Premium
Identification of STN7/STN8 kinase targets reveals connections between electron transport, metabolism and gene expression
Author(s) -
Schönberg Anna,
Rödiger Anja,
Mehwald Wiebke,
Galonska Johann,
Christ Gideon,
Helm Stefan,
Thieme Domenika,
Majovsky Petra,
Hoehenwarter Wolfgang,
Baginsky Sacha
Publication year - 2017
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.13536
Subject(s) - thylakoid , biochemistry , biology , kinase , phosphorylation , electron transport chain , protein phosphorylation , serine , rubisco , photosystem , mutant , protein subunit , microbiology and biotechnology , protein kinase a , gene , chloroplast
Summary The thylakoid‐associated kinases STN7 and STN8 are involved in short‐ and long‐term acclimation of photosynthetic electron transport to changing light conditions. Here we report the identification of STN7/STN8 in vivo targets that connect photosynthetic electron transport with metabolism and gene expression. Comparative phosphoproteomics with the stn7 and stn8 single and double mutants identified two proteases, one RNA‐binding protein, a ribosomal protein, the large subunit of Rubisco and a ferredoxin‐NADP reductase as targets for the thylakoid‐associated kinases. Phosphorylation of three of the above proteins can be partially complemented by STN8 in the stn7 single mutant, albeit at lower efficiency, while phosphorylation of the remaining three proteins strictly depends on STN7. The properties of the STN7‐dependent phosphorylation site are similar to those of phosphorylated light‐harvesting complex proteins entailing glycine or another small hydrophobic amino acid in the −1 position. Our analysis uncovers the STN7/STN8 kinases as mediators between photosynthetic electron transport, its immediate downstream sinks and long‐term adaptation processes affecting metabolite accumulation and gene expression.