Pepper RING-Type E3 Ligase CaFIRF1 Negatively Regulates the Protein Stability of Pepper Stress-Associated Protein, CaSAP14, in the Dehydration Stress Response.

Autor: Bae Y; Department of Life Science (BK21 program), Chung-Ang University, Seoul, Korea., Lim CW; Department of Life Science (BK21 program), Chung-Ang University, Seoul, Korea., Lee SC; Department of Life Science (BK21 program), Chung-Ang University, Seoul, Korea.
Jazyk: angličtina
Zdroj: Plant, cell & environment [Plant Cell Environ] 2024 Sep 13. Date of Electronic Publication: 2024 Sep 13.
DOI: 10.1111/pce.15147
Abstrakt: As part of the cellular stress response in plants, the ubiquitin-proteasome system (UPS) plays a crucial role in regulating the protein stability of stress-related transcription factors. Previous study has indicated that CaSAP14 is functionally involved in enhancing pepper plant tolerance to dehydration stress by modulating the expression of downstream genes. However, the comprehensive regulatory mechanism underlying CaSAP14 remains incompletely understood. Here, we identified a RING-type E3 ligase, CaFIRF1, which interacts with and ubiquitinates CaSAP14. Pepper plants with silenced CaFIRF1 exhibited a dehydration-tolerant phenotype when subjected to dehydration stress, while overexpression of CaFIRF1 in pepper and Arabidopsis resulted in reduced dehydration tolerance. Co-silencing of CaFIRF1 and CaSAP14 in pepper increased sensitivity to dehydration, suggesting that CaFIRF1 acts upstream of CaSAP14. A cell-free degradation analysis demonstrated that silencing of CaFIRF1 led to decreased CaSAP14 protein degradation, implicating CaFIRF1 in the regulation of CaSAP14 protein via the 26S proteasomal degradation pathway. Our findings suggest a mechanism by which CaFIRF1 mediates the ubiquitin-dependent proteasomal degradation of CaSAP14, thereby influencing the response of pepper plants to dehydration stress.
(© 2024 John Wiley & Sons Ltd.)
Databáze: MEDLINE
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