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| Title | The cryo-EM structure of full-length RAD52 protein contains an undecameric ring. |
|---|---|
| Journal, issue, pages | FEBS Open Bio, Vol. 13, Issue 3, Page 408-418, Year 2023 |
| Publish date | Feb 9, 2023 |
 Authors | Chiaki Kinoshita / Yoshimasa Takizawa / Mika Saotome / Shun Ogino / Hitoshi Kurumizaka / Wataru Kagawa /  |
| PubMed Abstract | 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 ...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. |
 External links | FEBS Open Bio / PubMed:36707939 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.48 Å |
| Structure data | EMDB-34430, PDB-8h1p: |
| Source |
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 Keywords |  RECOMBINATION / double-strand break repair / single strand annealing protein / DNA binding protein / self-oligomerization |
