BRCA2 diffuses as oligomeric clusters with RAD51 and changes mobility after DNA damage in live cells.

ABSTRACT: Genome maintenance by homologous recombination depends on coordinating many proteins in time and space to assemble at DNA break sites. To understand this process, we followed the mobility of BRCA2, a critical recombination mediator, in live cells at the single-molecule level using both single-particle tracking and fluorescence correlation spectroscopy. BRCA2-GFP and -YFP were compared to distinguish diffusion from fluorophore behavior. Diffusive behavior of fluorescent RAD51 and RAD54 was determined for comparison. All fluorescent proteins were expressed from endogenous loci. We found that nuclear BRCA2 existed in oligomeric clusters, and exhibited heterogeneous mobility. DNA damage increased BRCA2 transient binding, presumably including binding to damaged sites. Despite its very different

SUBMITTER: Reuter M 

PROVIDER: S-EPMC4259808 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature