ArticleThe Journal of biological chemistry2008
Crystal structure of MutS2 endonuclease domain and the mechanism of homologous recombination suppression.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Plant MutS2 proteins function in plastid ribosome quality control.bioRxiv : the preprint server for biology · 2025Article
- Expansion of the MutS gene family in plants.The Plant cell · 2025Article
- Putative MutS2 Homologs in Algae: More Goods in Shopping Bag?Journal of molecular evolution · 2024Article
- Expansion of the MutS Gene Family in Plants.bioRxiv : the preprint server for biology · 2024Article
- Plant Organellar MSH1 Is a Displacement Loop-Specific Endonuclease.Plant & cell physiology · 2024Article
- Article
- Deletion of the primase-polymerases encoding gene, located in a mobile element inFrontiers in microbiology · 2022Article
- Article
- NONU-1 Encodes a Conserved Endonuclease Required for mRNA Translation Surveillance.Cell reports · 2020Article
- A bacterial DNA repair pathway specific to a natural antibiotic.Molecular microbiology · 2019Article
- Molecular basis for the functions of a bacterial MutS2 in DNA repair and recombination.DNA repair · 2017Article
- PPR-SMR protein SOT1 has RNA endonuclease activity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- MutS2 Promotes Homologous Recombination in Bacillus subtilis.Journal of bacteriology · 2017Article
- Noncanonical views of homology-directed DNA repair.Genes & development · 2016Review
- Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function.BMC microbiology · 2016Article
- Structure-based functional identification of Helicobacter pylori HP0268 as a nuclease with both DNA nicking and RNase activities.Nucleic acids research · 2015Article
- The nucleotide excision repair system of Borrelia burgdorferi is the sole pathway involved in repair of DNA damage by UV light.Journal of bacteriology · 2013Article
- Postreplicative mismatch repair.Cold Spring Harbor perspectives in biology · 2013Review
- Characterization of multi-functional properties and conformational analysis of MutS2 from Thermotoga maritima MSB8.PloS one · 2012Article
- Two new subfamilies of DNA mismatch repair proteins (MutS) specifically abundant in the marine environment.The ISME journal · 2011Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA recombination events need to be strictly regulated, because an increase in the recombinational frequency causes unfavorable alteration of genetic information. Recent studies revealed the existence of a novel anti-recombination enzyme, MutS2. However, the mechanism by which MutS2 inhibits homologous recombination has been unknown. Previously, we found that Thermus thermophilus MutS2 (ttMutS2) harbors an endonuclease activity and that this activity is confined to the C-terminal domain, whose amino acid sequence is widely conserved in a variety of proteins with unknown function from almost all organisms ranging from bacteria to man. In this study, we determined the crystal structure of the ttMutS2 endonuclease domain at 1.7-angstroms resolution, which resembles the structure of the DNase I-like catalytic domain of Escherichia coli RNase E, a sequence-nonspecific endonuclease. The N-terminal domain of ttMutS2, however, recognized branched DNA structures, including the Holliday junction and D-loop structure, a primary intermediate in homologous recombination. The full-length of ttMutS2 digested the branched DNA structures at the junction. These results indicate that ttMutS2 suppresses homologous recombination through a novel mechanism involving resolution of early intermediates.
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