Involvement of the OB-fold and the C-terminal acidic tip of SSB in its interaction with RecO from Thermus thermophilus HB8

Clicks: 1
ID: 317491
2026
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal

Ranked #29 of 36 articles by views in The Journal of Biochemistry

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
In bacterial homologous recombination, the single-stranded DNA (ssDNA)-binding protein (SSB) coats exposed ssDNA to protect it but simultaneously inhibits RecA filament nucleation. RecO, a recombination mediator, overcomes this inhibition by interacting with SSB and displacing it from ssDNA. This SSB-RecO interaction has long been considered to rely primarily on the conserved C-terminal acidic tip (C-tip) of SSB. Here, using domain-truncated SSB variants from Thermus thermophilus HB8, we show that RecO directly binds both the SSB oligonucleotide/oligosaccharide-binding fold (OB-fold) and the C-tip. These two contacts make distinct contributions to RecO's mediator functions. Arg127 in RecO contributes to recognition of the SSB C-tip and to double-stranded DNA (dsDNA) binding, the latter of which is suppressed by the SSB C-tip. In RecO-mediated ssDNA annealing, the SSB C-tip primarily modulates SSB dynamics on ssDNA rather than directly activating RecO. Moreover, stable assembly of the SSB-RecO-RecR ternary complex requires the SSB C-tip. Our findings support a mechanism in which the SSB C-tip modulates RecO function and governs SSB behavior on ssDNA, whereas the OB-fold provides additional contacts whose functional contributions remain to be elucidated.
Reference Key
openalex_W7164896633 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Kazuki Kobayashi, Masao Inoue, K Fukui, Riku Aono, Anna Ochi, Ryoji Masui, Hisaaki Mihara
Journal The Journal of Biochemistry
Year 2026
DOI
10.1093/jb/mvag042
URL
https://doi.org/10.1093/jb/mvag042
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.