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Volumn 21, Issue 3, 2011, Pages 358-369

DNA polymerases provide a canon of strategies for translesion synthesis past oxidatively generated lesions

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; DEOXYADENOSINE PHOSPHATE; DEOXYADENOSINE TRIPHOSPHATE; DEOXYCYTIDINE PHOSPHATE; DEOXYGUANOSINE TRIPHOSPHATE; DNA POLYMERASE; GUANINE; POLYMERASE H; POLYMERASE KAPPA; SINGLE STRANDED DNA; TETRAHYDROFURAN; THYMIDINE TRIPHOSPHATE; UNCLASSIFIED DRUG;

EID: 79958072354     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2011.03.008     Document Type: Review
Times cited : (37)

References (57)
  • 3
    • 47649100711 scopus 로고    scopus 로고
    • DNA polymerases and human disease
    • Loeb L.A., Monnat R.J. DNA polymerases and human disease. Nat Rev Genet 2008, 9:594-604.
    • (2008) Nat Rev Genet , vol.9 , pp. 594-604
    • Loeb, L.A.1    Monnat, R.J.2
  • 4
    • 10044241865 scopus 로고    scopus 로고
    • Functions of DNA polymerases
    • Bebenek K., Kunkel T.A. Functions of DNA polymerases. Adv Protein Chem 2004, 69:137-165.
    • (2004) Adv Protein Chem , vol.69 , pp. 137-165
    • Bebenek, K.1    Kunkel, T.A.2
  • 5
    • 34547850193 scopus 로고    scopus 로고
    • Polymerase switching in DNA replication
    • Lovett S.T. Polymerase switching in DNA replication. Mol Cell 2007, 27:523-526.
    • (2007) Mol Cell , vol.27 , pp. 523-526
    • Lovett, S.T.1
  • 7
    • 0035997351 scopus 로고    scopus 로고
    • Active site tightness and substrate fit in DNA replication
    • Kool E.T. Active site tightness and substrate fit in DNA replication. Annu Rev Biochem 2002, 71:191-219.
    • (2002) Annu Rev Biochem , vol.71 , pp. 191-219
    • Kool, E.T.1
  • 8
    • 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 1999, 274:17395-17398.
    • (1999) J Biol Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 9
    • 0032425080 scopus 로고    scopus 로고
    • The mechanism of action of T7 DNA polymerase
    • Doublié S., Ellenberger T. The mechanism of action of T7 DNA polymerase. Curr Opin Struct Biol 1998, 8:704-712.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 704-712
    • Doublié, S.1    Ellenberger, T.2
  • 10
    • 27144542782 scopus 로고    scopus 로고
    • Fidelity of Dpo4: effect of metal ions, nucleotide selection and pyrophosphorolysis
    • Vaisman A., Ling H., Woodgate R., Yang W. Fidelity of Dpo4: effect of metal ions, nucleotide selection and pyrophosphorolysis. EMBO J 2005, 24:2957-2967.
    • (2005) EMBO J , vol.24 , pp. 2957-2967
    • Vaisman, A.1    Ling, H.2    Woodgate, R.3    Yang, W.4
  • 11
    • 35648951199 scopus 로고    scopus 로고
    • What a difference a decade makes: insights into translesion DNA synthesis
    • Yang W., Woodgate R. What a difference a decade makes: insights into translesion DNA synthesis. Proc Natl Acad Sci U S A 2007, 104:15591-15598.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15591-15598
    • Yang, W.1    Woodgate, R.2
  • 12
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David S.S., O'Shea V.L., Kundu S. Base-excision repair of oxidative DNA damage. Nature 2007, 447:941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 13
    • 0030971099 scopus 로고    scopus 로고
    • Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the 'A rule'
    • Shibutani S., Takeshita M., Grollman A.P. Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the 'A rule'. J Biol Chem 1997, 272:13916-13922.
    • (1997) J Biol Chem , vol.272 , pp. 13916-13922
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 14
    • 0346463162 scopus 로고    scopus 로고
    • Evaluating the contribution of base stacking during translesion DNA replication
    • Reineks E.Z., Berdis A.J. Evaluating the contribution of base stacking during translesion DNA replication. Biochemistry 2004, 43:393-404.
    • (2004) Biochemistry , vol.43 , pp. 393-404
    • Reineks, E.Z.1    Berdis, A.J.2
  • 15
    • 34548699886 scopus 로고    scopus 로고
    • Caught bending the A-rule: crystal structures of translesion DNA synthesis with a non-natural nucleotide
    • Zahn K.E., Belrhali H., Wallace S.S., Doublié S. Caught bending the A-rule: crystal structures of translesion DNA synthesis with a non-natural nucleotide. Biochemistry 2007, 46:10551-10561.
