Biochemical characterization of the presecretory protein translocation machinery of Escherichia coli

FEBS Letters

Tokuda, Hajime¹ 

[1] Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113, Japan

关键词: Protein translocation;    Sec apparatus;    Escherichia coli;    Reconstitution;    Everted membrane vesicle;    Δp;    proton motive force;    MBP;    maltose binding protein;    OmpA;    outer membrane protein A;    ER;    endoplasmic reticulum;    SRP;    signal recognition particle;    SR;    SRP receptor;   

DOI  :  10.1016/0014-5793(94)00317-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein translocation apparatus in Escherichia coli has been studied both genetically and biochemically. In vitro protein translocation systems involving everted membrane vesicles or reconstituted proteoliposomes have significantly contributed to biochemical clarification of the structure, mechanism and energetics of the apparatus. It is established that SecA, SecY and SecE are essential components, and play fundamental roles in the translocation reaction, and that both ATP and a proton motive force are required for the translocation. A new membrane factor, SecG, was found to participate in the formation of the apparatus, causing significant enhancement of the activity. SecD was found to play a role in the release of translocated proteins from the outer surface of the cytoplasmic membrane.

【 授权许可】

Unknown