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Investigation of the substrate specificity of thylakoid protein kinase using synthetic peptides
Author(s) -
White I.R.,
O'Donnell P.J.,
Keen J.N.,
Findlay J.B.C.,
Millner P.A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81116-6
Subject(s) - thylakoid , photosystem ii , pisum , biochemistry , peptide , phosphorylation , protein kinase a , chemistry , substrate (aquarium) , kinase , photosystem i , biophysics , biology , chloroplast , photosynthesis , gene , ecology
Synthetic peptide analogues of the N‐terminal region of the light harvesting chlorophyll a/b binding polypeptide of photosystem II (LHC II) were used to probe the effect of charged groups on the protein kinase activity of pea ( Pisum sativum ) thylakoid membranes. The effectiveness of the synthetic peptides as substrates for protein kinase activity or as inhibitors of LHC II phosphorylation was correlated with their net positive charge, which ranged between +2 and +5. The effects of the synthetic peptides on phosphorylation of other, non‐LHC II, thyakoid polypeptides are also discussed.