    • (2007) Biochemistry , vol.46 , pp. 10551-10561
    • Zahn, K.E.1    Belrhali, H.2    Wallace, S.S.3    Doublié, S.4
  • 16
    • 2342537864 scopus 로고    scopus 로고
    • Crystallographic snapshots of a replicative DNA polymerase encountering an abasic site
    • Hogg M., Wallace S.S., Doublié S. Crystallographic snapshots of a replicative DNA polymerase encountering an abasic site. EMBO J 2004, 23:1483-1493.
    • (2004) EMBO J , vol.23 , pp. 1483-1493
    • Hogg, M.1    Wallace, S.S.2    Doublié, S.3
  • 17
    • 2342484512 scopus 로고    scopus 로고
    • Lesion (in)tolerance reveals insights into DNA replication fidelity
    • Freisinger E., Grollman A.P., Miller H., Kisker C. Lesion (in)tolerance reveals insights into DNA replication fidelity. EMBO J 2004, 23:1494-1505.
    • (2004) EMBO J , vol.23 , pp. 1494-1505
    • Freisinger, E.1    Grollman, A.P.2    Miller, H.3    Kisker, C.4
  • 18
    • 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., Aggarwal A.K. Rev1 employs a novel mechanism of DNA synthesis using a protein template. Science 2005, 309:2219-2222.
    • (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
  • 20
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson J.R., Lawrence C.W., Hinkle D.C. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 1996, 382:729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 21
    • 70450257567 scopus 로고    scopus 로고
    • DNA polymerase beta substrate specificity: side chain modulation of the 'A-rule'
    • Beard W.A., Shock D.D., Batra V.K., Pedersen L.C., Wilson S.H. DNA polymerase beta substrate specificity: side chain modulation of the 'A-rule'. J Biol Chem 2009, 284:31680-31689.
    • (2009) J Biol Chem , vol.284 , pp. 31680-31689
    • Beard, W.A.1    Shock, D.D.2    Batra, V.K.3    Pedersen, L.C.4    Wilson, S.H.5
  • 22
    • 42949164023 scopus 로고    scopus 로고
    • Structures of DNA polymerase beta with active-site mismatches suggest a transient abasic site intermediate during misincorporation
    • Batra V.K., Beard W.A., Shock D.D., Pedersen L.C., Wilson S.H. Structures of DNA polymerase beta with active-site mismatches suggest a transient abasic site intermediate during misincorporation. Mol Cell 2008, 30:315-324.
    • (2008) Mol Cell , vol.30 , pp. 315-324
    • Batra, V.K.1    Beard, W.A.2    Shock, D.D.3    Pedersen, L.C.4    Wilson, S.H.5
  • 23
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • Johnson S.J., Taylor J.S., Beese L.S. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc Natl Acad Sci U S A 2003, 100:3895-3900.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 24
    • 77952582936 scopus 로고    scopus 로고
    • Replication through an abasic DNA lesion: structural basis for adenine selectivity
    • Obeid S., Blatter N., Kranaster R., Schnur A., Diederichs K., Welte W., Marx A. Replication through an abasic DNA lesion: structural basis for adenine selectivity. EMBO J 2010, 29:1738-1747.
    • (2010) EMBO J , vol.29 , pp. 1738-1747
    • Obeid, S.1    Blatter, N.2    Kranaster, R.3    Schnur, A.4    Diederichs, K.5    Welte, W.6    Marx, A.7
  • 25
    • 0033578332 scopus 로고    scopus 로고
    • Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation
    • Li Y., Mitaxov V., Waksman G. Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation. Proc Natl Acad Sci U S A 1999, 96:9491-9496.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9491-9496
    • Li, Y.1    Mitaxov, V.2    Waksman, G.3
  • 26
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase beta violates the 'A-rule', Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts
    • Efrati E., Tocco G., Eritja R., Wilson S.H., Goodman M.F. Abasic translesion synthesis by DNA polymerase beta violates the 'A-rule', Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts. J Biol Chem 1997, 272:2559-2569.
    • (1997) J Biol Chem , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 27
    • 1642382214 scopus 로고    scopus 로고
    • Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts
    • Ling H., Boudsocq F., Woodgate R., Yang W. Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts. Mol Cell 2004, 13:751-762.
    • (2004) Mol Cell , vol.13 , pp. 751-762
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 28
    • 72549092945 scopus 로고    scopus 로고
    • Structural insight into translesion synthesis by DNA Pol II
    • Wang F., Yang W. Structural insight into translesion synthesis by DNA Pol II. Cell 2009, 139:1279-1289.
    • (2009) Cell , vol.139 , pp. 1279-1289
    • Wang, F.1    Yang, W.2
  • 29
    • 44949150331 scopus 로고    scopus 로고
    • Use of 2-aminopurine fluorescence to study the role of the beta hairpin in the proofreading pathway catalyzed by the phage T4 and RB69 DNA polymerases
    • Subuddhi U., Hogg M., Reha-Krantz L.J. Use of 2-aminopurine fluorescence to study the role of the beta hairpin in the proofreading pathway catalyzed by the phage T4 and RB69 DNA polymerases. Biochemistry 2008, 47:6130-6137.
    • (2008) Biochemistry , vol.47 , pp. 6130-6137
    • Subuddhi, U.1    Hogg, M.2    Reha-Krantz, L.J.3
  • 30
    • 33847706180 scopus 로고    scopus 로고
    • Structural and biochemical investigation of the role in proofreading of a beta hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B family
    • Hogg M., Aller P., Konigsberg W., Wallace S.S., Doublié S. Structural and biochemical investigation of the role in proofreading of a beta hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B family. J Biol Chem 2007, 282:1432-1444.
    • (2007) J Biol Chem , vol.282 , pp. 1432-1444
    • Hogg, M.1    Aller, P.2    Konigsberg, W.3    Wallace, S.S.4    Doublié, S.5
  • 31
    • 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., 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 2006, 14:749-755.
    • (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
  • 32
    • 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., Aggarwal A.K. Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing. Nature 2004, 430:377-380.
    • (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
  • 33
  • 34
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • Kunkel T.A. DNA replication fidelity. J Biol Chem 2004, 279:16895-16898.
    • (2004) J Biol Chem , vol.279 , pp. 16895-16898
    • Kunkel, T.A.1
  • 35
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu G.W., Ober M., Carell T., Beese L.S. Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature 2004, 431:217-221.
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 36
    • 27644597370 scopus 로고    scopus 로고
    • A lysine residue in the fingers subdomain of T7 DNA polymerase modulates the miscoding potential of 8-oxo-7,8-dihydroguanosine
    • Brieba L.G., Kokoska R.J., Bebenek K., Kunkel T.A., Ellenberger T. A lysine residue in the fingers subdomain of T7 DNA polymerase modulates the miscoding potential of 8-oxo-7,8-dihydroguanosine. Structure 2005, 13:1653-1659.
    • (2005) Structure , vol.13 , pp. 1653-1659
    • Brieba, L.G.1    Kokoska, R.J.2    Bebenek, K.3    Kunkel, T.A.4    Ellenberger, T.5
  • 37
    • 77949532175 scopus 로고    scopus 로고
    • Kinetics of mismatch formation opposite lesions by the replicative DNA polymerase from bacteriophage RB69
    • Hogg M., Rudnicki J., Midkiff J., Reha-Krantz L., Doublié S., Wallace S.S. Kinetics of mismatch formation opposite lesions by the replicative DNA polymerase from bacteriophage RB69. Biochemistry 2010, 49:2317-2325.
    • (2010) Biochemistry , vol.49 , pp. 2317-2325
    • Hogg, M.1    Rudnicki, J.2    Midkiff, J.3    Reha-Krantz, L.4    Doublié, S.5    Wallace, S.S.6
  • 38
    • 77952407219 scopus 로고    scopus 로고
    • Substitution of Ala for Tyr567 in RB69 DNA polymerase allows dAMP to be inserted opposite 7,8-dihydro-8-oxoguanine
    • Beckman J., Wang M., Blaha G., Wang J., Konigsberg W.H. Substitution of Ala for Tyr567 in RB69 DNA polymerase allows dAMP to be inserted opposite 7,8-dihydro-8-oxoguanine. Biochemistry 2010, 49:4116-4125.
    • (2010) Biochemistry , vol.49 , pp. 4116-4125
    • Beckman, J.1    Wang, M.2    Blaha, G.3    Wang, J.4    Konigsberg, W.H.5
  • 39
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A.P. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 1991, 349:431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 40
    • 0037227566 scopus 로고    scopus 로고
    • Structure of DNA polymerase beta with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential
    • Krahn J.M., Beard W.A., Miller H., Grollman A.P., Wilson S.H. Structure of DNA polymerase beta with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential. Structure 2003, 11:121-127.
