Amino acid composition of the 9 kDa phosphoprotein of pea thylakoids.

The 9 kDa phosphoprotein of pea thylakoids was isolated by electroelution from SDS-polyacrylamide gels and its amino acid composition determined. The result is at variance with the amino acid compositions predicted from published nucleotide sequences of the genes for apocytochrome b-559 and for CFo subunit III. The amino acid composition of the 9 kDa phosphoprotein resembles that of the 25 kDa light-harvesting chlorophyll a/b protein (LHC-II). We propose that the 9 kDa polypeptide is a chlorophyll-binding protein of photosystem II, that it functions as a link in excitation energy transfer between LHC-II and the reaction centre, and that its phosphorylation regulates excitation energy distribution by means of mutual electrostatic repulsion between itself and phosphorylated LHC-II.