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Volumn 11, Issue 9, 2012, Pages 726-732

Escherichia coli UmuC active site mutants: Effects on translesion DNA synthesis, mutagenesis and cell survival

Author keywords

Pol V; Ribonucleotide incorporation; SOS mutagenesis; UV mutagenesis

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; CYCLOBUTANE DERIVATIVE; DIMER; DNA POLYMERASE; PYRIMIDINE DERIVATIVE; RIBONUCLEOTIDE; UMUC PROTEIN; UNCLASSIFIED DRUG;

EID: 84865090917     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2012.06.005     Document Type: Article
Times cited : (22)

References (54)
  • 2
    • 11944250947 scopus 로고
    • DNA polymerase II is encoded by the DNA damage-inducible dinA gene of Escherichia coli
    • Bonner C.A., Hays S., McEntee K., Goodman M.F. DNA polymerase II is encoded by the DNA damage-inducible dinA gene of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:7663-7667.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7663-7667
    • Bonner, C.A.1    Hays, S.2    McEntee, K.3    Goodman, M.F.4
  • 3
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes an novel Escherichia coli DNA polymerase (DNA pol IV) involved in mutagenesis
    • Wagner J., Gruz P., Kim S.R., Yamada M., Matsui K., Fuchs R.P.P., Nohmi T. The dinB gene encodes an novel Escherichia coli DNA polymerase (DNA pol IV) involved in mutagenesis. Mol. Cell 1999, 4:281-286.
    • (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.P.6    Nohmi, T.7
  • 5
    • 30544445218 scopus 로고    scopus 로고
    • A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates
    • Jarosz D.F., Godoy V.G., Delaney J.C., Essigmann J.M., Walker G.C. A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates. Nature 2006, 439:225-228.
    • (2006) Nature , vol.439 , pp. 225-228
    • Jarosz, D.F.1    Godoy, V.G.2    Delaney, J.C.3    Essigmann, J.M.4    Walker, G.C.5
  • 7
    • 0017743308 scopus 로고
    • Isolation and characterization of mutants of Escherichia coli deficient in induction of mutations by ultraviolet light
    • Kato T., Shinoura Y. Isolation and characterization of mutants of Escherichia coli deficient in induction of mutations by ultraviolet light. Mol. Gen. Genet. 1977, 156:121-131.
    • (1977) Mol. Gen. Genet. , vol.156 , pp. 121-131
    • Kato, T.1    Shinoura, Y.2
  • 8
    • 0018165062 scopus 로고
    • Uvm mutants of Escherichia coli K12 deficient in UV mutagenesis. I. Isolation of uvm mutants and their phenotypical characterization in DNA repair and mutagenesis
    • Steinborn G. Uvm mutants of Escherichia coli K12 deficient in UV mutagenesis. I. Isolation of uvm mutants and their phenotypical characterization in DNA repair and mutagenesis. Mol. Gen. Genet. 1978, 165:87-93.
    • (1978) Mol. Gen. Genet. , vol.165 , pp. 87-93
    • Steinborn, G.1
  • 9
    • 0000612097 scopus 로고
    • Inducibility of a gene product required for UV and chemical mutagenesis in Escherichia coli
    • Bagg A., Kenyon C.J., Walker G.C. Inducibility of a gene product required for UV and chemical mutagenesis in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1981, 78:5749-5753.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 5749-5753
    • Bagg, A.1    Kenyon, C.J.2    Walker, G.C.3
  • 11
    • 0035023305 scopus 로고    scopus 로고
    • Comparative gene expression profiles following UV exposure in wild-type and SOS-deficient Escherichia coli
    • Courcelle J., Khodursky A., Peter B., Brown P.O., Hanawalt P.C. Comparative gene expression profiles following UV exposure in wild-type and SOS-deficient Escherichia coli. Genetics 2001, 158:41-64.
    • (2001) Genetics , vol.158 , pp. 41-64
    • Courcelle, J.1    Khodursky, A.2    Peter, B.3    Brown, P.O.4    Hanawalt, P.C.5
  • 12
    • 0024121565 scopus 로고
    • UmuD mutagenesis protein of Escherichia coli: overproduction, purification and cleavage by RecA
    • Burckhardt S.E., Woodgate R., Scheuermann R.H., Echols H. UmuD mutagenesis protein of Escherichia coli: overproduction, purification and cleavage by RecA. Proc. Natl. Acad. Sci. U.S.A. 1988, 85:1811-1815.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1811-1815
    • Burckhardt, S.E.1    Woodgate, R.2    Scheuermann, R.H.3    Echols, H.4
  • 14
    • 0024121518 scopus 로고
    • RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation
    • Nohmi T., Battista J.R., Dodson L.A., Walker G.C. RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation. Proc. Natl. Acad. Sci. U.S.A. 1988, 85:1816-1820.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 1816-1820
    • Nohmi, T.1    Battista, J.R.2    Dodson, L.A.3    Walker, G.C.4
  • 15
    • 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., Walker G.C. Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:7190-7194.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7190-7194
    • Battista, J.R.1    Ohta, T.2    Nohmi, T.3    Sun, W.4    Walker, G.C.5
  • 16
    • 0031944934 scopus 로고    scopus 로고
    • Specific RecA amino acid changes affect RecA-UmuD'C interaction
    • Sommer S., Boudsocq F., Devoret R., Bailone A., Specific RecA amino acid changes affect RecA-UmuD'C interaction. Mol. Microbiol. 1998, 28:281-291.
    • (1998) Mol. Microbiol. , vol.28 , pp. 281-291
    • Sommer, S.1    Boudsocq, F.2    Devoret, R.3    Bailone, A.4
  • 19
    • 0032535038 scopus 로고    scopus 로고
    • Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis
    • Gonzalez M., Frank E.G., Levine A.S., Woodgate R. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis. Genes Dev. 1998, 12:3889-3899.
    • (1998) Genes Dev. , vol.12 , pp. 3889-3899
    • Gonzalez, M.1    Frank, E.G.2    Levine, A.S.3    Woodgate, R.4
  • 20
    • 0034596991 scopus 로고    scopus 로고
    • Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability
    • Gonzalez M., Rasulova F., Maurizi M.R., Woodgate R. Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability. EMBO J. 2000, 19:5251-5258.
    • (2000) EMBO J. , vol.19 , pp. 5251-5258
    • Gonzalez, M.1    Rasulova, F.2    Maurizi, M.R.3    Woodgate, R.4
  • 21
    • 0025815515 scopus 로고
    • Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage
    • Woodgate R., Ennis D.G. Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage. Mol. Gen. Genet. 1991, 229:10-16.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 10-16
    • Woodgate, R.1    Ennis, D.G.2
  • 23
    • 0029745671 scopus 로고    scopus 로고
    • The genetic requirements for UmuDC-mediated cold sensitivity are distinct from those for SOS mutagenesis
    • Opperman T., Murli S., Walker G.C. The genetic requirements for UmuDC-mediated cold sensitivity are distinct from those for SOS mutagenesis. J. Bacteriol. 1996, 178:4400-4411.
    • (1996) J. Bacteriol. , vol.178 , pp. 4400-4411
    • Opperman, T.1    Murli, S.2    Walker, G.C.3
  • 24
    • 0033959683 scopus 로고    scopus 로고
    • A role for the umuDC gene products of Escherichia coli in increasing resistance to DNA damage in stationary phase by inhibiting the transition to exponential growth
    • Murli S., Opperman T., Smith B.T., Walker G.C. A role for the umuDC gene products of Escherichia coli in increasing resistance to DNA damage in stationary phase by inhibiting the transition to exponential growth. J. Bacteriol. 2000, 182:1127-1135.
    • (2000) J. Bacteriol. , vol.182 , pp. 1127-1135
    • Murli, S.1    Opperman, T.2    Smith, B.T.3    Walker, G.C.4
  • 25
    • 0035139882 scopus 로고    scopus 로고
    • 2)C complex involved in a DNA damage checkpoint control
    • 2)C complex involved in a DNA damage checkpoint control. J. Bacteriol. 2001, 183:1215-1224.
    • (2001) J. Bacteriol. , vol.183 , pp. 1215-1224
    • Sutton, M.D.1    Walker, G.C.2
  • 26
    • 0027729063 scopus 로고
    • The appearance of the UmuD'C protein complex in Escherichia coli switches repair from homologous recombination to SOS mutagenesis
    • Sommer S., Bailone A., Devoret R. The appearance of the UmuD'C protein complex in Escherichia coli switches repair from homologous recombination to SOS mutagenesis. Mol. Microbiol. 1993, 10:963-971.
    • (1993) Mol. Microbiol. , vol.10 , pp. 963-971
    • Sommer, S.1    Bailone, A.2    Devoret, R.3
  • 27
    • 0034120803 scopus 로고    scopus 로고
    • Specific amino acid changes enhance the anti-recombination activity of the UmuD'C complex
    • Sommer S., Coste G., Bailone A. Specific amino acid changes enhance the anti-recombination activity of the UmuD'C complex. Mol. Microbiol. 2000, 35:1443-1453.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1443-1453
    • Sommer, S.1    Coste, G.2    Bailone, A.3
