Biochemical characterization of the RNA-binding and RNA-DNA strand exchange activities of the human RAD52 protein.
DNA repair
RNA
homologous recombination
intrinsically disordered region
protein-nucleic acid interaction
Journal
Journal of biochemistry
ISSN: 1756-2651
Titre abrégé: J Biochem
Pays: England
ID NLM: 0376600
Informations de publication
Date de publication:
30 Jun 2023
30 Jun 2023
Historique:
received:
14
12
2022
revised:
04
02
2023
accepted:
17
02
2023
medline:
3
7
2023
pubmed:
23
2
2023
entrez:
22
2
2023
Statut:
ppublish
Résumé
RAD52 is a single-stranded DNA (ssDNA) binding protein that functions in the repair of DNA double-strand breaks (DSBs) by promoting the annealing of complementary DNA strands. RAD52 may also play an important role in an RNA transcript-dependent type of DSB repair, in which it reportedly binds to RNA and mediates the RNA-DNA strand exchange reaction. However, the mechanistic details of these functions are still unclear. In the present study, we utilized the domain fragments of RAD52 to biochemically characterize the single-stranded RNA (ssRNA) binding and RNA-DNA strand exchange activities of RAD52. We found that the N-terminal half of RAD52 is primarily responsible for both activities. By contrast, significant differences were observed for the roles of the C-terminal half in RNA-DNA and DNA-DNA strand exchange reactions. The C-terminal fragment stimulated the inverse RNA-DNA strand exchange activity displayed by the N-terminal fragment in trans, whereas the trans stimulatory effect by the C-terminal fragment was not observed in the inverse DNA-DNA or forward RNA-DNA strand exchange reactions. These results suggest the specific function of the C-terminal half of RAD52 in RNA-templated DSB repair.
Identifiants
pubmed: 36811351
pii: 7051043
doi: 10.1093/jb/mvad019
pmc: PMC10312132
doi:
Substances chimiques
DNA
9007-49-2
DNA, Single-Stranded
0
DNA-Binding Proteins
0
Rad51 Recombinase
EC 2.7.7.-
Rad52 DNA Repair and Recombination Protein
0
RAD52 protein, human
0
RNA
63231-63-0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
59-69Informations de copyright
© The Author(s) 2023. Published by Oxford University Press on behalf of the Japanese Biochemical Society.
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