Cabello-Lobato, María J.González-Garrido, CristinaCano-Linares, María I.Wong, Ronald P.Yáñez-Vílchez, AuroraMorillo-Huesca, MacarenaRoldán-Romero, Juan M.Vicioso, MartaGonzález-Prieto, RománUlrich, Helle D.Prado, Félix2022-05-252022-05-252021-07-27Cabello-Lobato MJ, González-Garrido C, Cano-Linares MI, Wong RP, Yáñez-Vílchez A, Morillo-Huesca M, et al. Physical interactions between MCM and Rad51 facilitate replication fork lesion bypass and ssDNA gap filling by non-recombinogenic functions. Cell Rep. 2021 Jul 27;36(4):109440http://hdl.handle.net/10668/3669The 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.enAttribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/Cdc7DNA damageMCMRad51Rad52Homologous recombinationReplicationComponente 7 del complejo de mantenimiento de minicromosomaDaño del ADNRecombinasa Rad51Proteína recombinante y reparadora de ADN Rad52Recombinación homólogaReplicaciónMedical Subject Headings::Organisms::Eukaryota::Fungi::Ascomycota::Saccharomycetales::Saccharomyces::Saccharomyces cerevisiaeMedical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA DamageMedical Subject Headings::Chemicals and Drugs::Nucleic Acids, Nucleotides, and Nucleosides::Nucleic Acids::DNA::DNA, Single-StrandedMedical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Structures::Genome::Genome Components::DNA, Intergenic::Replication OriginMedical Subject Headings::Analytical, Diagnostic and Therapeutic Techniques and Equipment::Investigative Techniques::Models, Theoretical::Models, BiologicalMedical Subject Headings::Chemicals and Drugs::Macromolecular Substances::Multiprotein ComplexesMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Biochemical Processes::DNA Replication::S PhaseMedical Subject Headings::Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::DNA-Binding Proteins::Rad51 RecombinaseMedical Subject Headings::Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::DNA-Binding Proteins::Rad52 DNA Repair and Recombination ProteinMedical Subject Headings::Phenomena and Processes::Genetic Phenomena::Genetic Processes::Recombination, GeneticMedical Subject Headings::Anatomy::Cells::Cellular Structures::Intracellular Space::Cell Nucleus::Cell Nucleus Structures::Intranuclear Space::Nuclear MatrixMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Chemical Processes::Biochemical Processes::DNA Replicationconference presentation34320356Acceso abierto10.1016/j.celrep.2021.1094402211-1247