Human AAA+ ATPase FIGNL1 suppresses RAD51-mediated ultra-fine bridge formation.

ABSTRACT: RAD51 filament is crucial for the homology-dependent repair of DNA double-strand breaks and stalled DNA replication fork protection. Positive and negative regulators control RAD51 filament assembly and disassembly. RAD51 is vital for genome integrity but excessive accumulation of RAD51 on chromatin causes genome instability and growth defects. However, the detailed mechanism underlying RAD51 disassembly by negative regulators and the physiological consequence of abnormal RAD51 persistence remain largely unknown. Here, we report the role of the human AAA+ ATPase FIGNL1 in suppressing a novel type of RAD51-mediated genome instability. FIGNL1 knockout human cells were defective in RAD51 dissociation after replication fork restart and accumulated ultra-fine chromosome bridges (UFBs), whose for

SUBMITTER: Matsuzaki K 

PROVIDER: S-EPMC11162793 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature