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Effects of synthetic peptides on thylakoid phosphoprotein phosphatase reactions
Author(s) -
Cheng Lüling,
Stys Dalibor,
Allen John F.
Publication year - 1995
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 - 10.1034/j.1399-3054.1995.930124.x
Subject(s) - dephosphorylation , phosphoprotein , phosphopeptide , phosphorylation , thylakoid , biochemistry , phosphatase , protein phosphorylation , peptide , protein phosphatase 2 , chemistry , biology , chloroplast , protein kinase a , gene
A synthetic peptide analogue of the phosphorylation site of LHC II, when phosphorylated by thylakoid membranes, served as a substrate for the thylakoid phosphoprotein phosphatase. The phosphopeptide became dephosphorylated at a low rate, comparable to that of the 9 kDa phosphoprotein. Phospho‐LHC II itself became dephosphorylated much more rapidly, at a rate unaffected by endogenous phosphorylation of the peptide. Endogenous phosphorylation of the peptide was also without effect on other thylakoid protein phosphorylation and dephosphorylation reactions. In contrast, dephosphorylation of many thylakoid phosphoproteins was inhibited by addition of a pure, chemically‐synthesised phosphopeptide analogue of phospho‐LHC II. This result suggests that at least one thylakoid phosphoprotein phosphatase exhibits a broad substrate specificity. The results indicate that any one of a number of amino acid sequences can give a phosphoprotein configuration that is recognised by a single phosphatase.