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Volumn 195, Issue 7, 2013, Pages 1552-1560

Biochemical properties of MutT2 proteins from Mycobacterium tuberculosis and M. Smegmatis and their contrasting antimutator roles in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

5 METHYL DEOXYCYTIDINE TRIPHOSPHATE; 8 OXO DEOXYGUANOSINE TRIPHOSPHATE; 8 OXO GUANOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; DEOXYCYTIDINE TRIPHOSPHATE; DEOXYGUANOSINE TRIPHOSPHATE; GUANOSINE DERIVATIVE; GUANOSINE TRIPHOSPHATE; MSMMUTT2 PROTEIN; MTUMUTT2 PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84875521574     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02102-12     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 0036200214 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen intermediates and bacterial defenses: unusual adaptations in Mycobacterium tuberculosis
    • Zahrt TC, Deretic V. 2002. Reactive nitrogen and oxygen intermediates and bacterial defenses: unusual adaptations in Mycobacterium tuberculosis. Antioxid. Redox Signal. 4:141-159.
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 141-159
    • Zahrt, T.C.1    Deretic, V.2
  • 2
    • 67650164516 scopus 로고    scopus 로고
    • Mycobacterial survival strategies in the phagosome: defence against host stresses
    • Ehrt S, Schnappinger D. 2009. Mycobacterial survival strategies in the phagosome: defence against host stresses. Cell. Microbiol. 11:1170 -1178.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1170-1178
    • Ehrt, S.1    Schnappinger, D.2
  • 3
    • 84859645414 scopus 로고    scopus 로고
    • The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species
    • doi:10.3389/fmicb.2011.00105
    • Voskuil MI, Bartek IL, Visconti K, Schoolnik GK. 2011. The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species. Front. Microbiol. 2:105. doi:10.3389/fmicb.2011.00105.
    • (2011) Front. Microbiol. , vol.2 , pp. 105
    • Voskuil, M.I.1    Bartek, I.L.2    Visconti, K.3    Schoolnik, G.K.4
  • 4
    • 0019371501 scopus 로고
    • Killing of Mycobacterium microti by immunologically activated macrophages
    • Walker L, Lowrie DB. 1981. Killing of Mycobacterium microti by immunologically activated macrophages. Nature 293:69 -71.
    • (1981) Nature , vol.293 , pp. 69-71
    • Walker, L.1    Lowrie, D.B.2
  • 5
    • 0026549480 scopus 로고
    • Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages
    • Chan J, Xing Y, Magliozzo RS, Bloom BR. 1992. Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages. J. Exp. Med. 175:1111-1122.
    • (1992) J. Exp. Med. , vol.175 , pp. 1111-1122
    • Chan, J.1    Xing, Y.2    Magliozzo, R.S.3    Bloom, B.R.4
  • 7
    • 33646080824 scopus 로고    scopus 로고
    • Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products
    • Neeley WL, Essigmann JM. 2006. Mechanisms of formation, genotoxicity, and mutation of guanine oxidation products. Chem. Res. Toxicol. 19:491-505.
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 491-505
    • Neeley, W.L.1    Essigmann, J.M.2
  • 8
    • 0036628726 scopus 로고    scopus 로고
    • Biological consequences of free radical-damaged DNA bases
    • Wallace SS. 2002. Biological consequences of free radical-damaged DNA bases. Free Radic. Biol. Med. 33:1-14.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1-14
    • Wallace, S.S.1
  • 10
    • 80755128334 scopus 로고    scopus 로고
    • Base excision and nucleotide excision repair pathways in mycobacteria
    • Edinb.
    • Kurthkoti K, Varshney U. 2011. Base excision and nucleotide excision repair pathways in mycobacteria. Tuberculosis (Edinb.) 91:533-543.
    • (2011) Tuberculosis , vol.91 , pp. 533-543
    • Kurthkoti, K.1    Varshney, U.2
  • 11
    • 84860734902 scopus 로고    scopus 로고
    • Distinct mechanisms of DNA repair in mycobacteria and their implications in attenuation of the pathogen growth
    • Kurthkoti K, Varshney U. 2012. Distinct mechanisms of DNA repair in mycobacteria and their implications in attenuation of the pathogen growth. Mech. Ageing Dev. 133:138 -146.
