ArticleJournal of bacteriology2013
Biochemical and structural studies of the Mycobacterium tuberculosis O6-methylguanine methyltransferase and mutated variants.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- The DNA Alkyltransferase Family of DNA Repair Proteins: Common Mechanisms, Diverse Functions.International journal of molecular sciences · 2023Review
- First thermostable CLIP-Computational and structural biotechnology journal · 2022Article
- Roles of the hydroxy group of tyrosine in crystal structures of Sulfurisphaera tokodaiiOActa crystallographica. Section F, Structural biology communications · 2021Article
- Characterization of the Proteins Involved in the DNA Repair Mechanism inInternational journal of molecular sciences · 2020Article
- Review
- Targeting Genome Integrity inMolecules (Basel, Switzerland) · 2020Review
- A journey down to hell: new thermostable protein-tags for biotechnology at high temperatures.Extremophiles : life under extreme conditions · 2020Article
- The DNA Alkylguanine DNA Alkyltransferase-2 (AGT-2) Of Caenorhabditis Elegans Is Involved In Meiosis And Early Development Under Physiological Conditions.Scientific reports · 2019Article
- Mycobacterium tuberculosis Molecular Determinants of Infection, Survival Strategies, and Vulnerable Targets.Pathogens (Basel, Switzerland) · 2018Review
- Every OGT Is Illuminated … by Fluorescent and Synchrotron Lights.International journal of molecular sciences · 2017Review
- In vivo and in vitro protein imaging in thermophilic archaea by exploiting a novel protein tag.PloS one · 2017Article
- A novel thermostable protein-tag: optimization of the Sulfolobus solfataricus DNA- alkyl-transferase by protein engineering.Extremophiles : life under extreme conditions · 2016Article
- Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein.Nucleic acids research · 2015Article
- The BER necessities: the repair of DNA damage in human-adapted bacterial pathogens.Nature reviews. Microbiology · 2015Review
- Genome stability: recent insights in the topoisomerase reverse gyrase and thermophilic DNA alkyltransferase.Extremophiles : life under extreme conditions · 2014Review
- UVC-mutagenesis in acetogens: resistance to methanol, ethanol, acetone, or n-butanol in recombinants with tailored genomes as the step in engineering of commercial biocatalysts for continuous CO₂/H₂ blend fermentations.World journal of microbiology & biotechnology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis displays remarkable genetic stability despite continuous exposure to the hostile environment represented by the host's infected macrophages. Similarly to other organisms, M. tuberculosis possesses multiple systems to counteract the harmful potential of DNA alkylation. In particular, the suicidal enzyme O(6)-methylguanine-DNA methyltransferase (OGT) is responsible for the direct repair of O(6)-alkylguanine in double-stranded DNA and is therefore supposed to play a central role in protecting the mycobacterial genome from the risk of G · C-to-A · T transition mutations. Notably, a number of geographically widely distributed M. tuberculosis strains shows nonsynonymous single-nucleotide polymorphisms in their OGT-encoding gene, leading to amino acid substitutions at position 15 (T15S) or position 37 (R37L) of the N-terminal domain of the corresponding protein. However, the role of these mutations in M. tuberculosis pathogenesis is unknown. We describe here the in vitro characterization of M. tuberculosis OGT (MtOGT) and of two point-mutated versions of the protein mimicking the naturally occurring ones, revealing that both mutated proteins are impaired in their activity as a consequence of their lower affinity for alkylated DNA than the wild-type protein. The analysis of the crystal structures of MtOGT and MtOGT-R37L confirms the high level of structural conservation of members of this protein family and provides clues to an understanding of the molecular bases for the reduced affinity for the natural substrate displayed by mutated MtOGT. Our in vitro results could contribute to validate the inferred participation of mutated OGTs in M. tuberculosis phylogeny and biology.
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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.