"Central to HR is the RAD51 recombinase, whose assembly into a nucleoprotein filament is governed by five RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, XRCC3). Mutations in any of these proteins predispose individuals to multiple cancers or genetic disorders. These paralogs are thought to form two functionally separate complexes, BCDX2 and CX3, that act independently at different stages of HR."
"Here, we demonstrate that all five paralogs can assemble into a single, ATP-dependent BCDX2-CX3-RAD51 supercomplex. The architecture of this assembly bound to single-stranded DNA reveals a contiguous filament where the CX3 module stacks atop BCDX2, creating a protofilament template for RAD51 filament formation."
"We further identify a novel, RAD51B-independent DX2-CX3 complex (RAD51D-XRCC2-RAD51C-XRCC3) functioning as a stable RAD51 anchor on ssDNA, and we capture it in multiple states, including capping RAD51 filament segment."
DNA double-strand break repair through homologous recombination depends on RAD51 recombinase assembly, regulated by five RAD51 paralogs. These paralogs were previously thought to form two separate functional complexes operating independently. Cryoelectron microscopy reveals all five paralogs assemble into a unified BCDX2-CX3-RAD51 supercomplex. The CX3 module stacks atop BCDX2, creating a protofilament template for RAD51 filament formation on single-stranded DNA. Additionally, a novel RAD51B-independent DX2-CX3 complex functions as a stable RAD51 anchor, captured in multiple conformational states including capping RAD51 filament segments.
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