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.
Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro
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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.