• Medientyp: E-Artikel
  • Titel: Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro
  • Beteiligte: Kachkin, Daniel V.; Volkov, Kirill V.; Sopova, Julia V.; Bobylev, Alexander G.; Fedotov, Sergei A.; Inge-Vechtomov, Sergei G.; Galzitskaya, Oxana V.; Chernoff, Yury O.; Rubel, Aleksandr A.; Aksenova, Anna Y.
  • Erschienen: MDPI AG, 2022
  • Erschienen in: International Journal of Molecular Sciences, 23 (2022) 19, Seite 11657
  • Sprache: Englisch
  • DOI: 10.3390/ijms231911657
  • ISSN: 1422-0067
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: RAD51 is a central protein of homologous recombination and DNA repair processes that maintains genome stability and ensures the accurate repair of double-stranded breaks (DSBs). In this work, we assessed amyloid properties of RAD51 in vitro and in the bacterial curli-dependent amyloid generator (C-DAG) system. Resistance to ionic detergents, staining with amyloid-specific dyes, polarized microscopy, transmission electron microscopy (TEM), X-ray diffraction and other methods were used to evaluate the properties and structure of RAD51 aggregates. The purified human RAD51 protein formed detergent-resistant aggregates in vitro that had an unbranched cross-β fibrillar structure, which is typical for amyloids, and were stained with amyloid-specific dyes. Congo-red-stained RAD51 aggregates demonstrated birefringence under polarized light. RAD51 fibrils produced sharp circular X-ray reflections at 4.7 Å and 10 Å, demonstrating that they had a cross-β structure. Cytoplasmic aggregates of RAD51 were observed in cell cultures overexpressing RAD51. We demonstrated that a key protein that maintains genome stability, RAD51, has amyloid properties in vitro and in the C-DAG system and discussed the possible biological relevance of this observation.
  • Zugangsstatus: Freier Zugang