Light‐dependent N‐terminal phosphorylation of LHCSR3 and LHCB4 are interlinked in Chlamydomonas reinhardtii

Summary Phosphorylation dynamics of LHCSR3 were investigated in Chlamydomonas reinhardtii by quantitative proteomics and genetic engineering. LHCSR3 protein expression and phosphorylation were induced in high light. Our data revealed synergistic and dynamic N‐terminal LHCSR3 phosphorylation. Phospho...

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Published in:The Plant journal : for cell and molecular biology 2019-09, Vol.99 (5), p.877-894
Main Authors: Scholz, Martin, Gäbelein, Philipp, Xue, Huidan, Mosebach, Laura, Bergner, Sonja Verena, Hippler, Michael
Format: Article
Language:English
Subjects:
Chlamydomonas reinhardtii
Cluster analysis
Clustering
Dismantling
Genetic engineering
high light stress
Kinases
light harvesting
Molecular machines
Original
Oxidative stress
Phosphorylation
Photosynthesis
Photosystem II
Protein engineering
protein phosphorylation
Proteins
Proteomics
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Summary:Summary Phosphorylation dynamics of LHCSR3 were investigated in Chlamydomonas reinhardtii by quantitative proteomics and genetic engineering. LHCSR3 protein expression and phosphorylation were induced in high light. Our data revealed synergistic and dynamic N‐terminal LHCSR3 phosphorylation. Phosphorylated and nonphosphorylated LHCSR3 associated with PSII‐LHCII supercomplexes. The phosphorylation status of LHCB4 was closely linked to the phosphorylation of multiple sites at the N‐terminus of LHCSR3, indicating that LHCSR3 phosphorylation may operate as a molecular switch modulating LHCB4 phosphorylation, which in turn is important for PSII‐LHCII disassembly. Notably, LHCSR3 phosphorylation diminished under prolonged high light, which coincided with onset of CEF. Hierarchical clustering of significantly altered proteins revealed similar expression profiles of LHCSR3, CRX, and FNR. This finding indicated the existence of a functional link between LHCSR3 protein abundance and phosphorylation, photosynthetic electron flow, and the oxidative stress response. Significance Statement We analyzed light‐dependent phosphorylation of LHCSR3 and LHCB4 by quantitative proteomics, genetic engineering, and functional measurements. N‐terminal LHCSR3 phosphorylation is light dependent and modulates phosphorylation of LHCB4 and the association of LHCSR3 with photosynthetic multi‐protein complexes. Our data revealed the functional importance of LHCSR3 phosphorylation, pointing to unforeseen functions in algal photosynthesis.
ISSN:0960-7412
1365-313X
DOI:10.1111/tpj.14368