CryoEM micrographs collected on a RAD51-ADP filament sample
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ABSTRACT:
SUBMITTER: Luca Pellegrini
PROVIDER: EMPIAR-11696 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
A metal ion-dependent mechanism of RAD51 nucleoprotein filament disassembly.
Appleby Robert R Bollschweiler Daniel D Chirgadze Dimitri Y DY Joudeh Luay L Pellegrini Luca L
iScience 20230425 5
The RAD51 ATPase polymerizes on single-stranded DNA to form nucleoprotein filaments (NPFs) that are critical intermediates in the reaction of homologous recombination. ATP binding maintains the NPF in a competent conformation for strand pairing and exchange. Once strand exchange is completed, ATP hydrolysis licenses the filament for disassembly. Here we show that the ATP-binding site of the RAD51 NPF contains a second metal ion. In the presence of ATP, the metal ion promotes the local folding of ...[more]
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