    • (2003) Structure , vol.11 , pp. 121-127
    • Krahn, J.M.1    Beard, W.A.2    Miller, H.3    Grollman, A.P.4    Wilson, S.H.5
  • 41
    • 77954384819 scopus 로고    scopus 로고
    • Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site
    • Batra V.K., Beard W.A., Hou E.W., Pedersen L.C., Prasad R., Wilson S.H. Mutagenic conformation of 8-oxo-7,8-dihydro-2′-dGTP in the confines of a DNA polymerase active site. Nat Struct Mol Biol 2010, 17:889-890.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 889-890
    • Batra, V.K.1    Beard, W.A.2    Hou, E.W.3    Pedersen, L.C.4    Prasad, R.5    Wilson, S.H.6
  • 42
    • 24644443795 scopus 로고    scopus 로고
    • Distinct mechanisms of cis-syn thymine dimer bypass by Dpo4 and DNA polymerase eta
    • Johnson R.E., Prakash L., Prakash S. Distinct mechanisms of cis-syn thymine dimer bypass by Dpo4 and DNA polymerase eta. Proc Natl Acad Sci U S A 2005, 102:12359-12364.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12359-12364
    • Johnson, R.E.1    Prakash, L.2    Prakash, S.3
  • 44
    • 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 1999, 285:263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 45
    • 13844296708 scopus 로고    scopus 로고
    • Bumps in the road: how replicative DNA polymerases see DNA damage
    • Hogg M., Wallace S.S., Doublié S. Bumps in the road: how replicative DNA polymerases see DNA damage. Curr Opin Struct Biol 2005, 15:86-93.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 86-93
    • Hogg, M.1    Wallace, S.S.2    Doublié, S.3
  • 46
    • 33644866040 scopus 로고    scopus 로고
    • Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4
    • Zang H., Irimia A., Choi J.Y., Angel K.C., Loukachevitch L.V., Egli M., Guengerich F.P. Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4. J Biol Chem 2006, 281:2358-2372.
    • (2006) J Biol Chem , vol.281 , pp. 2358-2372
    • Zang, H.1    Irimia, A.2    Choi, J.Y.3    Angel, K.C.4    Loukachevitch, L.V.5    Egli, M.6    Guengerich, F.P.7
  • 48
    • 34547136494 scopus 로고    scopus 로고
    • Hydrogen bonding of 7,8-dihydro-8-oxodeoxyguanosine with a charged residue in the little finger domain determines miscoding events in Sulfolobus solfataricus DNA polymerase Dpo4
    • Eoff R.L., Irimia A., Angel K.C., Egli M., Guengerich F.P. Hydrogen bonding of 7,8-dihydro-8-oxodeoxyguanosine with a charged residue in the little finger domain determines miscoding events in Sulfolobus solfataricus DNA polymerase Dpo4. J Biol Chem 2007, 282:19831-19843.
    • (2007) J Biol Chem , vol.282 , pp. 19831-19843
    • Eoff, R.L.1    Irimia, A.2    Angel, K.C.3    Egli, M.4    Guengerich, F.P.5
  • 50
    • 78149443814 scopus 로고    scopus 로고
    • Structural basis for error-free replication of oxidatively damaged DNA by yeast DNA polymerase eta
    • Silverstein T.D., Jain R., Johnson R.E., Prakash L., Prakash S., Aggarwal A.K. Structural basis for error-free replication of oxidatively damaged DNA by yeast DNA polymerase eta. Structure 2010, 18:1463-1470.
    • (2010) Structure , vol.18 , pp. 1463-1470
    • Silverstein, T.D.1    Jain, R.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5    Aggarwal, A.K.6
  • 52
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis
    • 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 eta: implications for translesion DNA synthesis. Mol Cell 2001, 8:417-426.
    • (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
  • 54
    • 69249101227 scopus 로고    scopus 로고
    • Structural and functional elucidation of the mechanism promoting error-prone synthesis by human DNA polymerase kappa opposite the 7,8-dihydro-8-oxo-2′-deoxyguanosine adduct
    • Irimia A., Eoff R.L., Guengerich F.P., Egli M. Structural and functional elucidation of the mechanism promoting error-prone synthesis by human DNA polymerase kappa opposite the 7,8-dihydro-8-oxo-2′-deoxyguanosine adduct. J Biol Chem 2009, 284:22467-22480.
    • (2009) J Biol Chem , vol.284 , pp. 22467-22480
    • Irimia, A.1    Eoff, R.L.2    Guengerich, F.P.3    Egli, M.4
  • 55
    • 79952763415 scopus 로고    scopus 로고
    • Unique active site promotes error-free replication opposite an 8-oxo-guanine lesion by human DNA polymerase iota
    • Kirouac K.N., Ling H Unique active site promotes error-free replication opposite an 8-oxo-guanine lesion by human DNA polymerase iota. Proc Natl Acad Sci U S A 2011, 108:3210-3215.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3210-3215
    • Kirouac, K.N.1    Ling, H.2
  • 56
    • 0031861823 scopus 로고    scopus 로고
    • Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates
    • Li Y., Kong Y., Korolev S., Waksman G. Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates. Protein Sci 1998, 7:1116-1123.
    • (1998) Protein Sci , vol.7 , pp. 1116-1123
    • Li, Y.1    Kong, Y.2    Korolev, S.3    Waksman, G.4


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