Soluble P‐type ATPase from an archaeon, Methanococcus jannaschii

FEBS Letters

Ogawa, Haruo²  Toyoshima, Chikashi²  Haga, Tatsuya¹ 

[1] Department of Neurochemistry, Faculty of Medicine, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, Japan;Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, Japan

关键词: P-type ATPase;    Cloning;    Overexpression;    Ion pump;    Methanococcus jannaschii;   

DOI  :  10.1016/S0014-5793(00)01374-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

MJ0968 has been proposed to be an ancestor of P-type ATPase, because its primary structure is highly homologous to that of the core catalytic domain of P-type ATPase. However it completely lacks amino acid sequences that possibly constitute transmembrane domains. To examine if MJ0968 is indeed a P-type ATPase, it was overexpressed in Escherichia coli and purified. It did show ATPase activity, autophosphorylation and inhibition by vanadate. All these properties support the idea that MJ0968 is indeed a soluble P-type ATPase.

【 授权许可】

Unknown