ArticleNucleic acids research2012
Delineation of structural domains and identification of functionally important residues in DNA repair enzyme exonuclease VII.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 18 citations in OpenAlex.
- Actuation of CRP activating region 3 by formylation modulates theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026Article
- AFragmenter: schema-free, tuneable protein domain segmentation for AlphaFold protein structures.Bioinformatics (Oxford, England) · 2025Article
- Review
- Article
- Structure ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Streptococcus agalactiae Exonuclease ExoVII Is Required for Resistance to Exogenous DNA-Damaging Agents.Journal of bacteriology · 2023Article
- Exonuclease VII repairs quinolone-induced damage by resolving DNA gyrase cleavage complexes.Science advances · 2021Article
- A second RNA-binding protein is essential for ethanol tolerance provided by the bacterial OLE ribonucleoprotein complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The multiple antibiotic resistance operon of enteric bacteria controls DNA repair and outer membrane integrity.Nature communications · 2017Article
- Characterization of cell death in Escherichia coli mediated by XseA, a large subunit of exonuclease VII.Journal of microbiology (Seoul, Korea) · 2015Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Exonuclease VII (ExoVII) is a bacterial nuclease involved in DNA repair and recombination that hydrolyses single-stranded DNA. ExoVII is composed of two subunits: large XseA and small XseB. Thus far, little was known about the molecular structure of ExoVII, the interactions between XseA and XseB, the architecture of the nuclease active site or its mechanism of action. We used bioinformatics methods to predict the structure of XseA, which revealed four domains: an N-terminal OB-fold domain, a middle putatively catalytic domain, a coiled-coil domain and a short C-terminal segment. By series of deletion and site-directed mutagenesis experiments on XseA from Escherichia coli, we determined that the OB-fold domain is responsible for DNA binding, the coiled-coil domain is involved in binding multiple copies of the XseB subunit and residues D155, R205, H238 and D241 of the middle domain are important for the catalytic activity but not for DNA binding. Altogether, we propose a model of sequence-structure-function relationships in ExoVII.
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