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SUMOylation facilitates the assembly of a Nuclear Factor‐Y complex to enhance thermotolerance in Arabidopsis

Authors :
Junwen Huang
Junjie Huang
Qiyi Feng
Yaqiao Shi
Feige Wang
Kaiyong Zheng
Qize Huang
Jieming Jiang
Siyi Luo
Yun Xie
Danlu Han
Jianbin Lai
Chengwei Yang
Source :
Journal of Integrative Plant Biology. 65:692-702
Publication Year :
2023
Publisher :
Wiley, 2023.

Abstract

Heat stress (HS) has serious negative effects on plant development and has become a major threat to agriculture. A rapid transcriptional regulatory cascade has evolved in plants in response to HS. Nuclear Factor-Y (NF-Y) complexes are critical for this mechanism, but how NF-Y complexes are regulated remains unclear. In this study, we identified NF-YC10 (NF-Y subunit C10), a central regulator of the HS response in Arabidopsis thaliana, as a substrate of SUMOylation, an important post-translational modification. Biochemical analysis showed that the SUMO ligase SIZ1 (SAP AND MIZ1 DOMAIN-CONTAINING LIGASE1) interacts with NF-YC10 and enhances its SUMOylation during HS. The SUMOylation of NF-YC10 facilitates its interaction with and the nuclear translocation of NF-YB3, in which the SUMO interaction motif (SIM) is essential for its efficient association with NF-YC10. Further functional analysis indicated that the SUMOylation of NF-YC10 and the SIM of NF-YB3 are critical for HS-responsive gene expression and plant thermotolerance. These findings uncover a role for the SIZ1-mediated SUMOylation of NF-YC10 in NF-Y complex assembly under HS, providing new insights into the role of a post-translational modification in regulating transcription during abiotic stress responses in plants.

Details

ISSN :
17447909 and 16729072
Volume :
65
Database :
OpenAIRE
Journal :
Journal of Integrative Plant Biology
Accession number :
edsair.doi.dedup.....46f8cbab2b0d6b7ed6cc2bce77d80b34
Full Text :
https://doi.org/10.1111/jipb.13396