期刊
PLANT CELL
卷 34, 期 10, 页码 3899-3914出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/plcell/koac191
关键词
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资金
- Major Program of Guangdong Basic and Applied Research [2019B030302006]
- National Natural Science Foundation of China [31871222, 31970531, 31771504, 32000493, 31771349]
- Natural Science Foundation of Guangdong [2018B030308002, 2020A1515010964, 2021A1515011151]
- Guangdong Modern Agro-industry Technology Research System [2021KJ114]
- China Postdoctoral Science Foundation [2018M643111]
- Program for Changjiang Scholars
- Guangdong Special Support Program of Young Top-Notch Talent in Science and Technology Innovation [2019TQ05N651]
- Pearl River Talent Plan [2019QN01N108]
This study reveals that localization of the SMC5/6 complex at double-strand breaks in plant cells is dependent on the protein scaffold consisting of IDN2, CDC5, and ADA2b, and this recruitment is further mediated by DNA damage-induced RNAs.
The localization of the SMC5/6 complex at double-strand breaks is dependent on the IDN2-CDC5-ADA2b protein scaffold, which is further mediated by DNA damage-induced RNAs in plant cells. 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.
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