    • (2012) Mech. Ageing Dev. , vol.133 , pp. 138-146
    • Kurthkoti, K.1    Varshney, U.2
  • 12
    • 75149134881 scopus 로고    scopus 로고
    • The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts
    • Guo Y, Bandaru V, Jaruga P, Zhao X, Burrows CJ, Iwai S, Dizdaroglu M, Bond JP, Wallace SS. 2010. The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts. DNA Repair (Amst.) 9:177-190.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 177-190
    • Guo, Y.1    Bandaru, V.2    Jaruga, P.3    Zhao, X.4    Burrows, C.J.5    Iwai, S.6    Dizdaroglu, M.7    Bond, J.P.8    Wallace, S.S.9
  • 13
    • 35748939666 scopus 로고    scopus 로고
    • A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria
    • Jain R, Kumar P, Varshney U. 2007. A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria. DNA Repair (Amst.) 6:1774 -1785.
    • (2007) DNA Repair (Amst.) , vol.6
    • Jain, R.1    Kumar, P.2    Varshney, U.3
  • 14
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8- dihydro-8-oxoguanine)
    • Michaels ML, Miller JH. 1992. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8- dihydro-8-oxoguanine). J. Bacteriol. 174:6321- 6325.
    • (1992) J. Bacteriol. , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 15
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan HE, Standal R, Slupphaug G. 1997. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325(Pt 1):1-16.
    • (1997) Biochem. J. , vol.325 , Issue.PART 1 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 16
    • 0031692027 scopus 로고    scopus 로고
    • DNA repair in Mycobacterium tuberculosis What have we learnt from the genome sequence
    • Mizrahi V, Andersen SJ. 1998. DNA repair in Mycobacterium tuberculosis. What have we learnt from the genome sequence? Mol. Microbiol. 29:1331-1339.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1331-1339
    • Mizrahi, V.1    Andersen, S.J.2
  • 17
    • 0242690139 scopus 로고    scopus 로고
    • The majority of inducible DNA repair genes in Mycobacterium tuberculosis are induced independently of RecA
    • Rand L, Hinds J, Springer B, Sander P, Buxton RS, Davis EO. 2003. The majority of inducible DNA repair genes in Mycobacterium tuberculosis are induced independently of RecA. Mol. Microbiol. 50:1031-1042.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1031-1042
    • Rand, L.1    Hinds, J.2    Springer, B.3    Sander, P.4    Buxton, R.S.5    Davis, E.O.6
  • 18
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H, Sekiguchi M. 1992. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 355:273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 19
    • 17844405031 scopus 로고    scopus 로고
    • Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools
    • Ito R, Hayakawa H, Sekiguchi M, Ishibashi T. 2005. Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools. Biochemistry 44:6670-6674.
    • (2005) Biochemistry , vol.44 , pp. 6670-6674
    • Ito, R.1    Hayakawa, H.2    Sekiguchi, M.3    Ishibashi, T.4
  • 21
    • 9144272293 scopus 로고    scopus 로고
    • Increased A:T → C:G mutations in the mutT strain upon 8-hydroxy-dGTP treatment: direct evidence for MutT involvement in the prevention of mutations by oxidized dGTP
    • Kamiya H, Ishiguro C, Harashima H. 2004. Increased A:T → C:G mutations in the mutT strain upon 8-hydroxy-dGTP treatment: direct evidence for MutT involvement in the prevention of mutations by oxidized dGTP. J. Biochem. 136:359 -362.
    • (2004) J. Biochem. , vol.136 , pp. 359-362
    • Kamiya, H.1    Ishiguro, C.2    Harashima, H.3
  • 22
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • McLennan AG. 2006. The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63:123-143.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 23
    • 33646011231 scopus 로고    scopus 로고
    • Identification of Nudix hydrolase family members with an antimutator role in Mycobacterium tuberculosis and Mycobacterium smegmatis
    • Dos Vultos T, Blazquez J, Rauzier J, Matic I, Gicquel B. 2006. Identification of Nudix hydrolase family members with an antimutator role in Mycobacterium tuberculosis and Mycobacterium smegmatis. J. Bacteriol. 188:3159 -3161.
    • (2006) J. Bacteriol. , vol.188 , pp. 3159-3161
    • Dos Vultos, T.1    Blazquez, J.2    Rauzier, J.3    Matic, I.4    Gicquel, B.5
  • 24
    • 60749117447 scopus 로고    scopus 로고
    • Making sense of a missense mutation: characterization of MutT2, a Nudix hydrolase from Mycobacterium tuberculosis, and the G58R mutant encoded in W-Beijing strains of M
    • Moreland NJ, Charlier C, Dingley AJ, Baker EN, Lott JS. 2009. Making sense of a missense mutation: characterization of MutT2, a Nudix hydrolase from Mycobacterium tuberculosis, and the G58R mutant encoded in W-Beijing strains of M. tuberculosis. Biochemistry 48:699 -708.
    • (2009) tuberculosis. Biochemistry , vol.48 , pp. 699-708
    • Moreland, N.J.1    Charlier, C.2    Dingley, A.J.3    Baker, E.N.4    Lott, J.S.5
  • 28
    • 0345549815 scopus 로고
    • A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions
    • U.S.A.
    • Cupples CG, Miller JH. 1989. A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc. Natl. Acad. Sci. U. S. A. 86:5345-5349.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 5345-5349
    • Cupples, C.G.1    Miller, J.H.2
  • 29
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
    • Sedmak JJ, Grossberg SE. 1977. A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal. Biochem. 79:544 -552.
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 30
    • 0038449261 scopus 로고    scopus 로고
    • A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides
    • Ishibashi T, Hayakawa H, Sekiguchi M. 2003. A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides. EMBO Rep. 4:479-483.
    • (2003) EMBO Rep. , vol.4 , pp. 479-483
    • Ishibashi, T.1    Hayakawa, H.2    Sekiguchi, M.3
  • 31
    • 21644442775 scopus 로고    scopus 로고
    • Comprehensive analysis of cytosolic Nudix hydrolases in Arabidopsis thaliana
    • Ogawa T, Ueda Y, Yoshimura K, Shigeoka S. 2005. Comprehensive analysis of cytosolic Nudix hydrolases in Arabidopsis thaliana. J. Biol. Chem. 280:25277-25283.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25277-25283
    • Ogawa, T.1    Ueda, Y.2    Yoshimura, K.3    Shigeoka, S.4
  • 32
    • 84859958491 scopus 로고    scopus 로고
    • Oxidation of the guanine nucleotide pool underlies cell death by bactericidal antibiotics
    • Foti JJ, Devadoss B, Winkler JA, Collins JJ, Walker GC. 2012. Oxidation of the guanine nucleotide pool underlies cell death by bactericidal antibiotics. Science 336:315-319.
    • (2012) Science , vol.336 , pp. 315-319
    • Foti, J.J.1    Devadoss, B.2    Winkler, J.A.3    Collins, J.J.4    Walker, G.C.5
  • 33
    • 83355173923 scopus 로고    scopus 로고
    • Comparative analysis of mycobacterial NADH pyrophosphatase isoforms reveals a novel mechanism for isoniazid and ethionamide inactivation
    • Wang XD, Gu J, Wang T, Bi LJ, Zhang ZP, Cui ZQ, Wei HP, Deng JY, Zhang XE. 2011. Comparative analysis of mycobacterial NADH pyrophosphatase isoforms reveals a novel mechanism for isoniazid and ethionamide inactivation. Mol. Microbiol. 82:1375-1391.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1375-1391
    • Wang, X.D.1    Gu, J.2    Wang, T.3    Bi, L.J.4    Zhang, Z.P.5    Cui, Z.Q.6    Wei, H.P.7    Deng, J.Y.8    Zhang, X.E.9
  • 34
    • 0035937181 scopus 로고    scopus 로고
    • Orf135 from Escherichia coli is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP
    • O'Handley SF, Dunn CA, Bessman MJ. 2001. Orf135 from Escherichia coli is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP. J. Biol. Chem. 276:5421-5426.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5421-5426
    • O'Handley, S.F.1    Dunn, C.A.2    Bessman, M.J.3
  • 36
    • 4544279241 scopus 로고    scopus 로고
    • Important amino acids in the phosphohydrolase module of Escherichia coli Orf135
    • Kamiya H, Iida E, Harashima H. 2004. Important amino acids in the phosphohydrolase module of Escherichia coli Orf135. Biochem. Biophys. Res. Commun. 323:1063-1068.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 1063-1068
    • Kamiya, H.1    Iida, E.2    Harashima, H.3
  • 37
    • 17144391104 scopus 로고    scopus 로고
    • Amino acid residues involved in substrate recognition of the Escherichia coli Orf135 protein
    • Iida E, Satou K, Mishima M, Kojima C, Harashima H, Kamiya H. 2005. Amino acid residues involved in substrate recognition of the Escherichia coli Orf135 protein. Biochemistry 44:5683-5689.
    • (2005) Biochemistry , vol.44 , pp. 5683-5689
    • Iida, E.1    Satou, K.2    Mishima, M.3    Kojima, C.4    Harashima, H.5    Kamiya, H.6


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