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CryoEM micrographs of RAD51 filaments on dsDNA bound by the BRCA2 c-terminus

ABSTRACT:

SUBMITTER: Luca Pellegrini

PROVIDER: EMPIAR-11794 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural basis for stabilisation of the RAD51 nucleoprotein filament by BRCA2.

Appleby Robert R Joudeh Luay L Cobbett Katie K Pellegrini Luca L

Nature communications 20231102 1

The BRCA2 tumour suppressor protein preserves genomic integrity via interactions with the DNA-strand exchange RAD51 protein in homology-directed repair. The RAD51-binding TR2 motif at the BRCA2 C-terminus is essential for protection and restart of stalled replication forks. Biochemical evidence shows that TR2 recognises filamentous RAD51, but existing models of TR2 binding to RAD51 lack a structural basis. Here we used cryo-electron microscopy and structure-guided mutagenesis to elucidate the me ...[more]

PMID: 37919288

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