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TitleDSS1 and ssDNA regulate oligomerization of BRCA2.
Journal, issue, pagesNucleic Acids Res, Vol. 48, Issue 14, Page 7818-7833, Year 2020
Publish dateAug 20, 2020
AuthorsHang Phuong Le / Xiaoyan Ma / Jorge Vaquero / Megan Brinkmeyer / Fei Guo / Wolf-Dietrich Heyer / Jie Liu /
PubMed AbstractThe tumor suppressor BRCA2 plays a key role in initiating homologous recombination by facilitating RAD51 filament formation on single-stranded DNA. The small acidic protein DSS1 is a crucial partner ...The tumor suppressor BRCA2 plays a key role in initiating homologous recombination by facilitating RAD51 filament formation on single-stranded DNA. The small acidic protein DSS1 is a crucial partner to BRCA2 in this process. In vitro and in cells (1,2), BRCA2 associates into oligomeric complexes besides also existing as monomers. A dimeric structure was further characterized by electron microscopic analysis (3), but the functional significance of the different BRCA2 assemblies remains to be determined. Here, we used biochemistry and electron microscopic imaging to demonstrate that the multimerization of BRCA2 is counteracted by DSS1 and ssDNA. When validating the findings, we identified three self-interacting regions and two types of self-association, the N-to-C terminal and the N-to-N terminal interactions. The N-to-C terminal self-interaction of BRCA2 is sensitive to DSS1 and ssDNA. The N-to-N terminal self-interaction is modulated by ssDNA. Our results define a novel role of DSS1 to regulate BRCA2 in an RPA-independent fashion. Since DSS1 is required for BRCA2 function in recombination, we speculate that the monomeric and oligomeric forms of BRCA2 might be active for different cellular events in recombinational DNA repair and replication fork stabilization.
External linksNucleic Acids Res / PubMed:32609828 / PubMed Central
MethodsEM (single particle)
Resolution14.6 - 17.1 Å
Structure data

EMDB-20348:
EM structure of human tumor suppressor BRCA2 protein bound to human DSS1 protein and ssDNA without crosslinking
Method: EM (single particle) / Resolution: 17.1 Å

EMDB-21998:
EM structure of human tumor suppressor bound to human DSS1 protein and ssDNA with crosslinking
Method: EM (single particle) / Resolution: 14.6 Å

Source
  • Homo sapiens (human)

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