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

FEBS Letters

Paulsen, Harald²  Race, Helen L¹  Allen, John F¹  Dilly-Hartwig, Hans² 

[1]Plant Cell Biology, Lund University, Box 7007, S-220 02 Lund, Sweden

[2]Institut für Allgemeine Botanik, Johannes Gutenberg-Universität Mainz, Müllerweg 6, D-55099 Mainz, Germany

关键词: Light harvesting protein;    Protein kinase;    Thylakoid membrane;    Pea;    Spinach;    CHAPS;    3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate;    LHC II;    light harvesting;    chlorophyll a/b binding protein complex associated with photosystem II;    Lhcb1;    light harvesting protein of photosystem II;    LHCP;    light harvesting;    chlorophyll a/b binding protein;    OG;    octyl glucopyranoside;    PS II;    photosystem II;    PS II-PK;    protein kinase associated with photosystem II;    TCA;    trichloroacetic acid;    TX-100;    Triton X-100;   

DOI  :  10.1016/S0014-5793(98)01046-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown