PMID:8980112
| Citation |
Akiyama, Y, Kihara, A and Ito, K (1996) Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli. FEBS Lett. 399:26-8 |
|---|---|
| Abstract |
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 Fo part of H+-ATPase is another substrate of FtsH. Pulse-chase experiments showed that subunit a is unstable when it alone (without Fo 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. |
| Links | |
| Keywords |
ATP-Dependent Proteases; Bacterial Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Hydrolysis; Membrane Proteins/metabolism; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/metabolism; Substrate Specificity |
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