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Volumn 13, Issue 1, 2003, Pages 23-30

Damage repair DNA polymerases Y

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA POLYMERASE; EXONUCLEASE; ISOENZYME; SINGLE STRANDED DNA BINDING PROTEIN;

EID: 0037310493     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(02)00003-9     Document Type: Review
Times cited : (131)

References (51)
  • 1
    • 0017037398 scopus 로고
    • Ultraviolet mutagenesis and inducible DNA repair in Escherichia coli
    • Witkin E.M. Ultraviolet mutagenesis and inducible DNA repair in Escherichia coli. Bacteriol. Rev. 40:1976;869-907.
    • (1976) Bacteriol. Rev. , vol.40 , pp. 869-907
    • Witkin, E.M.1
  • 2
    • 0020594344 scopus 로고
    • Cloning and characterization of the umu operon responsible for inducible mutagenesis in Escherichia coli
    • Shinagawa H., Kato T., Ise T., Makino K., Nakata A. Cloning and characterization of the umu operon responsible for inducible mutagenesis in Escherichia coli. Gene. 23:1983;167-174.
    • (1983) Gene , vol.23 , pp. 167-174
    • Shinagawa, H.1    Kato, T.2    Ise, T.3    Makino, K.4    Nakata, A.5
  • 3
    • 0020536519 scopus 로고
    • Proteins required for ultraviolet light and chemical mutagenesis. Identification of the products of the umuC locus of Escherichia coli
    • Elledge S.J., Walker G.C. Proteins required for ultraviolet light and chemical mutagenesis. Identification of the products of the umuC locus of Escherichia coli. J. Mol. Biol. 164:1983;175-192.
    • (1983) J. Mol. Biol. , vol.164 , pp. 175-192
    • Elledge, S.J.1    Walker, G.C.2
  • 5
    • 0033527533 scopus 로고    scopus 로고
    • The mutagenesis protein UmuC is a DNA polymerase activated by UmuD′, RecA, and SSB and is specialized for translesion replication
    • Reuven N.B., Arad G., Maor-Shoshani A., Livneh Z. The mutagenesis protein UmuC is a DNA polymerase activated by UmuD′, RecA, and SSB and is specialized for translesion replication. J. Biol. Chem. 274:1999;31763-31766.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31763-31766
    • Reuven, N.B.1    Arad, G.2    Maor-Shoshani, A.3    Livneh, Z.4
  • 7
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Pol η
    • Johnson R.E., Prakash S., Prakash L. Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Pol η Science. 283:1999;1001-1004.
    • (1999) Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 9
    • 0030443024 scopus 로고    scopus 로고
    • DNA polymerase ζ and the control of DNA damage induced mutagenesis in eukaryotes
    • Lawrence C.W., Hinkle D.C. DNA polymerase ζ and the control of DNA damage induced mutagenesis in eukaryotes. Cancer Surv. 28:1996;21-31.
    • (1996) Cancer Surv. , vol.28 , pp. 21-31
    • Lawrence, C.W.1    Hinkle, D.C.2
  • 12
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis
    • Wagner J., Gruz P., Kim S.R., Yamada M., Matsui K., Fuchs R.P., Nohmi T. The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis. Mol. Cell. 4:1999;281-286.
    • (1999) Mol. Cell , vol.4 , pp. 281-286
    • Wagner, J.1    Gruz, P.2    Kim, S.R.3    Yamada, M.4    Matsui, K.5    Fuchs, R.P.6    Nohmi, T.7
  • 14
    • 0034462969 scopus 로고    scopus 로고
    • Role of the dinB gene product in spontaneous mutation in Escherichia coli with an impaired replicative polymerase
    • This paper shows that the relative activities and amounts of replicative versus lesion-bypass DNA polymerases (Pol III and DinB) in the cell influence the mutation rate during replication.
    • Strauss B.S., Roberts R., Francis L., Pouryazdanparast P. Role of the dinB gene product in spontaneous mutation in Escherichia coli with an impaired replicative polymerase. J. Bacteriol. 182:2000;6742-6750 This paper shows that the relative activities and amounts of replicative versus lesion-bypass DNA polymerases (Pol III and DinB) in the cell influence the mutation rate during replication.
    • (2000) J. Bacteriol. , vol.182 , pp. 6742-6750
    • Strauss, B.S.1    Roberts, R.2    Francis, L.3    Pouryazdanparast, P.4
  • 17
    • 0034214838 scopus 로고    scopus 로고
    • Pol ι, a remarkably error-prone human DNA polymerase
    • Tissier A., McDonald J.P., Frank E.G., Woodgate R. Pol ι, a remarkably error-prone human DNA polymerase. Genes Dev. 14:2000;1642-1650.
    • (2000) Genes Dev. , vol.14 , pp. 1642-1650
    • Tissier, A.1    McDonald, J.P.2    Frank, E.G.3    Woodgate, R.4
  • 18
    • 0033830464 scopus 로고    scopus 로고
    • Preferential incorporation of G opposite template T by the low-fidelity human DNA polymerase ι
    • Zhang Y., Yuan F., Wu X., Wang Z. Preferential incorporation of G opposite template T by the low-fidelity human DNA polymerase ι Mol. Cell Biol. 20:2000;7099-7108.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7099-7108
    • Zhang, Y.1    Yuan, F.2    Wu, X.3    Wang, Z.4
  • 19
    • 0033538470 scopus 로고    scopus 로고
    • HRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson R.E., Kondratick C.M., Prakash S., Prakash L. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 285:1999;263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 20
    • 0032814005 scopus 로고    scopus 로고
    • Archaeal DNA replication: Identifying the pieces to solve a puzzle
    • Cann I.K., Ishino Y. Archaeal DNA replication: identifying the pieces to solve a puzzle. Genetics. 152:1999;1249-1267.
    • (1999) Genetics , vol.152 , pp. 1249-1267
    • Cann, I.K.1    Ishino, Y.2
  • 21
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 22
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis D.L., Brick P., Hamlin R., Xuong N.G., Steitz T.A. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature. 313:1985;762-766.
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 23
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer J.R., Mao C., Braman J.C., Beese L.S. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature. 391:1998;304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 24
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • Franklin M.C., Wang J., Steitz T.A. Structure of the replicating complex of a pol α family DNA polymerase. Cell. 105:2001;657-667.
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 25
    • 0034595517 scopus 로고    scopus 로고
    • Crystal structure of a pol α family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7
    • Rodriguez A.C., Park H.W., Mao C., Beese L.S. Crystal structure of a pol α family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7. J. Mol. Biol. 299:2000;447-462.
    • (2000) J. Mol. Biol. , vol.299 , pp. 447-462
    • Rodriguez, A.C.1    Park, H.W.2    Mao, C.3    Beese, L.S.4
  • 26
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li Y., Korolev S., Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation. EMBO J. 17:1998;7514-7525.
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 27
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with DNA: Implications for catalytic mechanism, processivity, and fidelity
    • Pelletier H., Sawaya M.R., Wolfle W., Wilson S.H., Kraut J. Crystal structures of human DNA polymerase β complexed with DNA: implications for catalytic mechanism, processivity, and fidelity. Biochemistry. 35:1996;12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 28
    • 0034734386 scopus 로고    scopus 로고
    • Structural design of a eukaryotic DNA repair polymerase: DNA polymerase β
    • This paper provides a comprehensive summary of the structural and biochemical analyses of human Pol β.
    • Beard W.A., Wilson S.H. Structural design of a eukaryotic DNA repair polymerase: DNA polymerase β Mutat. Res. 460:2000;231-244 This paper provides a comprehensive summary of the structural and biochemical analyses of human Pol β.
    • (2000) Mutat. Res. , vol.460 , pp. 231-244
    • Beard, W.A.1    Wilson, S.H.2
  • 29
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya M.R., Prasad R., Wilson S.H., Kraut J., Pelletier H. Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry. 36:1997;11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 31
    • 0035902454 scopus 로고    scopus 로고
    • Evidence that replication fork components catalyze establishment of cohesion between sister chromatids
    • Carson D.R., Christman M.F. Evidence that replication fork components catalyze establishment of cohesion between sister chromatids. Proc. Natl. Acad. Sci. USA. 98:2001;8270-8275.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8270-8275
    • Carson, D.R.1    Christman, M.F.2
  • 34
    • 0035997344 scopus 로고    scopus 로고
    • Error-prone repair DNA polymerases in prokaryotes and eukaryotes
    • This is the most up-to-date review article of the X and Y family polymerases.
