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Involvement of protein phosphorylation in the sensitivity of photosystem II to strong illumination
Author(s) -
Giardi Maria T.,
Komenda Josef,
Masojidek Jiri
Publication year - 1994
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1994.tb06669.x
Subject(s) - thylakoid , photosystem ii , spinacia , dephosphorylation , photoinhibition , phosphorylation , biophysics , protein phosphorylation , biochemistry , biology , spinach , photosystem i , photosynthesis , electron transfer , chemistry , phosphatase , chloroplast , photochemistry , protein kinase a , gene
Four types of differently phosphorylated hylakoids isolated from field grown spinach ( Spinacia oleracea L.) were tested for the sensitivity of photosystem II (PSII) to photoinactivation. Phosphorylation of light‐harvesting II complexes (LHCII) protected PSII electron transfer from photoinhibitory damage, while the phosphorylation of the PSII core polypeptides slightly accelerated the decline of electron transfer during high irradiance treatment. Dephosphorylation of the CP43 apoprotein and PsbH protein by an alkaline phosphatase resulted in an extreme sensitivity of the thylakoids to strong illumination. The PSII photoinactivation of thylakoids with the impaired oxygen‐evolving complex was found to be independent of phosphorylation. The thylakoids of the thermophilic cyanobacterium Synechococcus elongates were used in order to compare the plants with an organism where LHCII complexes are missing and the PSII core proteins are not phosphorylated.