Lysine decrotonylation of glutathione peroxidase at lysine 220 site increases glutathione peroxidase activity to resist cold stress in chrysanthemum

Ecotoxicology and Environmental Safety

Beibei Jiang¹  Yuanzhi Pan¹  Yin Jia¹  Yunchen Luo¹  Fan Zhang¹  Lei Zhang¹  Yuchen Tian¹  Huiru Bai¹  Xin Li¹  Xiaohan Yang¹  Ping Lin¹  Xiaoqin Liao¹  Qinglin Liu¹  Yan Li² 

[1] Department of Ornamental Horticulture, Sichuan Agricultural University, 211 Huimin Road, Wenjiang District, Chengdu, Sichuan 611130, China;The Key Laboratory of Plant Resources Conservation and Germplasm Innovation in Mountainous Region, (Ministry of Education), Institute of Agro-Bioengineering and College of Life Sciences, Guizhou University, Guiyang 550025, Guizhou, China;

关键词: Chrysanthemum;    Cold resistance;    Glutathione peroxidase;    Low temperature stress;    Lysine decrotonylation;    ROS scavenging system;   

DOI  :  

来源: DOAJ

【 摘 要 】

Lysine crotonylation is a protein post-translational modification that has been newly discovered in recent years. There are few studies on the lysine crotonylation of proteins in plants, and their functions in response to cold stress are still unclear. In this study, the chrysanthemum (Chrysanthemum morifolium Ramat.) glutathione peroxidase (GPX) gene was selected and named DgGPX1, and was found to be responsive to low temperature. Overexpression of DgGPX1 improved the cold resistance of transgenic chrysanthemum by increasing GPX activity to reduce the accumulation of reactive oxygen species (ROS) under low-temperature conditions. Furthermore, the level of DgGPX1 lysine crotonylation at lysine (K) 220 decreased under low temperature in chrysanthemum. Lysine decrotonylation of DgGPX1 at K220 further increased GPX activity to reduce ROS accumulation under cold stress, and thereby enhanced the cold resistance of chrysanthemum. The above results show that lysine decrotonylation of DgGPX1 at K220 increases GPX activity to resist cold stress in chrysanthemum.

【 授权许可】

Unknown