Importation of chloroplast proteins under heat stress is facilitated by their SUMO conjugations

Summary Chloroplasts are hypersensitive to heat stress (HS). SUMOylation, a critical post‐translational modification, is conservatively involved in HS responses. However, the functional connection between SUMOylation and chloroplasts under HS remains to be studied. The bioinformatics, biochemistry,...

Full description

Saved in:
Bibliographic Details
Published in:The New phytologist 2022-07, Vol.235 (1), p.173-187
Main Authors: Zheng, Xiao‐Ting, Wang, Caijuan, Lin, Wenxiong, Lin, Chufang, Han, Danlu, Xie, Qi, Lai, Jianbin, Yang, Chengwei
Format: Article
Language:English
Subjects:
Arabidopsis
AtSIZ1
Bioinformatics
Biology
chloroplast
Chloroplasts
Complementation
Cytology
Cytoplasm
Heat stress
Heat tolerance
Importation
Localization
Organelles
Phosphorylation
Photosystem II
Physiological functions
protein importation
Proteins
Regulatory mechanisms (biology)
SUMO protein
SUMO3
SUMOylation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Summary Chloroplasts are hypersensitive to heat stress (HS). SUMOylation, a critical post‐translational modification, is conservatively involved in HS responses. However, the functional connection between SUMOylation and chloroplasts under HS remains to be studied. The bioinformatics, biochemistry, and cell biology analyses were used to detect the SUMOylation statuses of Arabidopsis nuclear‐encoded chloroplast proteins and the effect of SUMOylation on subcellular localization of these proteins under HS. PSBR, a subunit of photosystem II, was used as an example for a detailed investigation of functional mechanisms. After a global SUMOylation site prediction of nuclear‐encoded chloroplast proteins, biochemical data showed that most of the selected candidates are modified by SUMO3 in the cytoplasm. The chloroplast localization of these SUMOylation targets under long‐term HS is partially maintained by the SUMO ligase AtSIZ1. The HS‐induced SUMOylation on PSBR contributes to the maintenance of its chloroplast localization, which is dependent on its chloroplast importation efficiency correlated to phosphorylation. The complementation analysis provided evidence that SUMOylation is essential for the physiological function of PSBR under HS. Our study illustrated a general regulatory mechanism of SUMOylation in maintaining the chloroplast protein importation during HS and provided hints for further investigation on protein modifications associated with plant organelles under stress conditions.
ISSN:0028-646X
1469-8137
DOI:10.1111/nph.18121