Na+‐ATPase from the plasma membrane of the marine alga Tetraselmis (Platymonas) viridis forms a phosphorylated intermediate

FEBS Letters

Dietz, Karl-Josef¹  Popova, Larisa²  Gimmler, Hartmut¹  Balnokin, Yurii² 

[1] Julius-von-Sachs Institut für Biowissenschaften, Universität Würzburg, Mittlerer Dallenbergweg 64, D-97080 Würzburg, Germany;Institute of Plant Physiology, Russian Academy of Sciences, Botanicheskaya 35, 127276 Moscow, Russia

关键词: Plasma membrane;    Phosphointermediate;    Sodium pump;    Sodium ATPase;    Tetraselmis viridis;    Platymonas viridis;    DTT;    dithiothreitol;    CCCP;    m-chlorocarbonylcyanide phenylhydrazone;    PM;    plasma membrane;    pmf;    proton motive force;    PMSF;    phenylmethylsulfonyl fluoride;    PAGE;    polyacrylamide gel electrophoresis;    TCA;    trichloroacetic acid;   

DOI  :  10.1016/S0014-5793(98)00314-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Plasma membranes isolated from the marine unicellular alga Tetraselmis (Platymonas) viridis were phosphorylated by [γ-³²P]ATP, and membrane proteins were then analyzed by PAGE in SDS, under acidic conditions. Three radioactive components with apparent molecular masses of 100 kDa, 76 kDa, and 26 kDa were detected. The phosphorylation of one of them, the 100 kDa polypeptide, was specifically stimulated by Na⁺. Vanadate almost completely inhibited the Na⁺-mediated phosphorylation of the peptide. The phosphate bound to this peptide underwent rapid turnover and was discharged by hydroxylamine. The 100 kDa phosphopeptide was sensitive to ADP. The conclusion is drawn that the 100 kDa phosphopeptide is a phosphorylated intermediate of the Na⁺-transporting ATPase in the T. viridis plasma membrane.

【 授权许可】

Unknown