ArticleThe Journal of biological chemistry2011
A mechanism for single-stranded DNA-binding protein (SSB) displacement from single-stranded DNA upon SSB-RecO interaction.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- Nanoscale Analysis of SSB-RecO Interplay in SSB Interaction with the Target.International journal of molecular sciences · 2026Article
- Involvement of the OB-fold and the C-terminal acidic tip of SSB in its interaction with RecO from Thermus thermophilus HB8.Journal of biochemistry · 2026Article
- Spatiotemporal characterization of single-stranded DNA intermediates after UV irradiation: II. Rapid growth and effects of recA and recJ.PLoS genetics · 2026Article
- The Role of the RecFOR Complex in Genome Stability.International journal of molecular sciences · 2025Review
- The intrinsically disordered linker in the single-stranded DNA-binding protein influences DNA replication restart and recombination pathways inJournal of bacteriology · 2024Article
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
- Mechanism of RecF-RecO-RecR cooperation in bacterial homologous recombination.Nature structural & molecular biology · 2023Article
- Allosteric effects of E. coli SSB and RecR proteins on RecO protein binding to DNA.Nucleic acids research · 2023Article
- OB-fold Families of Genome Guardians: A Universal Theme Constructed From the Small β-barrel Building Block.Frontiers in molecular biosciences · 2022Review
- The mechanism of action of the SSB interactome reveals it is the first OB-fold family of genome guardians in prokaryotes.Protein science : a publication of the Protein Society · 2021Review
- Single-molecule insight into stalled replication fork rescue in Escherichia coli.Nucleic acids research · 2021Review
- Allosteric effects of SSB C-terminal tail on assembly of E. coli RecOR proteins.Nucleic acids research · 2021Article
- Precise sequencing of single protected-DNA fragment molecules for profiling of protein distribution and assembly on DNA.Chemical science · 2021Article
- Article
- ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair.Scientific reports · 2018Article
- The PL6-Family Plasmids ofFrontiers in microbiology · 2018Article
- RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.Nucleic acids research · 2017Article
- RecA-SSB Interaction Modulates RecA Nucleoprotein Filament Formation on SSB-Wrapped DNA.Scientific reports · 2017Article
- Article
- Structural mechanisms of PriA-mediated DNA replication restart.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Displacement of single-stranded DNA (ssDNA)-binding protein (SSB) from ssDNA is necessary for filament formation of RecA on ssDNA to initiate homologous recombination. The interaction between RecO and SSB is considered to be important for SSB displacement; however, the interaction has not been characterized at the atomic level. In this study, to clarify the mechanism underlying SSB displacement from ssDNA upon RecO binding, we examined the interaction between Thermus thermophilus RecO and cognate SSB by NMR analysis. We found that SSB interacts with the C-terminal positively charged region of RecO. Based on this result, we constructed some RecO mutants. The R127A mutant had considerably decreased binding affinity for SSB and could not anneal SSB-coated ssDNAs. Further, the mutant in the RecOR complex prevented the recovery of ssDNA-dependent ATPase activity of RecA from inhibition by SSB. These results indicated that the region surrounding Arg-127 is the binding site of SSB. We also performed NMR analysis using the C-terminal peptide of SSB and found that the acidic region of SSB is involved in the interaction with RecO, as seen in other protein-SSB interactions. Taken together with the findings of previous studies, we propose a model for SSB displacement from ssDNA where the acidic C-terminal region of SSB weakens the ssDNA binding affinity of SSB when the dynamics of the C-terminal region are suppressed by interactions with other proteins, including RecO.
Indexed as
Identifiers
What OpenQuestion holds
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.