ArticleThe Journal of biological chemistry2014
RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- The Role of the RecFOR Complex in Genome Stability.International journal of molecular sciences · 2025Review
- A CRISPR-nonhomologous end-joining-based strategy for rapid and efficient gene disruption inmLife · 2025Article
- Surviving the storm: exploring the role of natural transformation in nutrition and DNA repair of stressedApplied and environmental microbiology · 2025Article
- Allosteric effects of E. coli SSB and RecR proteins on RecO protein binding to DNA.Nucleic acids research · 2023Article
- Allosteric effects of SSB C-terminal tail on assembly of E. coli RecOR proteins.Nucleic acids research · 2021Article
- TnMicrobiology (Reading, England) · 2021Article
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- Touch, act and go: landing and operating on nucleosomes.The EMBO journal · 2016Review
- RecF and RecR Play Critical Roles in the Homologous Recombination and Single-Strand Annealing Pathways of Mycobacteria.Journal of bacteriology · 2015Article
- Bacillus subtilis RecO and SsbA are crucial for RecA-mediated recombinational DNA repair.Nucleic acids research · 2015Article
- Replication Restart after Replication-Transcription Conflicts Requires RecA in Bacillus subtilis.Journal of bacteriology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Recombination mediator proteins (RMPs) are important for genome stability in all organisms. Several RMPs support two alternative reactions: initiation of homologous recombination and DNA annealing. We examined mechanisms of RMPs in both reactions with Mycobacterium smegmatis RecO (MsRecO) and demonstrated that MsRecO interacts with ssDNA by two distinct mechanisms. Zinc stimulates MsRecO binding to ssDNA during annealing, whereas the recombination function is zinc-independent and is regulated by interaction with MsRecR. Thus, different structural motifs or conformations of MsRecO are responsible for interaction with ssDNA during annealing and recombination. Neither annealing nor recombinase loading depends on MsRecO interaction with the conserved C-terminal tail of single-stranded (ss) DNA-binding protein (SSB), which is known to bind Escherichia coli RecO. However, similarly to E. coli proteins, MsRecO and MsRecOR do not dismiss SSB from ssDNA, suggesting that RMPs form a complex with SSB-ssDNA even in the absence of binding to the major protein interaction motif. We propose that alternative conformations of such complexes define the mechanism by which RMPs initiate the repair of stalled replication and support two different functions during recombinational repair of DNA breaks.
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Registered trials
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