Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes
FEBS letters. Bd. 435. H. 1. Amsterdam u.a.: Elsevier 1998 S. 101 - 104
Erscheinungsjahr: 1998
ISBN/ISSN: 1873-3468 ; 0014-5793
Publikationstyp: Zeitschriftenaufsatz
Sprache: Englisch
Doi/URN: 10.1016/S0014-5793(98)01046-1
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Inhaltszusammenfassung
Previous 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 ...Previous 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, (C) 1998 Federation of European Biochemical Societies.» weiterlesen» einklappen
Autoren
Klassifikation
DFG Fachgebiet:
2.12 - Pflanzenwissenschaften
DDC Sachgruppe:
Pflanzen (Botanik)