Mechanism of AAA+ ATPase-mediated RuvAB-Holliday junction branch migration.

ABSTRACT: The Holliday junction is a key intermediate formed during DNA recombination across all kingdoms of life¹. In bacteria, the Holliday junction is processed by two homo-hexameric AAA+ ATPase RuvB motors, which assemble together with the RuvA-Holliday junction complex to energize the strand-exchange reaction². Despite its importance for chromosome maintenance, the structure and mechanism by which this complex facilitates branch migration are unknown. Here, using time-resolved cryo-electron microscopy, we obtained structures of the ATP-hydrolysing RuvAB complex in seven distinct conformational states, captured during assembly and processing of a Holliday junction. Five structures together resolve the complete nucleotide cycle and reveal the spatiotemporal relationship betw

SUBMITTER: Wald J 

PROVIDER: S-EPMC9477746 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature