ArticleJournal of bacteriology2007
Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- In vivo nucleotide excision repair by mycobacterial UvrD1 requires ATP hydrolysis but does not depend on cysteine disulfide-mediated dimerization and DNA unwinding.Nucleic acids research · 2025Article
- Mutation rates and adaptive variation among the clinically dominant clusters ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Rapid single-molecule characterisation of enzymes involved in nucleic-acid metabolism.Nucleic acids research · 2023Article
- Article
- An Adenosine Triphosphate- Dependent 5'-3' DNA Helicase From sk1-LikeFrontiers in microbiology · 2022Article
- A novel Ancestral Beijing sublineage of Mycobacterium tuberculosis suggests the transition site to Modern Beijing sublineages.Scientific reports · 2019Article
- Molecular and Functional Characterization of RecD, a Novel Member of the SF1 Family of Helicases, from Mycobacterium tuberculosis.The Journal of biological chemistry · 2015Article
- Mycobacterium tuberculosis DinG is a structure-specific helicase that unwinds G4 DNA: implications for targeting G4 DNA as a novel therapeutic approach.The Journal of biological chemistry · 2014Article
- Homology modeling, molecular docking and DNA binding studies of nucleotide excision repair UvrC protein from M. tuberculosis.The protein journal · 2013Article
- Mycobacterium smegmatis Lhr Is a DNA-dependent ATPase and a 3'-to-5' DNA translocase and helicase that prefers to unwind 3'-tailed RNA:DNA hybrids.The Journal of biological chemistry · 2013Article
- Mycobacterium smegmatis SftH exemplifies a distinctive clade of superfamily II DNA-dependent ATPases with 3' to 5' translocase and helicase activities.Nucleic acids research · 2012Article
- Mycobacterium tuberculosis RecG binds and unwinds model DNA substrates with a preference for Holliday junctions.Microbiology (Reading, England) · 2012Article
- Important role for Mycobacterium tuberculosis UvrD1 in pathogenesis and persistence apart from its function in nucleotide excision repair.Journal of bacteriology · 2012Article
- Mycobacterium smegmatis RqlH defines a novel clade of bacterial RecQ-like DNA helicases with ATP-dependent 3'-5' translocase and duplex unwinding activities.Nucleic acids research · 2012Article
- Article
- Enzymatic activities and DNA substrate specificity of Mycobacterium tuberculosis DNA helicase XPB.PloS one · 2012Article
- UvrD2 is essential in Mycobacterium tuberculosis, but its helicase activity is not required.Journal of bacteriology · 2011Article
- Processive translocation mechanism of the human Bloom's syndrome helicase along single-stranded DNA.Nucleic acids research · 2010Article
- A SRS2 homolog from Arabidopsis thaliana disrupts recombinogenic DNA intermediates and facilitates single strand annealing.Nucleic acids research · 2009Article
- Mutational analysis of Mycobacterium UvrD1 identifies functional groups required for ATP hydrolysis, DNA unwinding, and chemomechanical coupling.Biochemistry · 2009Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
UvrD is a helicase that is widely conserved in gram-negative bacteria. A uvrD homologue was identified in Mycobacterium tuberculosis on the basis of the homology of its encoded protein with Escherichia coli UvrD, with which it shares 39% amino acid identity, distributed throughout the protein. The gene was cloned, and a histidine-tagged form of the protein was expressed and purified to homogeneity. The purified protein had in vitro ATPase activity that was dependent upon the presence of DNA. Oligonucleotides as short as four nucleotides were sufficient to promote the ATPase activity. The DNA helicase activity of the enzyme was only fueled by ATP and dATP. UvrD preferentially unwound 3'-single-stranded tailed duplex substrates over 5'-single-stranded ones, indicating that the protein had a duplex-unwinding activity with 3'-to-5' polarity. A 3' single-stranded DNA tail of 18 nucleotides was required for effective unwinding. By using a series of synthetic oligonucleotide substrates, we demonstrated that M. tuberculosis UvrD has an unwinding preference towards nicked DNA duplexes and stalled replication forks, representing the likely sites of action in vivo. The potential role of M. tuberculosis UvrD in maintenance of bacterial genomic integrity makes it a promising target for drug design against M. tuberculosis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.