ArticleNucleic acids research2018
The bacterial Mre11-Rad50 homolog SbcCD cleaves opposing strands of DNA by two chemically distinct nuclease reactions.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Structure and activation mechanism of a Lamassu phage and plasmid defense system.Nature structural & molecular biology · 2025Article
- Phage-encoded TelN inhibits bacterial Mre11-Rad50 nuclease to protect hairpin telomeres.The EMBO journal · 2025Article
- Dynamic conformations of the P. furiosus MR-DNA complex link Mre11 nuclease activity to DNA-stimulated Rad50 ATP hydrolysis.Communications biology · 2025Article
- Telomeric transposons are pervasive in linear bacterial genomes.Science (New York, N.Y.) · 2025Article
- Structure ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- The dynamic nature of the Mre11-Rad50 DNA break repair complex.Progress in biophysics and molecular biology · 2021Review
- Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus.Journal of microbiology (Seoul, Korea) · 2021Article
- A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Pseudomonas putida MPE, a manganese-dependent endonuclease of the binuclear metallophosphoesterase superfamily, incises single-strand DNA in two orientations to yield a mixture of 3'-PO4 and 3'-OH termini.Nucleic acids research · 2021Article
- Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions.Journal of molecular biology · 2020Article
- Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms.Nucleic acids research · 2020Article
- RecBCD, SbcCD and ExoI process a substrate created by convergent replisomes to complete DNA replication.Molecular microbiology · 2019Article
- Processing of DNA Double-Strand Breaks by the MRX Complex in a Chromatin Context.Frontiers in molecular biosciences · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Mre11-Rad50 complex is a DNA double-strand break sensor that cleaves blocked DNA ends and hairpins by an ATP-dependent endo/exonuclease activity for subsequent repair. For that, Mre11-Rad50 complexes, including the Escherichia coli homolog SbcCD, can endonucleolytically cleave one or both strands near a protein block and process free DNA ends via a 3'-5' exonuclease, but a unified basis for these distinct activities is lacking. Here we analyzed DNA binding, ATPase and nuclease reactions on different DNA substrates. SbcCD clips terminal bases of both strands of the DNA end in the presence of ATPγS. It introduces a DNA double-strand break around 20-25 bp from a blocked end after multiple rounds of ATP hydrolysis in a reaction that correlates with local DNA meltability. Interestingly, we find that nuclease reactions on opposing strands are chemically distinct, leaving a 5' phosphate on one strand, but a 3' phosphate on the other strand. Collectively, our results identify an unexpected chemical variability of the nuclease, indicating that the complex is oriented at a free DNA end and facing a block with opposite polarity. This suggests a unified model for ATP-dependent endo- and exonuclease reactions at internal DNA near a block and at free DNA ends.
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