Light‐induced D1 protein degradation is catalyzed by a serine‐type protease

FEBS Letters

Virgin, Ivar²  Salter, A.Hugh²  Andersson, Bertil²  Ghanotakis, Demetrios F.¹ 

[1] Department of Chemistry, University of Crete, PO Box 1470, Iraklion, Crete, Greece;Department of Biochemistry, Arrhenius Laboratories, Stockholm University, S-106 91 Stockholm, Sweden

关键词: D1 protein;    Photoinhibition;    Photosystem II;    Protease inhibitor;    Protein turnover;    Serine protease;    pA-PMSF;    [4-amidino-phenyl]-methane-sulphonyl fluoride;    chl;    chlorophyll;    DFP;    diisopropylfluorophosphate;    EDTA;    ethylene diaminetetraacetate;    disodium salt;    MES;    2-morpholino-ethanesulphonic acid-1-hydrate;    PAGE;    polyacrylamide gel electrophoresis;    PVDF;    polyvinylidene difluoride;    SDS;    sodium dodecyl sulphate;   

DOI  :  10.1016/0014-5793(91)80031-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Light-induced degradation of the D1 protein in isolated spinach photosystem II core preparations was studied after addition of various protease inhibitors. The degradation was selectively inhibited by several serine protease inhibitors in particular diisopropylfluorophosphate. The results demonstrate that the D1 protein is degraded by a serine-type of proteolytic activity that is an integral part of photosystem II.

【 授权许可】

Unknown