A structural phylogenetic tree of Rad52 and its annealase superfamily.

ABSTRACT: Rad52, a highly conserved eukaryotic protein, plays a crucial role in DNA repair, particularly in double-strand break repair. Recent findings reveal that its distinct structural features, including a characteristic β-sheet and β-hairpin motif, are shared with the lambda phage single-strand annealing protein, Redβ, and other prokaryotic single-strand annealing proteins (SSAPs), indicating a common superfamily. Our analysis of over 10,000 SSAPs across all domains of life supports this hypothesis, confirming the presence of the characteristic motif despite variations in size and composition. We found that archaea, representing only 1% of the studied proteins, exhibit most of these variations as reflected by their spread across the phylogenetic tree, whereas eukaryotes exh

SUBMITTER: Al-Fatlawi A 

PROVIDER: S-EPMC11783212 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature