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
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
408-418Informations 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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