%0 Generic
%A Cabello-Lobato, María J.
%A González-Garrido, Cristina
%A Cano-Linares, María I.
%A Wong, Ronald P.
%A Yáñez-Vílchez, Aurora
%A Morillo-Huesca, Macarena
%A Roldán-Romero, Juan M.
%A Vicioso, Marta
%A González-Prieto, Román
%A Ulrich, Helle D.
%A Prado, Félix
%T Physical interactions between MCM and Rad51 facilitate replication fork lesion bypass and ssDNA gap filling by non-recombinogenic functions
%D 2021
%U http://hdl.handle.net/10668/3669
%X The minichromosome maintenance (MCM) helicase physically interacts with the recombination proteins Rad51 and Rad52 from yeast to human cells. We show, in Saccharomyces cerevisiae, that these interactions occur within a nuclease-insoluble scaffold enriched in replication/repair factors. Rad51 accumulates in a MCM- and DNA-binding-independent manner and interacts with MCM helicases located outside of the replication origins and forks. MCM, Rad51, and Rad52 accumulate in this scaffold in G1 and are released during the S phase. In the presence of replication-blocking lesions, Cdc7 prevents their release from the scaffold, thus maintaining the interactions. We identify a rad51 mutant that is impaired in its ability to bind to MCM but not to the scaffold. This mutant is proficient in recombination but partially defective in single-stranded DNA (ssDNA) gap filling and replication fork progression through damaged DNA. Therefore, cells accumulate MCM/Rad51/Rad52 complexes at specific nuclear scaffolds in G1 to assist stressed forks through non-recombinogenic functions.
%K Cdc7
%K DNA damage
%K MCM
%K Rad51
%K Rad52
%K Homologous recombination
%K Replication
%K Componente 7 del complejo de mantenimiento de minicromosoma
%K Daño del ADN
%K Recombinasa Rad51
%K Proteína recombinante y reparadora de ADN Rad52
%K Recombinación homóloga
%K Replicación
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