메뉴 건너뛰기




Volumn 390, Issue 4, 2009, Pages 699-709

Structure of the Human Rev1-DNA-dNTP Ternary Complex

Author keywords

DNA polymerase; DNA repair; DNA replication; N2 deoxyguanosine; N2 dG; Rev1; Y family polymerase

Indexed keywords

ARGININE; DEOXYCYTIDINE TRIPHOSPHATE; DEOXYGUANOSINE; DEOXYRIBONUCLEOTIDE; DNA POLYMERASE; DNA POLYMERASE REV1; GUANINE; TERNARY COMPLEX FACTOR;

EID: 67649381629     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.05.026     Document Type: Article
Times cited : (64)

References (55)
  • 1
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function
    • Prakash S., Johnson R.E., and Prakash L. Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function. Annu. Rev. Biochem. 74 (2005) 317-353
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 2
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Poleta
    • Johnson R.E., Prakash S., and Prakash L. Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Poleta. Science 283 (1999) 1001-1004
    • (1999) Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 4
    • 0034724287 scopus 로고    scopus 로고
    • Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase eta [see comments]
    • Washington M.T., Johnson R.E., Prakash S., and Prakash L. Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase eta [see comments]. Proc. Natl Acad. Sci. USA 97 (2000) 3094-3099
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3094-3099
    • Washington, M.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 5
    • 0142123120 scopus 로고    scopus 로고
    • Mechanism of nucleotide incorporation opposite a thymine-thymine dimer by yeast DNA polymerase eta
    • Washington M.T., Prakash L., and Prakash S. Mechanism of nucleotide incorporation opposite a thymine-thymine dimer by yeast DNA polymerase eta. Proc. Natl Acad. Sci. USA 100 (2003) 12093-12098
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12093-12098
    • Washington, M.T.1    Prakash, L.2    Prakash, S.3
  • 6
    • 0033538470 scopus 로고    scopus 로고
    • hRAD30 mutations in the variant form of xeroderma pigmentosum [see comments]
    • Johnson R.E., Kondratick C.M., Prakash S., and Prakash L. hRAD30 mutations in the variant form of xeroderma pigmentosum [see comments]. 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
  • 7
    • 0033578040 scopus 로고    scopus 로고
    • The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta [see comments]
    • Masutani C., Kusumoto R., Yamada A., Dohmae N., Yokoi M., Yuasa M., et al. The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta [see comments]. Nature 399 (1999) 700-704
    • (1999) Nature , vol.399 , pp. 700-704
    • Masutani, C.1    Kusumoto, R.2    Yamada, A.3    Dohmae, N.4    Yokoi, M.5    Yuasa, M.6
  • 8
    • 0034738983 scopus 로고    scopus 로고
    • Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions
    • Johnson R.E., Washington M.T., Haracska L., Prakash S., and Prakash L. Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions. Nature 406 (2000) 1015-1019
    • (2000) Nature , vol.406 , pp. 1015-1019
    • Johnson, R.E.1    Washington, M.T.2    Haracska, L.3    Prakash, S.4    Prakash, L.5
  • 10
    • 2942753954 scopus 로고    scopus 로고
    • Efficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappa
    • Washington M.T., Minko I.G., Johnson R.E., Wolfle W.T., Harris T.M., Lloyd R.S., et al. Efficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappa. Mol. Cell. Biol. 24 (2004) 5687-5693
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5687-5693
    • Washington, M.T.1    Minko, I.G.2    Johnson, R.E.3    Wolfle, W.T.4    Harris, T.M.5    Lloyd, R.S.6
  • 11
    • 33645241164 scopus 로고    scopus 로고
    • Replication past a trans-4-hydroxynonenal minor-groove adduct by the sequential action of human DNA polymerases iota and kappa
    • Wolfle W.T., Johnson R.E., Minko I.G., Lloyd R.S., Prakash S., and Prakash L. Replication past a trans-4-hydroxynonenal minor-groove adduct by the sequential action of human DNA polymerases iota and kappa. Mol. Cell. Biol. 26 (2006) 381-386
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 381-386
    • Wolfle, W.T.1    Johnson, R.E.2    Minko, I.G.3    Lloyd, R.S.4    Prakash, S.5    Prakash, L.6
  • 12
    • 3142674288 scopus 로고    scopus 로고
    • Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing
    • Nair D.T., Johnson R.E., Prakash S., Prakash L., and Aggarwal A.K. Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing. Nature 430 (2004) 377-380
    • (2004) Nature , vol.430 , pp. 377-380
    • Nair, D.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4    Aggarwal, A.K.5
  • 15
    • 33646492746 scopus 로고    scopus 로고
    • An incoming nucleotide imposes an anti to syn conformational change on the templating purine in the human DNA polymerase-iota active site
    • Nair D.T., Johnson R.E., Prakash L., Prakash S., and Aggarwal A.K. An incoming nucleotide imposes an anti to syn conformational change on the templating purine in the human DNA polymerase-iota active site. Structure 14 (2006) 749-755
    • (2006) Structure , vol.14 , pp. 749-755
    • Nair, D.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4    Aggarwal, A.K.5
  • 16
    • 0034635953 scopus 로고    scopus 로고
    • The human DINB1 gene encodes the DNA polymerase Poltheta [see comments]
    • Johnson R.E., Prakash S., and Prakash L. The human DINB1 gene encodes the DNA polymerase Poltheta [see comments]. Proc. Natl Acad. Sci. USA 97 (2000) 3838-3843
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3838-3843
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 17
    • 0037133339 scopus 로고    scopus 로고
    • Human DINB1-encoded DNA polymerase kappa is a promiscuous extender of mispaired primer termini
    • Washington M.T., Johnson R.E., Prakash L., and Prakash S. Human DINB1-encoded DNA polymerase kappa is a promiscuous extender of mispaired primer termini. Proc. Natl Acad. Sci. USA 99 (2002) 1910-1914
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1910-1914
    • Washington, M.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4
  • 18
    • 33847208855 scopus 로고    scopus 로고
    • Human DNA polymerase kappa encircles DNA: implications for mismatch extension and lesion bypass
    • Lone S., Townson S.A., Uljon S.N., Johnson R.E., Brahma A., Nair D.T., et al. Human DNA polymerase kappa encircles DNA: implications for mismatch extension and lesion bypass. Mol. Cell 25 (2007) 601-614
    • (2007) Mol. Cell , vol.25 , pp. 601-614
    • Lone, S.1    Townson, S.A.2    Uljon, S.N.3    Johnson, R.E.4    Brahma, A.5    Nair, D.T.6
  • 19
    • 0037013287 scopus 로고    scopus 로고
    • Yeast Rev1 protein is a G template-specific DNA polymerase
    • Haracska L., Prakash S., and Prakash L. Yeast Rev1 protein is a G template-specific DNA polymerase. J. Biol. Chem. 277 (2002) 15546-15551
    • (2002) J. Biol. Chem. , vol.277 , pp. 15546-15551
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 20
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson J.R., Lawrence C.W., and Hinkle D.C. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 382 (1996) 729-731
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 21
    • 25844440534 scopus 로고    scopus 로고
    • Rev1 employs a novel mechanism of DNA synthesis using a protein template
    • Nair D.T., Johnson R.E., Prakash L., Prakash S., and Aggarwal A.K. Rev1 employs a novel mechanism of DNA synthesis using a protein template. Science 309 (2005) 2219-2222
    • (2005) Science , vol.309 , pp. 2219-2222
    • Nair, D.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4    Aggarwal, A.K.5
  • 22
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution [see comments]
    • Doublie S., Tabor S., Long A.M., Richardson C.C., and Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution [see comments]. 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
  • 23
    • 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., and 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
  • 24
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: structural diversity and common mechanisms
    • Steitz T.A. DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem. 274 (1999) 17395-17398
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 25
    • 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. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell 107 (2001) 91-102
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 27
    • 33845427432 scopus 로고    scopus 로고
    • Complex formation with Rev1 enhances the proficiency of Saccharomyces cerevisiae DNA polymerase zeta for mismatch extension and for extension opposite from DNA lesions
    • Acharya N., Johnson R.E., Prakash S., and Prakash L. Complex formation with Rev1 enhances the proficiency of Saccharomyces cerevisiae DNA polymerase zeta for mismatch extension and for extension opposite from DNA lesions. Mol. Cell. Biol. 26 (2006) 9555-9563
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9555-9563
    • Acharya, N.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 28
    • 0032821162 scopus 로고    scopus 로고
    • Distinct roles for Rev1p and Rev7p during translesion synthesis in Saccharomyces cerevisiae
    • Baynton K., Bresson-Roy A., and Fuchs R.P. Distinct roles for Rev1p and Rev7p during translesion synthesis in Saccharomyces cerevisiae. Mol. Microbiol. 34 (1999) 124-133
    • (1999) Mol. Microbiol. , vol.34 , pp. 124-133
    • Baynton, K.1    Bresson-Roy, A.2    Fuchs, R.P.3
  • 31
    • 36849015797 scopus 로고    scopus 로고
    • Complex formation of yeast Rev1 with DNA polymerase eta
    • Acharya N., Haracska L., Prakash S., and Prakash L. Complex formation of yeast Rev1 with DNA polymerase eta. Mol. Cell. Biol. 27 (2007) 8401-8408
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8401-8408
    • Acharya, N.1    Haracska, L.2    Prakash, S.3    Prakash, L.4
  • 33
    • 4544251295 scopus 로고    scopus 로고
    • Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein
    • Tissier A., Kannouche P., Reck M.P., Lehmann A.R., Fuchs R.P., and Cordonnier A. Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. DNA Repair (Amsterdam) 3 (2004) 1503-1514
    • (2004) DNA Repair (Amsterdam) , vol.3 , pp. 1503-1514
    • Tissier, A.1    Kannouche, P.2    Reck, M.P.3    Lehmann, A.R.4    Fuchs, R.P.5    Cordonnier, A.6
  • 34
    • 27144521116 scopus 로고    scopus 로고
    • Complex formation of yeast Rev1 and Rev7 proteins: a novel role for the polymerase-associated domain
    • Acharya N., Haracska L., Johnson R.E., Unk I., Prakash S., and Prakash L. Complex formation of yeast Rev1 and Rev7 proteins: a novel role for the polymerase-associated domain. Mol. Cell. Biol. 25 (2005) 9734-9740
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9734-9740
    • Acharya, N.1    Haracska, L.2    Johnson, R.E.3    Unk, I.4    Prakash, S.5    Prakash, L.6
  • 35
    • 48149104225 scopus 로고    scopus 로고
    • Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance
    • D'Souza S., Waters L.S., and Walker G.C. Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance. DNA Repair (Amsterdam) 7 (2008) 1455-1470
    • (2008) DNA Repair (Amsterdam) , vol.7 , pp. 1455-1470
    • D'Souza, S.1    Waters, L.S.2    Walker, G.C.3
  • 36
    • 0038823615 scopus 로고    scopus 로고
    • Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins
    • Masuda Y., Ohmae M., Masuda K., and Kamiya K. Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. J. Biol. Chem. 278 (2003) 12356-12360
    • (2003) J. Biol. Chem. , vol.278 , pp. 12356-12360
    • Masuda, Y.1    Ohmae, M.2    Masuda, K.3    Kamiya, K.4
  • 37
    • 0035929659 scopus 로고    scopus 로고
    • Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7
    • Murakumo Y., Ogura Y., Ishii H., Numata S., Ichihara M., Croce C.M., et al. Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. J. Biol. Chem. 276 (2001) 35644-35651
    • (2001) J. Biol. Chem. , vol.276 , pp. 35644-35651
    • Murakumo, Y.1    Ogura, Y.2    Ishii, H.3    Numata, S.4    Ichihara, M.5    Croce, C.M.6
  • 39
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R.J., and Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radical Biol. Med. 11 (1991) 81-128
    • (1991) Free Radical Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 40
    • 0029824077 scopus 로고    scopus 로고
    • Lipid peroxidation as a potential endogenous source for the formation of exocyclic DNA adducts
    • Chung F.L., Chen H.J., and Nath R.G. Lipid peroxidation as a potential endogenous source for the formation of exocyclic DNA adducts. Carcinogenesis 17 (1996) 2105-2111
    • (1996) Carcinogenesis , vol.17 , pp. 2105-2111
    • Chung, F.L.1    Chen, H.J.2    Nath, R.G.3
  • 42
    • 0029664516 scopus 로고    scopus 로고
    • 2-propanodeoxyguanosine adducts as potential endogenous DNA lesions in rodent and human tissues
    • 2-propanodeoxyguanosine adducts as potential endogenous DNA lesions in rodent and human tissues. Cancer Res. 56 (1996) 452-456
    • (1996) Cancer Res. , vol.56 , pp. 452-456
    • Nath, R.G.1    Ocando, J.E.2    Chung, F.L.3
  • 43
    • 38949182319 scopus 로고    scopus 로고
    • Protein-template-directed synthesis across an acrolein-derived DNA adduct by yeast Rev1 DNA polymerase
    • Nair D.T., Johnson R.E., Prakash L., Prakash S., and Aggarwal A.K. Protein-template-directed synthesis across an acrolein-derived DNA adduct by yeast Rev1 DNA polymerase. Structure 16 (2008) 239-245
    • (2008) Structure , vol.16 , pp. 239-245
    • Nair, D.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4    Aggarwal, A.K.5
  • 44
    • 0018425446 scopus 로고
    • Double-stranded DNA stereoselectively binds benzo(a)pyrene diol epoxides
    • Meehan T., and Straub K. Double-stranded DNA stereoselectively binds benzo(a)pyrene diol epoxides. Nature 277 (1979) 410-412
    • (1979) Nature , vol.277 , pp. 410-412
    • Meehan, T.1    Straub, K.2
  • 45
    • 0033565866 scopus 로고    scopus 로고
    • Polycyclic aromatic hydrocarbons in the diet
    • Phillips D.H. Polycyclic aromatic hydrocarbons in the diet. Mutat. Res. 443 (1999) 139-147
    • (1999) Mutat. Res. , vol.443 , pp. 139-147
    • Phillips, D.H.1
  • 46
    • 0020523616 scopus 로고
    • Fifty years of benzo(a)pyrene
    • Phillips D.H. Fifty years of benzo(a)pyrene. Nature 303 (1983) 468-472
    • (1983) Nature , vol.303 , pp. 468-472
    • Phillips, D.H.1
  • 47
    • 53049095093 scopus 로고    scopus 로고
    • 6-alkylguanine DNA adducts by human DNA polymerase REV1
    • 6-alkylguanine DNA adducts by human DNA polymerase REV1. J. Biol. Chem. 283 (2008) 23645-23655
    • (2008) J. Biol. Chem. , vol.283 , pp. 23645-23655
    • Choi, J.Y.1    Guengerich, F.P.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 51
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 52
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn M.D., Murshudov G.N., and Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374 (2003) 300-321
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 53
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 54
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer G., Cohen S.X., Lamzin V.S., and Perrakis A. Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3 (2008) 1171-1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.