    • Goodman M.F. Error-prone repair DNA polymerases in prokaryotes and eukaryotes. Annu. Rev. Biochem. 71:2002;17-50 This is the most up-to-date review article of the X and Y family polymerases.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 17-50
    • Goodman, M.F.1
  • 35
    • 0034945915 scopus 로고    scopus 로고
    • Expression of error-prone polymerases in BL2 cells activated for Ig somatic hypermutation
    • This paper provides evidence for the role of Y-family polymerases in somatic hypermutation.
    • Poltoratsky V., Woo C.J., Tippin B., Martin A., Goodman M.F., Scharff M.D. Expression of error-prone polymerases in BL2 cells activated for Ig somatic hypermutation. Proc. Natl. Acad. Sci. USA. 98:2001;7976-7981 This paper provides evidence for the role of Y-family polymerases in somatic hypermutation.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7976-7981
    • Poltoratsky, V.1    Woo, C.J.2    Tippin, B.3    Martin, A.4    Goodman, M.F.5    Scharff, M.D.6
  • 36
    • 0037206851 scopus 로고    scopus 로고
    • Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota
    • Faili A., Aoufouchi S., Flatter E., Gueranger Q., Reynaud C.A., Weill J.C. Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota. Nature. 419:2002;944-947.
    • (2002) Nature , vol.419 , pp. 944-947
    • Faili, A.1    Aoufouchi, S.2    Flatter, E.3    Gueranger, Q.4    Reynaud, C.A.5    Weill, J.C.6
  • 37
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • The crystal structure of the Dbh1 catalytic core is the first to be elucidated of the Y-family polymerases. This structure suggests that the Y-family polymerase is in a 'closed' active conformation even in the absence of substrate.
    • Zhou B.L., Pata J.D., Steitz T.A. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol. Cell. 8:2001;427-437 The crystal structure of the Dbh1 catalytic core is the first to be elucidated of the Y-family polymerases. This structure suggests that the Y-family polymerase is in a 'closed' active conformation even in the absence of substrate.
    • (2001) Mol. Cell , vol.8 , pp. 427-437
    • Zhou, B.L.1    Pata, J.D.2    Steitz, T.A.3
  • 38
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of S. cerevisiae DNA polymerase η: Implications for translesion DNA synthesis
    • This paper reports the crystal structure of a large fragment of yeast Pol η, the homolog of human XP-V protein implicated in skin cancer. It is also the first structure of a eukaryotic Y-family polymerase.
    • Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L., Aggarwal A.K. Structure of the catalytic core of S. cerevisiae DNA polymerase η: implications for translesion DNA synthesis. Mol. Cell. 8:2001;417-426 This paper reports the crystal structure of a large fragment of yeast Pol η, the homolog of human XP-V protein implicated in skin cancer. It is also the first structure of a eukaryotic Y-family polymerase.
    • (2001) Mol. Cell , vol.8 , pp. 417-426
    • Trincao, J.1    Johnson, R.E.2    Escalante, C.R.3    Prakash, S.4    Prakash, L.5    Aggarwal, A.K.6
  • 40
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • The crystal structures of Dpo4-DNA complexes revealed the details of protein-DNA interactions and a mechanism by which the Y-family polymerases perform low-fidelity and translesion DNA synthesis.
    • Ling H., Boudsocq F., Woodgate R., Yang W. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell. 107:2001;91-102 The crystal structures of Dpo4-DNA complexes revealed the details of protein-DNA interactions and a mechanism by which the Y-family polymerases perform low-fidelity and translesion DNA synthesis.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 41
    • 0035862988 scopus 로고    scopus 로고
    • Domain structure, localization, and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells
    • Kannouche P., Broughton B.C., Volker M., Hanaoka F., Mullenders L.H., Lehmann A.R. Domain structure, localization, and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells. Genes Dev. 15:2001;158-172.
