Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli

FEBS Letters

Akiyama, Yoshinori¹  Kihara, Akio¹  Ito, Koreaki¹ 

[1] Department of Cell Biology, Institute for Virus Research, Kyoto University, Kyoto 606-01, Japan

关键词: FtsH;    F1F0-ATP synthase;    Subunit a;    Membrane protein;    Protein degradation;    SDS-PAGE;    sodium dodecyl sulphate polyacrylamide gel electrophoresis;    FtsH-His6-Myc;    hexahistidine and Myc epitope-tagged FtsH;   

DOI  :  10.1016/S0014-5793(96)01283-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Escherichia coli FtsH is a membrane-bound ATPase with a proteolytic activity against the SecY subunit of protein translocase. We now report that subunit a of the membrane-embedded F₀ part of H⁺-ATPase is another substrate of FtsH. Pulse-chase experiments showed that subunit a is unstable when it alone (without F₀ subunits b and c) was oversynthesized and that it is stabilized in the ftsH mutants. Selective and ATP-dependent degradation of subunit a by purified FtsH protein was demonstrated in vitro. These results suggest that FtsH serves as a quality-control mechanism to avoid potentially harmful accumulation of free subunit a in the membrane.

【 授权许可】

Unknown