Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes.
Previous studies directed towards understanding phosphorylation of the chlorophyll alb binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhch1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of which are discussed.
Institut für Allgemeine Botanik, Johannes Gutenberg-Universität Mainz, Germany.
H
H
Dilly-Hartwig
J F
JF
Allen
H
H
Paulsen
H L
HL
Race
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism; D045342:Light-Harvesting Protein Complexes; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D018532:Pisum sativum; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D011494:Protein Kinases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism*; D013379:Substrate Specificity / Q000235:genetics
D002352:Carrier Proteins; D045342:Light-Harvesting Protein Complexes; D046911:Macromolecular Substances; D010446:Peptide Fragments; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D011994:Recombinant Proteins; D011494:Protein Kinases