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Light‐dependent N‐terminal phosphorylation of LHCSR3 and LHCB4 are interlinked in Chlamydomonas reinhardtii
Author(s) -
Scholz Martin,
Gäbelein Philipp,
Xue Huidan,
Mosebach Laura,
Bergner Sonja Verena,
Hippler Michael
Publication year - 2019
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.14368
Subject(s) - chlamydomonas reinhardtii , phosphorylation , biology , chlamydomonas , oxidative phosphorylation , protein phosphorylation , microbiology and biotechnology , proteomics , biochemistry , gene , protein kinase a , mutant
Summary Phosphorylation dynamics of LHCSR 3 were investigated in Chlamydomonas reinhardtii by quantitative proteomics and genetic engineering. LHCSR 3 protein expression and phosphorylation were induced in high light. Our data revealed synergistic and dynamic N‐terminal LHCSR 3 phosphorylation. Phosphorylated and nonphosphorylated LHCSR 3 associated with PSII ‐ LHCII supercomplexes. The phosphorylation status of LHCB 4 was closely linked to the phosphorylation of multiple sites at the N‐terminus of LHCSR 3, indicating that LHCSR 3 phosphorylation may operate as a molecular switch modulating LHCB 4 phosphorylation, which in turn is important for PSII ‐ LHCII disassembly. Notably, LHCSR 3 phosphorylation diminished under prolonged high light, which coincided with onset of CEF . Hierarchical clustering of significantly altered proteins revealed similar expression profiles of LHCSR 3, CRX , and FNR . This finding indicated the existence of a functional link between LHCSR 3 protein abundance and phosphorylation, photosynthetic electron flow, and the oxidative stress response.