  • 30
    • 84864479581 scopus 로고    scopus 로고
    • Critical amino acids in Escherichia coli responsible for sugar discrimination and base-substitution fidelity, Nucleic Acids Res.in press doi:10.1093/nar/gks233
    • A. Vaisman, W. Kuban, J.P. McDonald, K. Karata, W. Yang, M.F. Goodman, R. Woodgate, Critical amino acids in Escherichia coli responsible for sugar discrimination and base-substitution fidelity, Nucleic Acids Res., , in press. doi:10.1093/nar/gks233.
    • Vaisman, A.1    Kuban, W.2    McDonald, J.P.3    Karata, K.4    Yang, W.5    Goodman, M.F.6    Woodgate, R.7
  • 31
    • 0032584219 scopus 로고    scopus 로고
    • A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides
    • Astatke M., Ng K., Grindley N.D., Joyce C.M. A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:3402-3407.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3402-3407
    • Astatke, M.1    Ng, K.2    Grindley, N.D.3    Joyce, C.M.4
  • 32
    • 33748742873 scopus 로고    scopus 로고
    • The properties of steric gate mutants reveal different constraints within the active sites of Y-family and A-family DNA polymerases
    • DeLucia A.M., Chaudhuri S., Potapova O., Grindley N.D., Joyce C.M. The properties of steric gate mutants reveal different constraints within the active sites of Y-family and A-family DNA polymerases. J. Biol. Chem. 2006, 281:27286-27291.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27286-27291
    • DeLucia, A.M.1    Chaudhuri, S.2    Potapova, O.3    Grindley, N.D.4    Joyce, C.M.5
  • 33
    • 0242317682 scopus 로고    scopus 로고
    • An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides
    • DeLucia A.M., Grindley N.D., Joyce C.M. An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides. Nucleic Acids Res. 2003, 31:4129-4137.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4129-4137
    • DeLucia, A.M.1    Grindley, N.D.2    Joyce, C.M.3
  • 34
    • 79951620951 scopus 로고    scopus 로고
    • Unlocking the sugar steric gate of DNA polymerases
    • Brown J.A., Suo Z. Unlocking the sugar steric gate of DNA polymerases. Biochemistry 2011, 50:1135-1142.
    • (2011) Biochemistry , vol.50 , pp. 1135-1142
    • Brown, J.A.1    Suo, Z.2
  • 36
    • 66149161889 scopus 로고    scopus 로고
    • The steric gate amino acid tyrosine 112 is required for efficient mismatched-primer extension by human DNA polymerase κ
    • Niimi N., Sassa A., Katafuchi A., Gruz P., Fujimoto H., Bonala R.R., Johnson F., Ohta T., Nohmi T. The steric gate amino acid tyrosine 112 is required for efficient mismatched-primer extension by human DNA polymerase κ. Biochemistry 2009, 48:4239-4246.
    • (2009) Biochemistry , vol.48 , pp. 4239-4246
    • Niimi, N.1    Sassa, A.2    Katafuchi, A.3    Gruz, P.4    Fujimoto, H.5    Bonala, R.R.6    Johnson, F.7    Ohta, T.8    Nohmi, T.9
  • 37
    • 0345293208 scopus 로고    scopus 로고
    • Altered translesion synthesis in E. coli Pol V mutants selected for increased recombination inhibition
    • Sommer S., Becherel O.J., Coste G., Bailone A., Fuchs R.P. Altered translesion synthesis in E. coli Pol V mutants selected for increased recombination inhibition. DNA Repair 2003, 2:1361-1369.
    • (2003) DNA Repair , vol.2 , pp. 1361-1369
    • Sommer, S.1    Becherel, O.J.2    Coste, G.3    Bailone, A.4    Fuchs, R.P.5
  • 39
    • 0021714276 scopus 로고
    • A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors
    • Churchward G., Belin D., Nagamine Y. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors. Gene 1984, 31:165-171.
    • (1984) Gene , vol.31 , pp. 165-171
    • Churchward, G.1    Belin, D.2    Nagamine, Y.3
  • 40
    • 0029916565 scopus 로고    scopus 로고
    • Substitution of mucAB or rumAB for umuDC alters the relative frequencies of the two classes of mutations induced by a site-specific T-T cyclobutane dimer and the efficiency of translesion DNA synthesis
    • Szekeres E.S.J., Woodgate R., Lawrence C.W. Substitution of mucAB or rumAB for umuDC alters the relative frequencies of the two classes of mutations induced by a site-specific T-T cyclobutane dimer and the efficiency of translesion DNA synthesis. J. Bacteriol. 1996, 178:2559-2563.
    • (1996) J. Bacteriol. , vol.178 , pp. 2559-2563
    • Szekeres, E.S.J.1    Woodgate, R.2    Lawrence, C.W.3
