Item request has been placed! ×
Item request cannot be made. ×
loading  Processing Request

Physical interactions between MCM and Rad51 facilitate replication fork lesion bypass and ssDNA gap filling by non-recombinogenic functions

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
اقرأ أكثر حفظ في قائمتي
  • معلومة اضافية
    • Contributors:
      Cabello-Lobato,MJ; González-Garrido,C; Cano-Linares,MI; Yáñez-Vílchez,A; Morillo-Huesca,M; Roldán-Romero,JM; Vicioso,M; González-Prieto,R; Prado,F Centro Andaluz de Biología Molecular y Medicina Regenerativa–CABIMER, Consejo Superior de Investigaciones Científicas; Universidad de Sevilla; Universidad Pablo de Olavide; Seville, Spain. Wong,RP; Ulrich,HD Institute of Molecular Biology (IMB), Mainz, Germany. Cabello-Lobato,MJ : Manchester Cancer Research Centre, Division of Cancer Sciences, University of Manchester, Manchester, UK. González-Prieto,R Department of Cell and Chemical Biology, Leiden University Medical Center, Leiden, the Netherlands.; This work was supported by grants BFU2015-63698-P and PGC2018-099182-B-I00 (to F.P.) from the Spanish government, and project-ID 393547839-SFB1361 (to H.D.U.) from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation). M.J.C.-L., M.I.C.-L., C.G.-G, A.Y.-V., and R.G.-P were recipients of pre-doctoral training grants from the Spanish government.
    • بيانات النشر:
      Cell Press
    • الموضوع:
      2021
    • Collection:
      Sistema Sanitario Público de Andalucía (SSPA): Repositorio
    • نبذة مختصرة :
      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. ; Yes
    • File Description:
      application/pdf
    • ISSN:
      2211-1247
    • Relation:
      https://www.sciencedirect.com/science/article/pii/S2211124721008573?via%3Dihub; Cabello-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):109440; http://hdl.handle.net/10668/3669
    • الرقم المعرف:
      10.1016/j.celrep.2021.109440
    • الدخول الالكتروني :
      http://hdl.handle.net/10668/3669
      https://doi.org/10.1016/j.celrep.2021.109440
    • Rights:
      Attribution-NonCommercial-NoDerivatives 4.0 Internacional ; http://creativecommons.org/licenses/by-nc-nd/4.0/ ; Acceso abierto
    • الرقم المعرف:
      edsbas.EDC17CB9