Structural and functional investigation of DinG containing a 3'-5' exonuclease domain.

ABSTRACT: Damage-inducible gene G (DinG), a bacterial homolog of SF2 helicase, has been extensively studied in Escherichia coli. However, the structural and functional characteristics of DinG homologs fused with an N-terminal 3'-5' exonuclease domain, such as Staphylococcus aureus DinG (SaDinG), remain unexplored. In this study, we demonstrate that SaDinG possesses 3'-5' exonuclease activity and exhibits 5'-3' helicase activity on diverse DNA substrates, including splayed duplexes, 5'-overhangs, double flaps, bubbles, and gapped duplexes, resolving prior ambiguities about its biochemical functions. Intriguingly, both enzymatic activities were inhibited by elevated ATP concentrations, suggesting a potential ATP-dependent regulatory mechanism in vivo. We determined the crystal str

SUBMITTER: Gao T 

PROVIDER: S-EPMC12345164 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature