ArticleThe Journal of biological chemistry2010
RecN is a cohesin-like protein that stimulates intermolecular DNA interactions in vitro.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- RecN: A tunable switch for DNA repair choice and stress tolerance inBiodesign research · 2026Article
- Species-specific coevolution of RecA-RecN interfaces governs DNA double-strand break repair in Escherichia coli.PLoS genetics · 2026Article
- Structural switches: intracellular G-quadruplexes modulate DNA repair and genome maintenance inmBio · 2025Article
- The DR2416/DR2415 two-component system is responsible for the radioresistance of Deinococcus radiodurans.Antonie van Leeuwenhoek · 2025Article
- RecN and RecA orchestrate an ordered DNA supercompaction response following ciprofloxacin-induced DNA damage in Escherichia coli.Nucleic acids research · 2025Article
- The mismatch repair endonuclease MutLα tethers duplex regions of DNA together and relieves DNA torsional tension.Nucleic acids research · 2023Article
- The SMC-like RecN protein is at the crossroads of several genotoxic stress responses inFrontiers in microbiology · 2023Article
- SMC protein RecN drives RecA filament translocation for in vivo homology search.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protease-deficient SOS constitutive cells have RecN-dependent cell division phenotypes.Molecular microbiology · 2019Article
- Topological DNA-binding of structural maintenance of chromosomes-like RecN promotes DNA double-strand break repair inCommunications biology · 2019Article
- Rad50 ATPase activity is regulated by DNA ends and requires coordination of both active sites.Nucleic acids research · 2017Article
- The cohesin-like RecN protein stimulates RecA-mediated recombinational repair of DNA double-strand breaks.Nature communications · 2017Article
- Management of E. coli sister chromatid cohesion in response to genotoxic stress.Nature communications · 2017Article
- Cyclic AMP Receptor Protein Acts as a Transcription Regulator in Response to Stresses in Deinococcus radiodurans.PloS one · 2016Article
- A Decade of Biochemical and Structural Studies of the DNA Repair Machinery ofComputational and structural biotechnology journal · 2016Review
- Exploratory Investigation ofFrontiers in microbiology · 2016Article
- An Overview of the Molecular Mechanisms of Recombinational DNA Repair.Cold Spring Harbor perspectives in biology · 2015Review
- The Smc5-Smc6 heterodimer associates with DNA through several independent binding domains.Scientific reports · 2015Article
- Article
- MukBEF, a chromosomal organizer.Journal of molecular microbiology and biotechnology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The bacterial RecN protein is involved in the recombinational repair of DNA double-stranded breaks, and recN mutants are sensitive to DNA-damaging agents. Little is known about the biochemical function of RecN. Protein sequence analysis suggests that RecN is related to the SMC (structural maintenance of chromosomes) family of proteins, predicting globular N- and C-terminal domains connected by an extensive coil-coiled domain. The N- and C-domains contain the nucleotide-binding sequences Walker A and Walker B, respectively. We have purified the RecN protein from Deinococcus radiodurans and characterized its DNA-dependent and DNA-independent ATPase activity. The RecN protein hydrolyzes ATP with a k(cat) of 24 min(-1), and this rate is stimulated 4-fold by duplex DNA but not by single-stranded DNA. This DNA-dependent ATP turnover rate exhibits a dependence on the concentration of RecN protein, suggesting that RecN-RecN interactions are required for efficient ATP hydrolysis, and those interactions are stabilized only by duplex DNA. Finally, we show that RecN stimulates the intermolecular ligation of linear DNA molecules in the presence of DNA ligase. This DNA bridging activity is strikingly similar to that of the cohesin complex, an SMC family member, to which RecN is related.
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Registered trials
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.