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Volumn 40, Issue 12, 2012, Pages 5511-5522

Selective disruption of the DNA polymerase III α-β complex by the umuD gene products

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE GAMMA; DNA DIRECTED DNA POLYMERASE III ALPHA SUBUNIT; DNA DIRECTED DNA POLYMERASE III BETA SUBUNIT; UNCLASSIFIED DRUG;

EID: 84863194099     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks229     Document Type: Article
Times cited : (14)

References (73)
  • 1
    • 0023897674 scopus 로고
    • DNA polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites
    • Maki,H., Maki,S. and Kornberg,A. (1988) DNA polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites. J. Biol. Chem., 263, 6570-6578.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6570-6578
    • Maki, H.1    Maki, S.2    Kornberg, A.3
  • 2
    • 0029026635 scopus 로고
    • DNA polymerase III holoenzyme: Structure and function of a chromosomal replicating machine
    • Kelman,Z. and O'Donnell,M. (1995) DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine. Annu. Rev. Biochem., 64, 171-200.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 171-200
    • Kelman, Z.1    O'Donnell, M.2
  • 3
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • DOI 10.1146/annurev.biochem.73.011303.073859
    • Johnson,A. and O'Donnell,M. (2005) Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem., 74, 283-315. (Pubitemid 40995509)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 4
    • 79959431646 scopus 로고    scopus 로고
    • DNA replicases from a bacterial perspective
    • McHenry,C.S. (2011) DNA replicases from a bacterial perspective. Annu. Rev. Biochem., 80, 403-436.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 403-436
    • McHenry, C.S.1
  • 5
    • 0029053989 scopus 로고
    • Assembly of a chromosomal replication machine: Two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. III. Interface between two polymerases and the clamp loader
    • Onrust,R., Finkelstein,J., Turner,J., Naktinis,V. and O'Donnell,M. (1995) Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. III. Interface between two polymerases and the clamp loader. J. Biol. Chem., 270, 13366-13377.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13366-13377
    • Onrust, R.1    Finkelstein, J.2    Turner, J.3    Naktinis, V.4    O'Donnell, M.5
  • 6
    • 0035929237 scopus 로고    scopus 로고
    • Opening of the clamp: An intimate view of an ATP-driven biological machine
    • DOI 10.1016/S0092-8674(01)00498-6
    • Ellison,V. and Stillman,B. (2001) Opening of the clamp: an intimate view of an ATP-driven biological machine. Cell, 106, 655-660. (Pubitemid 32900657)
    • (2001) Cell , vol.106 , Issue.6 , pp. 655-660
    • Ellison, V.1    Stillman, B.2
  • 7
    • 0035830939 scopus 로고    scopus 로고
    • Tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain
    • Gao,D. and McHenry,C.S. (2001) Tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain. J. Biol. Chem., 276, 4433-4440.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4433-4440
    • Gao, D.1    McHenry, C.S.2
  • 8
    • 0028839775 scopus 로고
    • DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta-delta' to a physiologically relevant range
    • Olson,M.W., Dallmann,H.G. and McHenry,C.S. (1995) DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta-delta' to a physiologically relevant range. J. Biol. Chem., 270, 29570-29577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29570-29577
    • Olson, M.W.1    Dallmann, H.G.2    McHenry, C.S.3
  • 9
    • 0034686075 scopus 로고    scopus 로고
    • Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha and DnaB and can partially replace tau in reconstituted replication forks
    • DOI 10.1074/jbc.M909257199
    • Dallmann,H.G., Kim,S., Pritchard,A.E., Marians,K.J. and McHenry,C.S. (2000) Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha AND DnaB and can partially replace tau in reconstituted replication forks. J. Biol. Chem., 275, 15512-15519. (Pubitemid 30337284)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.20 , pp. 15512-15519
    • Dallmann, H.G.1    Kim, S.2    Pritchard, A.E.3    Marians, K.J.4    McHenry, C.S.5
  • 10
    • 0023646086 scopus 로고
    • Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli
    • O'Donnell,M.E. (1987) Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli. J. Biol. Chem., 262, 16558-16565.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16558-16565
    • O'Donnell, M.E.1
  • 11
    • 33748146483 scopus 로고    scopus 로고
    • Crystal Structure of the Catalytic alpha Subunit of E. coli Replicative DNA Polymerase III
    • DOI 10.1016/j.cell.2006.07.028, PII S0092867406010221
    • Lamers,M.H., Georgescu,R.E., Lee,S.G., O'Donnell,M. and Kuriyan,J. (2006) Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III. Cell, 126, 881-892. (Pubitemid 44310779)
    • (2006) Cell , vol.126 , Issue.5 , pp. 881-892
    • Lamers, M.H.1    Georgescu, R.E.2    Lee, S.-G.3    O'Donnell, M.4    Kuriyan, J.5
  • 12
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • DOI 10.1016/S0959-440X(98)80010-9
    • Brautigam,C.A. and Steitz,T.A. (1998) Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol., 8, 54-63. (Pubitemid 28107916)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.1 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 13
    • 26844566830 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerases
    • DOI 10.1016/S0065-3233(04)71011-6, PII S0065323304710116
    • Rothwell,P.J. and Waksman,G. (2005) Structure and mechanism of DNA polymerases. Adv. Protein Chem., 71, 401-440. (Pubitemid 41446935)
    • (2005) Advances in Protein Chemistry , vol.71 , pp. 401-440
    • Rothwell, P.J.1    Waksman, G.2
  • 14
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • DOI 10.1093/nar/26.16.3746
    • Aravind,L. and Koonin,E.V. (1998) Phosphoesterase domains associated with DNA polymerases of diverse origins. Nucleic Acids Res., 26, 3746-3752. (Pubitemid 28367981)
    • (1998) Nucleic Acids Research , vol.26 , Issue.16 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 15
    • 33744952342 scopus 로고    scopus 로고
    • 2-terminal php domain of the alpha subunit of the Escherichia coli replicase binds the epsilon proofreading subunit
    • DOI 10.1074/jbc.M513844200
    • Wieczorek,A. and McHenry,C.S. (2006) The NH2-terminal PHP domain of the alpha subunit of the Escherichia coli replicase binds the epsilon proofreading subunit. J. Biol. Chem., 281, 12561-12567. (Pubitemid 43855344)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12561-12567
    • Wieczorek, A.1    McHenry, C.S.2
  • 16
    • 33748146034 scopus 로고    scopus 로고
    • The Structure of T. aquaticus DNA Polymerase III Is Distinct from Eukaryotic Replicative DNA Polymerases
    • DOI 10.1016/j.cell.2006.07.027, PII S009286740601021X
    • Bailey,S., Wing,R.A. and Steitz,T.A. (2006) The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell, 126, 893-904. (Pubitemid 44310778)
    • (2006) Cell , vol.126 , Issue.5 , pp. 893-904
    • Bailey, S.1    Wing, R.A.2    Steitz, T.A.3
  • 17
    • 53449084401 scopus 로고    scopus 로고
    • Distinct double- and single-stranded DNA binding of E. coli replicative DNA polymerase III alpha subunit
    • McCauley,M.J., Shokri,L., Sefcikova,J., Venclovas,C., Beuning,P.J. and Williams,M.C. (2008) Distinct double- and single-stranded DNA binding of E. coli replicative DNA polymerase III alpha subunit. ACS Chem. Biol., 3, 577-587.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 577-587
    • McCauley, M.J.1    Shokri, L.2    Sefcikova, J.3    Venclovas, C.4    Beuning, P.J.5    Williams, M.C.6
  • 19
    • 34248596298 scopus 로고    scopus 로고
    • The unstructed C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit
    • DOI 10.1093/nar/gkm079
    • Jergic,S., Ozawa,K., Williams,N.K., Su,X.C., Scott,D.D., Hamdan,S.M., Crowther,J.A., Otting,G. and Dixon,N.E. (2007) The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit. Nucleic Acids Res., 35, 2813-2824. (Pubitemid 47073621)
    • (2007) Nucleic Acids Research , vol.35 , Issue.9 , pp. 2813-2824
    • Jergic, S.1    Ozawa, K.2    Williams, N.K.3    Su, X.-C.4    Scott, D.D.5    Hamdan, S.M.6    Crowther, J.A.7    Otting, G.8    Dixon, N.E.9
  • 20
    • 34248551243 scopus 로고    scopus 로고
    • Solution structure of domains IVa and V of the tau subunit Escherichia coli DNA polymerase III and interaction with the alpha subunit
    • DOI 10.1093/nar/gkm080
    • Su,X.C., Jergic,S., Keniry,M.A., Dixon,N.E. and Otting,G. (2007) Solution structure of domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit. Nucleic Acids Res., 35, 2825-2832. (Pubitemid 47073622)
    • (2007) Nucleic Acids Research , vol.35 , Issue.9 , pp. 2825-2832
    • Su, X.-C.1    Jergic, S.2    Keniry, M.A.3    Dixon, N.E.4    Otting, G.5
  • 21
    • 0348134870 scopus 로고    scopus 로고
    • Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair
    • DOI 10.1093/emboj/cdg603
    • López de Saro,F.J., Georgescu,R.E., Goodman,M.F. and O'Donnell,M. (2003) Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair. EMBO J., 22, 6408-6418. (Pubitemid 37522597)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6408-6418
    • Lopez, D.S.F.J.1    Georgescu, R.E.2    Goodman, M.F.3    O'Donnell, M.4
  • 22
    • 20444420519 scopus 로고    scopus 로고
    • A bipartite polymerase-processivity factor interaction: Only the internal beta binding site of the alpha subunit is required for processive replication by the DNA polymerase III holoenzyme
    • DOI 10.1016/j.jmb.2005.04.065, PII S0022283605004985
    • Dohrmann,P.R. and McHenry,C.S. (2005) A bipartite polymerase-processivity factor interaction: only the internal beta binding site of the alpha subunit is required for processive replication by the DNA polymerase III holoenzyme. J. Mol. Biol., 350, 228-239. (Pubitemid 40805458)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.2 , pp. 228-239
    • Dohrmann, P.R.1    McHenry, C.S.2
  • 23
    • 33744952342 scopus 로고    scopus 로고
    • 2-terminal php domain of the alpha subunit of the Escherichia coli replicase binds the epsilon proofreading subunit
    • DOI 10.1074/jbc.M513844200
    • Wieczorek,A. and McHenry,C.S. (2006) The NH2-terminal php domain of the alpha subunit of the Escherichia coli replicase binds the epsilon proofreading subunit. J. Biol. Chem., 281, 12561-12567. (Pubitemid 43855344)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12561-12567
    • Wieczorek, A.1    McHenry, C.S.2
  • 25
    • 20444420519 scopus 로고    scopus 로고
    • A bipartite polymerase-processivity factor interaction: Only the internal alpha binding site of the alpha subunit is required for processive replication by the DNA polymerase III holoenzyme
    • DOI 10.1016/j.jmb.2005.04.065, PII S0022283605004985
    • Dohrmann,P.R. and McHenry,C.S. (2005) A bipartite polymerase-processivity factor interaction: only the internal beta binding site of the alpha subunit is required for processive replication by the DNA polymerase III holoenzyme. J. Mol. Biol., 350, 228-239. (Pubitemid 40805458)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.2 , pp. 228-239
    • Dohrmann, P.R.1    McHenry, C.S.2
  • 26
    • 0035830939 scopus 로고    scopus 로고
    • Tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain
    • Gao,D. and McHenry,C.S. (2001) Tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain. J. Biol. Chem., 276, 4433-4440.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4433-4440
    • Gao, D.1    McHenry, C.S.2
  • 29
    • 34548425656 scopus 로고    scopus 로고
    • Interplay Among Replicative and Specialized DNA Polymerases Determines Failure or Success of Translesion Synthesis Pathways
    • DOI 10.1016/j.jmb.2007.07.036, PII S0022283607009631
    • Fujii,S. and Fuchs,R.P. (2007) Interplay among replicative and specialized DNA polymerases determines failure or success of translesion synthesis pathways. J. Mol. Biol., 372, 883-893. (Pubitemid 47368357)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.4 , pp. 883-893
    • Fujii, S.1    Fuchs, R.P.2
  • 30
    • 9144264274 scopus 로고    scopus 로고
    • Defining the position of the switches between replicative and bypass DNA polymerases
    • DOI 10.1038/sj.emboj.7600438
    • Fujii,S. and Fuchs,R.P. (2004) Defining the position of the switches between replicative and bypass DNA polymerases. EMBO J., 23, 4342-4352. (Pubitemid 39546171)
    • (2004) EMBO Journal , vol.23 , Issue.21 , pp. 4342-4352
    • Fujii, S.1    Fuchs, R.P.2
  • 31
    • 0038365180 scopus 로고    scopus 로고
    • Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro
    • DOI 10.1046/j.1365-2443.2003.00646.x
    • Higuchi,K., Katayama,T., Iwai,S., Hidaka,M., Horiuchi,T. and Maki,H. (2003) Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro. Genes Cells, 8, 437-449. (Pubitemid 36553443)
    • (2003) Genes to Cells , vol.8 , Issue.5 , pp. 437-449
    • Higuchi, K.1    Katayama, T.2    Iwai, S.3    Hidaka, M.4    Horiuchi, T.5    Maki, H.6
  • 32
    • 0037799191 scopus 로고    scopus 로고
    • Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo
    • DOI 10.1126/science.1083964
    • Pagés,V. and Fuchs,R.P. (2003) Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo. Science, 300, 1300-1303. (Pubitemid 36618243)
    • (2003) Science , vol.300 , Issue.5623 , pp. 1300-1303
    • Pages, V.1    Fuchs, R.P.2
  • 33
    • 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
  • 34
    • 0025361131 scopus 로고
    • Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication
    • Sassanfar,M. and Roberts,J.W. (1990) Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication. J. Mol. Biol., 212, 79-96.
    • (1990) J. Mol. Biol. , vol.212 , pp. 79-96
    • Sassanfar, M.1    Roberts, J.W.2
  • 35
    • 70349146584 scopus 로고    scopus 로고
    • Chapter 5.4.3 the SOS Regulatory Network
    • Böck,A., Curtiss III.R., Kaper,J.B., Karp,P.D., Neidhardt,F.C., Nyström,T., Slauch,J.M., Squires,C.L. and Ussery,D. (eds), ASM Press, Washington, D.C.
    • Simmons,L.A., Foti,J.J., Cohen,S.E. and Walker,G.C. (2008) Chapter 5.4.3 The SOS Regulatory Network. In: Böck,A., Curtiss III.R., Kaper,J.B., Karp,P.D., Neidhardt,F.C., Nyström,T., Slauch,J.M., Squires,C.L. and Ussery,D. (eds), EcoSal-Escherichia coli and Salmonella: Cellular and Molecular Biology. ASM Press, Washington, D.C.
