Literature DB >> 16585780

Identification of Nudix hydrolase family members with an antimutator role in Mycobacterium tuberculosis and Mycobacterium smegmatis.

T Dos Vultos1, J Blázquez, J Rauzier, I Matic, B Gicquel.   

Abstract

Mycobacterium tuberculosis and Mycobacterium smegmatis MutT1, MutT2, MutT3, and Rv3908 (MutT4) enzymes were screened for an antimutator role. Results indicate that both MutT1, in M. tuberculosis and M. smegmatis, and MutT4, in M. smegmatis, have that role. Furthermore, an 8-oxo-guanosine triphosphatase function for MutT1 and MutT2 is suggested.

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Year:  2006        PMID： 16585780      PMCID： PMC1446978          DOI： 10.1128/JB.188.8.3159-3161.2006

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  27 in total

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5.  Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance.

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  22 in total

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2.  Crystallization and preliminary X-ray characterization of MutT2, MSMEG_5148 from Mycobacterium smegmatis.

Authors:  S M Arif; P B Sang; U Varshney; M Vijayan
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-01-21       Impact factor: 1.056

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Review 4.  A new evolutionary and pharmacokinetic-pharmacodynamic scenario for rapid emergence of resistance to single and multiple anti-tuberculosis drugs.

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5.  Nucleoside Diphosphate Kinase Escalates A-to-C Mutations in MutT-Deficient Strains of Escherichia coli.

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

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7.  Isoxyl activation is required for bacteriostatic activity against Mycobacterium tuberculosis.

Authors:  Jana Korduláková; Yves L Janin; Avraham Liav; Nathalie Barilone; Tiago Dos Vultos; Jean Rauzier; Patrick J Brennan; Brigitte Gicquel; Mary Jackson
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8.  Oxidation of dCTP contributes to antibiotic lethality in stationary-phase mycobacteria.

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10.  Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both?

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