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RESEARCH PRODUCT
Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes
John F. AllenHelen L. RaceHans G. Dilly-hartwigHarald Paulsensubject
inorganic chemicalsPhotosystem IIMacromolecular SubstancesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsmacromolecular substancesBiologyBiochemistryDNA-binding proteinProtein kinaseThylakoid membraneSubstrate Specificitylaw.inventionStructural BiologylawGeneticsProtein phosphorylationAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyPlant ProteinsKinasePeasPeaPhotosystem II Protein Complexfood and beveragesCell BiologySpinachPeptide FragmentsRecombinant Proteinsenzymes and coenzymes (carbohydrates)BiochemistryThylakoidRecombinant DNALight harvesting proteinPhosphorylationbacteriaCarrier ProteinsProtein Kinasesdescription
AbstractPrevious studies directed towards understanding phosphorylation of the chlorophyll a/b 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 Lhcb1 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1998-10-02 | FEBS Letters |