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A diRNA-protein scaffold module mediates SMC5/6 recruitment in plant DNA repair.
- Source :
-
The Plant cell [Plant Cell] 2022 Sep 27; Vol. 34 (10), pp. 3899-3914. - Publication Year :
- 2022
-
Abstract
- In eukaryotes, the STRUCTURAL MAINTENANCE OF CHROMOSOME 5/6 (SMC5/6) complex is critical to maintaining chromosomal structures around double-strand breaks (DSBs) in DNA damage repair. However, the recruitment mechanism of this conserved complex at DSBs remains unclear. In this study, using Arabidopsis thaliana as a model, we found that SMC5/6 localization at DSBs is dependent on the protein scaffold containing INVOLVED IN DE NOVO 2 (IDN2), CELL DIVISION CYCLE 5 (CDC5), and ALTERATION/DEFICIENCY IN ACTIVATION 2B (ADA2b), whose recruitment is further mediated by DNA-damage-induced RNAs (diRNAs) generated from DNA regions around DSBs. The physical interactions of protein components including SMC5-ADA2b, ADA2b-CDC5, and CDC5-IDN2 result in formation of the protein scaffold. Further analysis indicated that the DSB localization of IDN2 requires its RNA-binding activity and ARGONAUTE 2 (AGO2), indicating a role for the AGO2-diRNA complex in this process. Given that most of the components in the scaffold are conserved, the mechanism presented here, which connects SMC5/6 recruitment and small RNAs, will improve our understanding of DNA repair mechanisms in eukaryotes.<br /> (© American Society of Plant Biologists 2022. All rights reserved. For permissions, please email: journals.permissions@oup.com.)
- Subjects :
- Cell Cycle Proteins genetics
Cell Cycle Proteins metabolism
DNA Breaks, Double-Stranded
DNA Damage genetics
DNA Repair genetics
DNA, Plant metabolism
RNA genetics
Transcription Factors metabolism
Arabidopsis genetics
Arabidopsis metabolism
Arabidopsis Proteins genetics
Arabidopsis Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1532-298X
- Volume :
- 34
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- The Plant cell
- Publication Type :
- Academic Journal
- Accession number :
- 35775944
- Full Text :
- https://doi.org/10.1093/plcell/koac191