0000000000359193

AUTHOR

Hans G. Dilly-hartwig

showing 2 related works from this author

Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes

1998

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 wh…

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 KinasesFEBS Letters
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Light Regulation of the Thylakoid LHCII Protein Phosphorylation at the Substrate Level

1998

The distribution of light energy between the two photosystems as well as the light-induced turnover of PSII proteins are regulated by the reversible phosphorylation of LHCII and the PSII-core proteins. The thylakoid protein kinase(s) is activated by a signal transduction system involving the interaction of reduced plastoquinone with the quinol oxidation site of the cytochrome bf complex [1]. Phosphorylation of the mobile pool of LHCII induces dissociation of this antenna from PSII and allows its interaction with the PSI in the stroma exposed membranes (state transition)[21. Dephosphorylation of LHCII by a membrane -bound phosphatase appears to be regulated by a cyclophilinlike protein locat…

chemistry.chemical_compoundChemistryThylakoidBiophysicsfood and beveragesPhosphorylationPlastoquinoneProtein phosphorylationmacromolecular substancesKinase activityProtein kinase AThreonine Phosphorylation SitePhotosystem
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