دورية أكاديمية
أعرض في EDS

Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro .

التفاصيل البيبلوغرافية
العنوان: Human RAD51 Protein Forms Amyloid-like Aggregates In Vitro .
المؤلفون: Kachkin DV; Laboratory of Amyloid Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Volkov KV; Research Resource Center 'Molecular and Cell Technologies', Research Park, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia., Sopova JV; Laboratory of Amyloid Biology, St. Petersburg State University, 199034 St. Petersburg, Russia.; Center of Transgenesis and Genome Editing, St. Petersburg State University, 199034 St. Petersburg, Russia., Bobylev AG; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 3 Institutskaya St., 142290 Moscow, Russia., Fedotov SA; Laboratory of Amyloid Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Inge-Vechtomov SG; Department of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia., Galzitskaya OV; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 3 Institutskaya St., 142290 Moscow, Russia.; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia., Chernoff YO; School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332-2000, USA., Rubel AA; Laboratory of Amyloid Biology, St. Petersburg State University, 199034 St. Petersburg, Russia.; Department of Genetics and Biotechnology, St. Petersburg State University, 199034 St. Petersburg, Russia., Aksenova AY; Laboratory of Amyloid Biology, St. Petersburg State University, 199034 St. Petersburg, Russia.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2022 Oct 01; Vol. 23 (19). Date of Electronic Publication: 2022 Oct 01.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: Detergents* , Rad51 Recombinase*/chemistry, Amyloid/metabolism ; Amyloidogenic Proteins/chemistry ; Coloring Agents ; Genomic Instability ; Humans ; Protein Aggregates
مستخلص: 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.
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معلومات مُعتمدة: 20-14-00148 Russian Science Foundation; 18-04-00799 Russian Foundation for Basic Research
فهرسة مساهمة: Keywords: RAD51; X-ray diffraction; amyloid; amyloidogenesis; functional amyloids; protein aggregation; protein fibrils
المشرفين على المادة: 0 (Amyloid)
0 (Amyloidogenic Proteins)
0 (Coloring Agents)
0 (Detergents)
0 (Protein Aggregates)
EC 2.7.7.- (RAD51 protein, human)
EC 2.7.7.- (Rad51 Recombinase)
تواريخ الأحداث: Date Created: 20221014 Date Completed: 20221017 Latest Revision: 20221019
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC9570251
DOI: 10.3390/ijms231911657
PMID: 36232958
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms231911657