ArticleNucleic acids research2021
Allosteric effects of SSB C-terminal tail on assembly of E. coli RecOR proteins.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The Role of the RecFOR Complex in Genome Stability.International journal of molecular sciences · 2025Review
- DNA damage alters binding conformations of E. coli single-stranded DNA-binding protein.Biophysical journal · 2023Article
- Structural and Biochemical Analysis of the Recombination Mediator Protein RecR fromInternational journal of molecular sciences · 2023Article
- RecF protein targeting to postreplication (daughter strand) gaps I: DNA binding by RecF and RecFR.Nucleic acids research · 2023Article
- Mechanism of RecF-RecO-RecR cooperation in bacterial homologous recombination.Nature structural & molecular biology · 2023Article
- Structural Adaptation of the Single-Stranded DNA-Binding Protein C-Terminal to DNA Metabolizing Partners Guides Inhibitor Design.Pharmaceutics · 2023Article
- Allosteric effects of E. coli SSB and RecR proteins on RecO protein binding to DNA.Nucleic acids research · 2023Article
- The Escherichia coli clamp loader rapidly remodels SSB on DNA to load clamps.Nucleic acids research · 2022Article
- Crystal Structure of the Recombination Mediator Protein RecO fromInternational journal of molecular sciences · 2022Article
- Towards a better understanding of antimicrobial resistance dissemination: what can be learnt from studying model conjugative plasmids?Military Medical Research · 2022Review
- Multi-start Evolutionary Nonlinear OpTimizeR (MENOTR): A hybrid parameter optimization toolbox.Biophysical chemistry · 2021Article
- Review
- Molecular insights into the prototypical single-stranded DNA-binding protein fromCritical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Escherichia coli RecO is a recombination mediator protein that functions in the RecF pathway of homologous recombination, in concert with RecR, and interacts with E. coli single stranded (ss) DNA binding (SSB) protein via the last 9 amino acids of the C-terminal tails (SSB-Ct). Structures of the E. coli RecR and RecOR complexes are unavailable; however, crystal structures from other organisms show differences in RecR oligomeric state and RecO stoichiometry. We report analytical ultracentrifugation studies of E. coli RecR assembly and its interaction with RecO for a range of solution conditions using both sedimentation velocity and equilibrium approaches. We find that RecR exists in a pH-dependent dimer-tetramer equilibrium that explains the different assembly states reported in previous studies. RecO binds with positive cooperativity to a RecR tetramer, forming both RecR4O and RecR4O2 complexes. We find no evidence of a stable RecO complex with RecR dimers. However, binding of RecO to SSB-Ct peptides elicits an allosteric effect, eliminating the positive cooperativity and shifting the equilibrium to favor a RecR4O complex. These studies suggest a mechanism for how SSB binding to RecO influences the distribution of RecOR complexes to facilitate loading of RecA onto SSB coated ssDNA to initiate homologous recombination.
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Registered trials
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