Interaction with single-stranded DNA-binding protein modulates Escherichia coli RadD DNA repair activities.

ABSTRACT: The bacterial RadD enzyme is important for multiple genome maintenance pathways, including RecA DNA strand exchange and RecA-independent suppression of DNA crossover template switching. However, much remains unknown about the precise roles of RadD. One potential clue into RadD mechanisms is its direct interaction with the single-stranded DNA binding protein (SSB), which coats single-stranded DNA exposed during genome maintenance reactions in cells. Interaction with SSB stimulates the ATPase activity of RadD. To probe the mechanism and importance of RadD-SSB complex formation, we identified a pocket on RadD that is essential for binding SSB. In a mechanism shared with many other SSB-interacting proteins, RadD uses a hydrophobic pocket framed by basic residues to bind the C-terminal end of S

SUBMITTER: Osorio Garcia MA 

PROVIDER: S-EPMC10238739 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature