Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock

• Published in: Nature plants Vol. 7; no. 10; pp. 1420 - 1432
• Main Authors: Ji, Shuiling, Siegel, Alex, Shan, Shu-ou, Grimm, Bernhard, Wang, Peng
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.10.2021; Nature Publishing Group
• Subjects: 09 BIOMASS FUELS; 631/449/1736; 631/449/2661/2663; 631/449/448/1374; Agglomeration; Arabidopsis - genetics; Arabidopsis - physiology; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Assembly; BASIC BIOLOGICAL SCIENCES; Binding; Biomedical and Life Sciences; Biosynthesis; Chlorophyll; Chlorophyll - biosynthesis; Chlorophyll - genetics; Chloroplasts; Heat; Heat shock; Heat-Shock Response - genetics; High temperature; Life Sciences; light harvesting complex; molecular chaperone; Plant Sciences; Post-translation; Proteins; Recognition; Sensitivity; Signal recognition particle; Signal Recognition Particle - genetics; Signal Recognition Particle - metabolism; Substrates; thermoprotection
• ISSN: 2055-0278; 2055-0278
• DOI: 10.1038/s41477-021-00994-y

The assembly of light-harvesting chlorophyll-binding proteins (LHCPs) is coordinated with chlorophyll biosynthesis during chloroplast development. The ATP-independent chaperone known as chloroplast signal recognition particle 43 (cpSRP43) mediates post-translational LHCP targeting to the thylakoid membrane and also participates in tetrapyrrole biosynthesis (TBS). How these distinct actions of cpSRP43 are controlled has remained unclear. Here, we demonstrate that cpSRP43 effectively protects several TBS proteins from heat-induced aggregation and enhances their stability during leaf greening and heat shock. While the substrate-binding domain of cpSRP43 is sufficient for chaperoning LHCPs, the stabilization of TBS clients requires the chromodomain 2 of the protein. Strikingly, cpSRP54—which activates cpSRP43’s LHCP-targeted function—inhibits the chaperone activity of cpSRP43 towards TBS proteins. High temperature weakens the interaction of cpSRP54 with cpSRP43, thus freeing cpSRP43 to interact with and protect the integrity of TBS proteins. Our data indicate that the temperature sensitivity of the cpSRP43–cpSRP54 complex enables cpSRP43 to serve as an autonomous chaperone for the thermoprotection of TBS proteins. The temperature sensitivity of a chloroplast signal recognition particle complex provides thermoprotection for tetrapyrrole biosynthesis proteins, protecting several proteins from heat-induced aggregation during the assembly of chlorophyll-binding proteins.