic DNA polymerases other than E. coli Pol I
    • W.H. Freeman and Co., New York, NY
    • Kornberg,A. and Baker,T.A. (1992) Prokaryotic DNA polymerases other than E. coli Pol I. In DNA Replication. W.H. Freeman and Co., New York, NY, pp. 165-196.
    • (1992) DNA Replication , pp. 165-196
    • Kornberg, A.1    Baker, T.A.2
  • 22
    • 0034789619 scopus 로고    scopus 로고
    • Roles of chromosomal and episomal dinB genes encoding DNA pol IV in targeted and untargeted mutagenesis in Escherichia coli
    • Kim,S.R., Matsui,K., Yamada,M., Gruz,P. and Nohmi,T. (2001) Roles of chromosomal and episomal dinB genes encoding DNA pol IV in targeted and untargeted mutagenesis in Escherichia coli. Mol. Genet. Genomics, 266, 207-215.
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 207-215
    • Kim, S.R.1    Matsui, K.2    Yamada, M.3    Gruz, P.4    Nohmi, T.5
  • 23
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta
    • Haracska,L., Yu,S.L., Johnson,R.E., Prakash,L. and Prakash,S. (2000) Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta. Nature Genet., 25, 458-461.
    • (2000) Nature Genet. , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 26
    • 0034744964 scopus 로고    scopus 로고
    • Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP
    • Persson,R., Cedergren-Zeppezauer,E.S. and Wilson,K.S. (2001) Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP. Curr. Protein Pept. Sci., 2, 287-300.
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 287-300
    • Persson, R.1    Cedergren-Zeppezauer, E.S.2    Wilson, K.S.3
  • 27
    • 0036023039 scopus 로고    scopus 로고
    • Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli
    • Chung,J.H., Park,H.Y., Lee,J.H. and Jang,Y. (2002) Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli. J. Biochem. Mol. Biol., 35, 403-408.
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 403-408
    • Chung, J.H.1    Park, H.Y.2    Lee, J.H.3    Jang, Y.4
  • 28
    • 0035879027 scopus 로고    scopus 로고
    • Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii
    • Chung,J.H., Back,J.H., Park,Y.I. and Han,Y.S. (2001) Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii. Nucleic Acids Res., 29, 3099-3107.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3099-3107
    • Chung, J.H.1    Back, J.H.2    Park, Y.I.3    Han, Y.S.4
  • 29
    • 0035379753 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene
    • Lin,S., McLennan,A.G., Ying,K., Wang,Z., Gu,S., Jin,H., Wu,C., Liu,W., Yuan,Y., Tang,R. et al. (2001) Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J. Biol. Chem., 276, 18695-18701.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18695-18701
    • Lin, S.1    McLennan, A.G.2    Ying, K.3    Wang, Z.4    Gu, S.5    Jin, H.6    Wu, C.7    Liu, W.8    Yuan, Y.9    Tang, R.10
  • 30
    • 0027521347 scopus 로고
    • PCR with degenerate primers containing deoxyinosine fails with Pfu DNA polymerase
    • Knittel,T. and Picard,D. (1993) PCR with degenerate primers containing deoxyinosine fails with Pfu DNA polymerase. PCR Methods Appl., 2, 346-347.
    • (1993) PCR Methods Appl. , vol.2 , pp. 346-347
    • Knittel, T.1    Picard, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.