  • 41
    • 84858998856 scopus 로고    scopus 로고
    • Simple and efficient purification of E. coli DNA polymerase V: cofactor requirements for optimal activity and processivity in vitro
    • Karata K., Vaisman A., Goodman M.F., Woodgate R. Simple and efficient purification of E. coli DNA polymerase V: cofactor requirements for optimal activity and processivity in vitro. DNA Repair 2012, 11:431-440.
    • (2012) DNA Repair , vol.11 , pp. 431-440
    • Karata, K.1    Vaisman, A.2    Goodman, M.F.3    Woodgate, R.4
  • 42
    • 67349106024 scopus 로고    scopus 로고
    • Construction of a circular single-stranded DNA template containing a defined lesion
    • Karata K., Vidal A.E., Woodgate R. Construction of a circular single-stranded DNA template containing a defined lesion. DNA Repair 2009, 8:852-856.
    • (2009) DNA Repair , vol.8 , pp. 852-856
    • Karata, K.1    Vidal, A.E.2    Woodgate, R.3
  • 44
    • 0002802808 scopus 로고
    • Mutants of Escherichia coli requiring methionine or vitamin B12
    • Davis B.D., Mingioli E.S. Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bacteriol. 1950, 60:17-28.
    • (1950) J. Bacteriol. , vol.60 , pp. 17-28
    • Davis, B.D.1    Mingioli, E.S.2
  • 46
    • 33747862944 scopus 로고    scopus 로고
    • RecA acts in trans to allow replication of damaged DNA by DNA polymerase V
    • Schlacher K., Cox M.M., Woodgate R., Goodman M.F. RecA acts in trans to allow replication of damaged DNA by DNA polymerase V. Nature 2006, 442:883-887.
    • (2006) Nature , vol.442 , pp. 883-887
    • Schlacher, K.1    Cox, M.M.2    Woodgate, R.3    Goodman, M.F.4
  • 48
    • 0001015633 scopus 로고
    • Purines and pyrimidines
    • American Society for Microbiology, Washington, DC, J.L. Ingraham, K.B. Low, F.C. Neidhardt, B. Magasanik, M. Schaechter, H.E. Umbarger (Eds.)
    • Neuhard J., Nygaard P. Purines and pyrimidines. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology 1987, 445-473. American Society for Microbiology, Washington, DC. J.L. Ingraham, K.B. Low, F.C. Neidhardt, B. Magasanik, M. Schaechter, H.E. Umbarger (Eds.).
    • (1987) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 445-473
    • Neuhard, J.1    Nygaard, P.2
  • 49
    • 0037192312 scopus 로고    scopus 로고
    • Sequence analysis and phenotypes of five temperature sensitive mutator alleles of dnaE, encoding modified a-catalytic subunits of Escherichia coli DNA polymerase III holoenzyme
    • Vandewiele D., Fernández de Henestrosa A.R., Timms A.R., Bridges B.A., Woodgate R. Sequence analysis and phenotypes of five temperature sensitive mutator alleles of dnaE, encoding modified a-catalytic subunits of Escherichia coli DNA polymerase III holoenzyme. Mutat. Res. 2002, 499:85-95.
    • (2002) Mutat. Res. , vol.499 , pp. 85-95
    • Vandewiele, D.1    Fernández de Henestrosa, A.R.2    Timms, A.R.3    Bridges, B.A.4    Woodgate, R.5
  • 50
    • 0025314791 scopus 로고
    • RecA protein of Escherichia coli has a third essential role in SOS mutator activity
    • Sweasy J.B., Witkin E.M., Sinha N., Roegner-Maniscalco V. RecA protein of Escherichia coli has a third essential role in SOS mutator activity. J. Bacteriol. 1990, 172:3030-3036.
    • (1990) J. Bacteriol. , vol.172 , pp. 3030-3036
    • Sweasy, J.B.1    Witkin, E.M.2    Sinha, N.3    Roegner-Maniscalco, V.4
  • 51
    • 0027299907 scopus 로고
    • Induction of only one SOS operon, umuDC, is required for SOS mutagenesis in Escherichia coli
    • Sommer S., Knezevic J., Bailone A., Devoret R. Induction of only one SOS operon, umuDC, is required for SOS mutagenesis in Escherichia coli. Mol. Gen. Genet. 1993, 239:137-144.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 137-144
    • Sommer, S.1    Knezevic, J.2    Bailone, A.3    Devoret, R.4
  • 53
    • 0033564917 scopus 로고    scopus 로고
    • Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity
    • Masutani C., Araki M., Yamada A., Kusumoto R., Nogimori T., Maekawa T., Iwai S., Hanaoka F. Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity. EMBO J. 1999, 18:3491-3501.
    • (1999) EMBO J. , vol.18 , pp. 3491-3501
    • Masutani, C.1    Araki, M.2    Yamada, A.3    Kusumoto, R.4    Nogimori, T.5    Maekawa, T.6    Iwai, S.7    Hanaoka, F.8


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