Investigation of the substrate specificity of thylakoid protein kinase using synthetic peptides.
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.
White
I R
IR
Department of Biochemistry, University of Leeds, UK.
O'Donnell
P J
PJ
Keen
J N
JN
Findlay
J B
JB
Millner
P A
PA
D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000201:enzymology* / Q000648:ultrastructure; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D010766:Phosphorylation; D010944:Plants; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity
D009842:Oligopeptides; D011494:Protein Kinases