The cryo-EM structure of full-length RAD52 protein contains an undecameric ring.

DNA annealing protein DNA double-strand break repair cryo-electron microscopy intrinsically disordered region oligomerisation ring structure

Journal

FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716

Informations de publication

Date de publication:
03 2023
Historique:
revised: 29 12 2022
received: 22 10 2022
accepted: 26 01 2023
pubmed: 29 1 2023
medline: 9 3 2023
entrez: 28 1 2023
Statut: ppublish

Résumé

The human RAD52 protein, which forms an oligomeric ring structure, is involved in DNA double-strand break repair. The N-terminal half of RAD52 is primarily responsible for self-oligomerisation and DNA binding. Crystallographic studies have revealed the detailed structure of the N-terminal half. However, only low-resolution structures have been reported for the full-length protein, and thus the structural role of the C-terminal half in self-oligomerisation has remained elusive. In this study, we determined the solution structure of the human RAD52 protein by cryo-electron microscopy (cryo-EM), at an average resolution of 3.5 Å. The structure revealed an undecameric ring that is nearly identical to the crystal structures of the N-terminal half. The cryo-EM map for the C-terminal half was poorly defined, indicating that the region is intrinsically disordered. The present cryo-EM structure provides important insights into the mechanistic roles played by the N-terminal and C-terminal halves of RAD52 during DNA double-strand break repair.

Identifiants

pubmed: 36707939
doi: 10.1002/2211-5463.13565
pmc: PMC9989933
doi:

Substances chimiques

Rad52 DNA Repair and Recombination Protein 0
DNA-Binding Proteins 0
DNA 9007-49-2
RAD52 protein, human 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

408-418

Informations de copyright

© 2023 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

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Auteurs

Chiaki Kinoshita (C)

Department of Chemistry, Graduate School of Science and Engineering, Meisei University, Tokyo, Japan.

Yoshimasa Takizawa (Y)

Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Japan.

Mika Saotome (M)

Department of Chemistry, Graduate School of Science and Engineering, Meisei University, Tokyo, Japan.

Shun Ogino (S)

Department of Chemistry, Graduate School of Science and Engineering, Meisei University, Tokyo, Japan.

Hitoshi Kurumizaka (H)

Laboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Japan.

Wataru Kagawa (W)

Department of Chemistry, Graduate School of Science and Engineering, Meisei University, Tokyo, Japan.

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Classifications MeSH