CHENG-YANG HUANG2026-10-162026-10-162025-09-01Pure ID: 14884661Pure UUID: 50ad6a2e-adf4-4b20-bd6c-a20896aa26bc10.31083/FBL36350https://www.scopus.com/pages/publications/105017880763https://scholars.csmu.edu.tw/handle/123456789/22254To maintain genome stability, the coordinated actions of multiple proteins and protein complexes, which are collectively known as genome guardians, are required. In prokaryotes, one such 20-member genome guardian family known as the single-stranded DNA binding protein (SSB) interactome exists. Proteins within this essential family contain oligonucleotide/oligosaccharide-binding folds (OB-fold). These structurally conserved OB-folds bind to the intrinsically disordered linkers characteristic of SSB protein C-termini, resulting in partner regulation. The mechanism of binding employed is similar to that utilized by Src homology 3 domain (SH3) proteins in eukaryotes. Binding requires the interaction of conserved PXXP motifs in the SSB linker with the OB-fold in the partner. A second region of SSB C-termini, an 8-10 stretch of predominantly acidic amino acids functions to maintain the linker domain in a biologically active conformation, while simultaneously preventing it from adhering to the OB-folds of the SSB tetramer from which it emanates. In addition, this acidic domain also functions as a secondary binding site docking with a distal site in the partner, stabilizing the linker/OBfold interactions. The interaction of an SSB with its partner proteins is genus-specific and results in the loading of partners onto the genome at various stages of the cell cycle thereby maintaining genome stability.enjournal article