Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Journal of bacteriology - 1 Apr 2006

Dos Vultos T, Blázquez J, Rauzier J, Matic I, Gicquel B

Abstract excerpt

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.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Gene Deletion
Share to Genes, Bacterial
Share to Guanosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Insertional

Share to Mycobacterium smegmatis

Share to Mycobacterium tuberculosis

Share to Nucleotides

Share to Pyrophosphatases

Source

Open in PubMed Open full text

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of Nudix hydrolase family members with an antimutator role in Mycobacterium tuberculosis and Mycobacterium smegmatis.PMID 16585780Read ↗

Mycobacterium tuberculosis MutT1 (Rv2985) and ADPRase (Rv1700) proteins constitute a two-stage mechanism of 8-oxo-dGTP and 8-oxo-GTP detoxification and adenosine to cytidine mutation avoidance.Semantic proximity Read ↗

Biochemical properties of MutT2 proteins from Mycobacterium tuberculosis and M. smegmatis and their contrasting antimutator roles in Escherichia coli.Semantic proximity Read ↗

Mycobacterium smegmatis SftH exemplifies a distinctive clade of superfamily II DNA-dependent ATPases with 3' to 5' translocase and helicase activities.Semantic proximity Read ↗

The dUTPase enzyme is essential in Mycobacterium smegmatis.Semantic proximity Read ↗

Synergistic effects of UdgB and Ung in mutation prevention and protection against commonly encountered DNA damaging agents in Mycobacterium smegmatis.Semantic proximity Read ↗

A novel Nudix hydrolase for oxidized purine nucleoside triphosphates encoded by ORFYLR151c (PCD1 gene) in Saccharomyces cerevisiae.Semantic proximity Read ↗

Inhibitors of UDP-Galactopyranose Mutase Thwart Mycobacterial GrowthSemantic proximity Read ↗

Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.Semantic proximity Read ↗

A distinct physiological role of MutY in mutation prevention in mycobacteria.Semantic proximity Read ↗

Compounds with Potential Activity against Mycobacterium tuberculosis.Semantic proximity Read ↗

A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria.Semantic proximity Read ↗

Unique C-terminal extension and interactome of Mycobacterium tuberculosis GlmU impacts it's in vivo function and the survival of pathogen.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.