Cyanobacterial thylakoid membrane proteins are reversibly phosphorylated under plastoquinone‐reducing conditions in vitro

FEBS Letters

Allen, John F.¹  Harrison, Michael A.¹  Tsinoremas, Nicholas F.¹ 

[1] Department of Pure and Applied Biology, University Of Leeds, LS29JT, UK

关键词: Photosynthesis;    Protein phosphorylation;    State transition;    Protein kinase;    Phosphatase;    Cyanobacterium;    DCMU;    3-(3′;    4′ dichlorophenyl)-1;    1-dimethylurea;    DQ;    duroquinone;    DQH2;    duroquinol;    FSBA;    5′ p-fluorylsulphonylbenzoyl adenosine;    HEPES;    N-2-hydroxyethylpiperazine-N′ 2-ethanesulphonic acid;    LHC-II;    the chlorophyll a/b-binding light-harvesting complex of PSII;    MV;    methyl viologen;    PSI;    photosystem I;    PSII;    photosystem II;    SDS;    sodium dodecyl sulphate;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(91)80499-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Reversible, light-dependent protein phosphorylation was observed in isolated thylakoid membranes of the cyanobacterium Synechococcus 6301. A polypeptide of 15 kDA in particular was phosphorylated under plastoquinone-reducing conditions and was not phosphorylated under plastoquinone-oxidising conditions. Phosphorylation and dephosphorylation reactions involving this and several other membrane polypeptides showed sensitivity to inhibitors of protein kinases and phosphatases. Changes in phosphorylation state correlated with changes in low temperature fluorescence emission characteristic or changes in excitation energy distribution between the photosystems. The 15 kDa phosphopolypeptide is likely to be involved directly in light state adaptations in cyanobacteria.

【 授权许可】

Unknown