    • (2008) EcoSal-Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Simmons, L.A.1    Foti, J.J.2    Cohen, S.E.3    Walker, G.C.4
  • 36
    • 33846695786 scopus 로고    scopus 로고
    • Y-family DNA polymerases in Escherichia coli
    • DOI 10.1016/j.tim.2006.12.004, PII S0966842X06002782
    • Jarosz,D.F., Beuning,P.J., Cohen,S.E. and Walker,G.C. (2007) Y-family DNA polymerases in Escherichia coli. Trends Microbiol., 15, 70-77. (Pubitemid 46199189)
    • (2007) Trends in Microbiology , vol.15 , Issue.2 , pp. 70-77
    • Jarosz, D.F.1    Beuning, P.J.2    Cohen, S.E.3    Walker, G.C.4
  • 37
    • 77949570579 scopus 로고    scopus 로고
    • Structural diversity of the Y-family DNA polymerases
    • Pata,J.D. (2010) Structural diversity of the Y-family DNA polymerases. Biochim. Biophys. Acta, 1804, 1124-1135.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1124-1135
    • Pata, J.D.1
  • 42
    • 0035997344 scopus 로고    scopus 로고
    • Error-prone repair DNA polymerases in prokaryotes and eukaryotes
    • Goodman,M.F. (2002) Error-prone repair DNA polymerases in prokaryotes and eukaryotes. Annu. Rev. Biochem., 71, 17-50.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 17-50
    • Goodman, M.F.1
  • 43
    • 0037115955 scopus 로고    scopus 로고
    • How DNA lesions are turned into mutations within cells?
    • DOI 10.1038/sj.onc.1206006
    • Pagés,V. and Fuchs,R.P. (2002) How DNA lesions are turned into mutations within cells? Oncogene, 21, 8957-8966. (Pubitemid 36110825)
    • (2002) Oncogene , vol.21 , Issue.58 REV. ISS. 8 , pp. 8957-8966
    • Pages, V.1    Fuchs, R.P.P.2
  • 44
    • 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. and Livneh,Z. (1999) The mutagenesis protein UmuC is a DNA polymerase activated by UmuD', RecA, and SSB and is specialized for translesion replication. J. Biol. Chem., 274, 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
  • 46
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis
    • DOI 10.1016/S1097-2765(00)80376-7
    • Wagner,J., Gruz,P., Kim,S.R., Yamada,M., Matsui,K., Fuchs,R.P. and Nohmi,T. (1999) The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis. Mol. Cell., 4, 281-286. (Pubitemid 29456897)
    • (1999) Molecular Cell , vol.4 , Issue.2 , pp. 281-286
    • Wagner, J.1    Gruz, P.2    Kim, S.-R.3    Yamada, M.4    Matsui, K.5    Fuchs, R.P.P.6    Nohmi, T.7
  • 47
  • 48
    • 0035139882 scopus 로고    scopus 로고
    • 2C complex involved in a DNA damage checkpoint control
    • 2C complex involved in a DNA damage checkpoint control. J. Bacteriol., 183, 1215-1224.
    • (2001) J. Bacteriol. , vol.183 , pp. 1215-1224
    • Sutton, M.D.1    Walker, G.C.2
  • 49
    • 0021960630 scopus 로고
    • Cold sensitivity induced by overproduction of UmuDC in Escherichia coli
    • Marsh,L. and Walker,G.C. (1985) Cold sensitivity induced by overproduction of UmuDC in Escherichia coli. J. Bacteriol., 162, 155-161. (Pubitemid 15095847)
    • (1985) Journal of Bacteriology , vol.162 , Issue.1 , pp. 155-161
    • Marsh, L.1    Walker, G.C.2
  • 51
    • 0037117539 scopus 로고    scopus 로고
    • Posttranslational modification of the umuD-encoded subunit of Escherichia coli DNA polymerase V regulates its interactions with the beta processivity clamp
    • DOI 10.1073/pnas.082322099
    • Sutton,M.D., Narumi,I. and Walker,G.C. (2002) Posttranslational modification of the umuD-encoded subunit of Escherichia coli DNA polymerase V regulates its interactions with the beta processivity clamp. Proc. Natl Acad. Sci. USA, 99, 5307-5312. (Pubitemid 34411544)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.8 , pp. 5307-5312
    • Sutton, M.D.1    Narumi, I.2    Walker, G.C.3
  • 52
    • 77950867868 scopus 로고    scopus 로고
    • Damage signals triggering the Escherichia coli SOS response
    • Seide,W., Kow,Y.W. and Doetsch,P.W. (eds), Taylor and Francis, New York, NY
    • Sutton,M.D. (2006) Damage signals triggering the Escherichia coli SOS response. In: Seide,W., Kow,Y.W. and Doetsch,P.W. (eds), DNA Damage and Recognition. Taylor and Francis, New York, NY, pp. 781-802.
    • (2006) DNA Damage and Recognition , pp. 781-802
    • Sutton, M.D.1
  • 53
    • 0034720286 scopus 로고    scopus 로고
    • Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis
    • DOI 10.1038/35010020
    • Tang,M., Pham,P., Shen,X., Taylor,J.S., O'Donnell,M., Woodgate,R. and Goodman,M.F. (2000) Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis. Nature, 404, 1014-1018. (Pubitemid 30243598)
    • (2000) Nature , vol.404 , Issue.6781 , pp. 1014-1018
    • Tang, M.1    Pham, P.2    Shen, X.3    Taylor, J.-S.4    O'Donnell, M.5    Woodgate, R.6    Goodman, M.F.7
  • 56
    • 80755147176 scopus 로고    scopus 로고
    • Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD
    • Ollivierre,J.N., Budil,D.E. and Beuning,P.J. (2011) Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD. Mol. BioSyst. 7, 3183-3186.
    • (2011) Mol. BioSyst. , vol.7 , pp. 3183-3186
    • Ollivierre, J.N.1    Budil, D.E.2    Beuning, P.J.3
  • 57
    • 37349132340 scopus 로고    scopus 로고
    • UmuD and RecA Directly Modulate the Mutagenic Potential of the Y Family DNA Polymerase DinB
    • DOI 10.1016/j.molcel.2007.10.025, PII S1097276507007320
    • Godoy,V.G., Jarosz,D.F., Simon,S.M., Abyzov,A., Ilyin,V. and Walker,G.C. (2007) UmuD and RecA directly modulate the mutagenic potential of the Y family DNA polymerase DinB. Mol. Cell, 28, 1058-1070. (Pubitemid 350297024)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 1058-1070
    • Godoy, V.G.1    Jarosz, D.F.2    Simon, S.M.3    Abyzov, A.4    Ilyin, V.5    Walker, G.C.6
  • 59
    • 45549085521 scopus 로고    scopus 로고
    • A dynamic polymerase exchange with Escherichia coli DNA polymerase IV replacing DNA polymerase III on the sliding clamp
    • Furukohri,A., Goodman,M.F. and Maki,H. (2008) A dynamic polymerase exchange with Escherichia coli DNA polymerase IV replacing DNA polymerase III on the sliding clamp. J. Biol. Chem., 283, 11260-11269.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11260-11269
    • Furukohri, A.1    Goodman, M.F.2    Maki, H.3
  • 60
    • 33745021288 scopus 로고    scopus 로고
    • Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors
    • Beuning,P.J., Simon,S.M., Godoy,V.G., Jarosz,D.F. and Walker,G.C. (2006) Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Methods Enzymol., 408, 318-340.
    • (2006) Methods Enzymol. , vol.408 , pp. 318-340
    • Beuning, P.J.1    Simon, S.M.2    Godoy, V.G.3    Jarosz, D.F.4    Walker, G.C.5
  • 61
    • 79959799630 scopus 로고    scopus 로고
    • Escherichia coli processivity clamp beta from DNA polymerase III is dynamic in solution
    • Fang,J., Engen,J.R. and Beuning,P.J. (2011) Escherichia coli processivity clamp beta from DNA polymerase III is dynamic in solution. Biochemistry, 50, 5958-5968.
    • (2011) Biochemistry , vol.50 , pp. 5958-5968
    • Fang, J.1    Engen, J.R.2    Beuning, P.J.3
  • 63
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • DOI 10.1016/j.ab.2006.07.027, PII S0003269706005355
    • Ericsson,U.B., Hallberg,B.M., Detitta,G.T., Dekker,N. and Nordlund,P. (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem., 357, 289-298. (Pubitemid 44430091)
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 64
    • 77950863538 scopus 로고    scopus 로고
    • Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD'
    • Fang,J., Rand,K.D., Silva,M.C., Wales,T.E., Engen,J.R. and Beuning,P.J. (2010) Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD'. J. Mol. Biol., 398, 40-53.
    • (2010) J. Mol. Biol. , vol.398 , pp. 40-53
    • Fang, J.1    Rand, K.D.2    Silva, M.C.3    Wales, T.E.4    Engen, J.R.5    Beuning, P.J.6
  • 65
    • 0028142571 scopus 로고
    • A monocysteine approach for probing the structure and interactions of the UmuD protein
    • Lee,M.H., Ohta,T. and Walker,G.C. (1994) A monocysteine approach for probing the structure and interactions of the UmuD protein. J. Bacteriol., 176, 4825-4837. (Pubitemid 24253718)
    • (1994) Journal of Bacteriology , vol.176 , Issue.16 , pp. 4825-4837
    • Lee, M.H.1    Ohta, T.2    Walker, G.C.3
  • 66
    • 0029076389 scopus 로고
    • Characterization of the umu-complementing operon from R391
    • Kulaeva,O.I., Wootton,J.C., Levine,A.S. and Woodgate,R. (1995) Characterization of the umu-complementing operon from R391. J. Bacteriol., 177, 2737-2743.
    • (1995) J. Bacteriol. , vol.177 , pp. 2737-2743
    • Kulaeva, O.I.1    Wootton, J.C.2    Levine, A.S.3    Woodgate, R.4
  • 67
    • 0025043337 scopus 로고
    • Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis
    • Battista,J.R., Ohta,T., Nohmi,T., Sun,W. and Walker,G.C. (1990) Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis. Proc. Natl Acad. Sci. USA, 87, 7190-7194.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 7190-7194
    • Battista, J.R.1    Ohta, T.2    Nohmi, T.3    Sun, W.4    Walker, G.C.5
  • 69
    • 0842281648 scopus 로고    scopus 로고
    • Identification of specific amino acid residues in the E. coli beta processivity clamp involved in interactions with DNA polymerase III, UmuD and UmuD'
    • DOI 10.1016/j.dnarep.2003.11.008
    • Duzen,J.M., Walker,G.C. and Sutton,M.D. (2004) Identification of specific amino acid residues in the E. coli beta processivity clamp involved in interactions with DNA polymerase III, UmuD and UmuD'. DNA Repair, 3, 301-312. (Pubitemid 38177251)
    • (2004) DNA Repair , vol.3 , Issue.3 , pp. 301-312
    • Duzen, J.M.1    Walker, G.C.2    Sutton, M.D.3
  • 70
    • 24944543952 scopus 로고    scopus 로고
    • A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously
    • DOI 10.1016/j.molcel.2005.08.011, PII S1097276505015534
    • Indiani,C., McInerney,P., Georgescu,R., Goodman,M.F. and O'Donnell,M. (2005) A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously. Mol. Cell, 19, 805-815. (Pubitemid 41316674)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 805-815
    • Indiani, C.1    McInerney, P.2    Georgescu, R.3    Goodman, M.F.4    O'Donnell, M.5
  • 72
    • 0025815515 scopus 로고
    • Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage
    • Woodgate,R. and Ennis,D.G. (1991) Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage. Mol. Gen. Genet., 229, 10-16.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 10-16
    • Woodgate, R.1    Ennis, D.G.2
  • 73
    • 70350564160 scopus 로고    scopus 로고
    • Mechanism of polymerase collision release from sliding clamps on the lagging strand
    • Georgescu,R.E., Kurth,I., Yao,N.Y., Stewart,J., Yurieva,O. and O'Donnell,M. (2009) Mechanism of polymerase collision release from sliding clamps on the lagging strand. EMBO J., 28, 2981-2991.
    • (2009) EMBO J. , vol.28 , pp. 2981-2991
    • Georgescu, R.E.1    Kurth, I.2    Yao, N.Y.3    Stewart, J.4    Yurieva, O.5    O'Donnell, M.6


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