    • (2001) Genes Dev. , vol.15 , pp. 158-172
    • Kannouche, P.1    Broughton, B.C.2    Volker, M.3    Hanaoka, F.4    Mullenders, L.H.5    Lehmann, A.R.6
  • 42
    • 0034852569 scopus 로고    scopus 로고
    • Interaction with PCNA is essential for yeast DNA polymerase η function
    • This paper reports the role of PCNA in lesion-bypass DNA synthesis and identifies the region of Pol η that interacts physically with PCNA.
    • Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L. Interaction with PCNA is essential for yeast DNA polymerase η function. Mol. Cell. 8:2001;407-415 This paper reports the role of PCNA in lesion-bypass DNA synthesis and identifies the region of Pol η that interacts physically with PCNA.
    • (2001) Mol. Cell , vol.8 , pp. 407-415
    • Haracska, L.1    Kondratick, C.M.2    Unk, I.3    Prakash, S.4    Prakash, L.5
  • 43
    • 0035966270 scopus 로고    scopus 로고
    • Yeast DNA polymerase η utilizes an induced-fit mechanism of nucleotide incorporation
    • Washington M.T., Prakash L., Prakash S. Yeast DNA polymerase η utilizes an induced-fit mechanism of nucleotide incorporation. Cell. 107:2001;917-927.
    • (2001) Cell , vol.107 , pp. 917-927
    • Washington, M.T.1    Prakash, L.2    Prakash, S.3
  • 44
    • 0037126608 scopus 로고    scopus 로고
    • Mutations in human DNA polymerase η motif II alter bypass of DNA lesions
    • Glick E., Vigna K.L., Loeb L.A. Mutations in human DNA polymerase η motif II alter bypass of DNA lesions. EMBO J. 20:2001;7303-7312.
    • (2001) EMBO J. , vol.20 , pp. 7303-7312
    • Glick, E.1    Vigna, K.L.2    Loeb, L.A.3
  • 46
    • 0035937141 scopus 로고    scopus 로고
    • Lesion bypass by the Escherichia coli DNA polymerase V requires assembly of a RecA nucleoprotein filament
    • Reuven N.B., Arad G., Stasiak A.Z., Stasiak A., Livneh Z. Lesion bypass by the Escherichia coli DNA polymerase V requires assembly of a RecA nucleoprotein filament. J. Biol. Chem. 276:2001;5511-5517.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5511-5517
    • Reuven, N.B.1    Arad, G.2    Stasiak, A.Z.3    Stasiak, A.4    Livneh, Z.5
  • 47
    • 0036171550 scopus 로고    scopus 로고
    • The processivity factor β controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo
    • This paper provides a connection between regular DNA synthesis and translesion synthesis in bacteria, which is through β clamp, the processivity factor (PCNA equivalent).
    • Lenne-Samuel N., Wagner J., Etienne H., Fuchs R.P. The processivity factor β controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo. EMBO Rep. 3:2002;45-49 This paper provides a connection between regular DNA synthesis and translesion synthesis in bacteria, which is through β clamp, the processivity factor (PCNA equivalent).
    • (2002) EMBO Rep. , vol.3 , pp. 45-49
    • Lenne-Samuel, N.1    Wagner, J.2    Etienne, H.3    Fuchs, R.P.4
  • 48
    • 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., Nohmi T. 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. 276:2001;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
  • 49
    • 0036118423 scopus 로고    scopus 로고
    • Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae
    • Torres-Ramos C.A., Prakash S., Prakash L. Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae. Mol. Cell Biol. 22:2002;2419-2426.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 2419-2426
    • Torres-Ramos, C.A.1    Prakash, S.2    Prakash, L.3
  • 50
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • This paper identifies for the first time the sites of ubiquitination and sumoylation on yeast and human PCNA and the correlation between these modifications and DNA repair.
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141 This paper identifies for the first time the sites of ubiquitination and sumoylation on yeast and human PCNA and the correlation between these modifications and DNA repair.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 51
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson M. Ribbon models of macromolecules. J. Mol. Graph. 5:1987;103-106.
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1


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