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Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes
Author(s) -
Dilly-Hartwig Hans,
Allen John F,
Paulsen Harald,
Race Helen L
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01046-1
Subject(s) - photosystem ii , phosphorylation , light harvesting complex , protein kinase a , biochemistry , recombinant dna , protein phosphorylation , photosystem i , chemistry , biophysics , photosystem , biology , microbiology and biotechnology , photosynthesis , gene
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.