PMID:12034886
| Citation |
Akiyama, Y (2002) Proton-motive force stimulates the proteolytic activity of FtsH, a membrane-bound ATP-dependent protease in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 99:8066-71 |
|---|---|
| Abstract |
FtsH is a membrane-bound, ATP-dependent metalloprotease in Escherichia coli that degrades some integral membrane proteins and cytoplasmic proteins. In this study, we show that FtsH-dependent degradation of both membrane-bound and soluble proteins is retarded when cells are treated with carbonyl cyanide-3-chlorophenylhydrazone or 2,4-dinitrophenol uncouplers, which dissipate the proton-motive force. In vitro casein degradation by membrane-integrated FtsH was stimulated by succinate, a respiratory substrate; this stimulation was counteracted by cyanide-3-chlorophenylhydrazone. Potassium thiocyanate, which specifically collapses Deltapsi, partially canceled the effect of succinate, but ammonium sulfate, which collapses DeltapH, showed little effect. These results indicate that the proton-motive force, in particular the Deltapsi component, plays a role in efficient degradation of substrates by FtsH in its native state. FtsH variants with altered transmembrane regions did not receive proton-motive force stimulation, suggesting that the proton-motive force activates FtsH, directly or indirectly, through the transmembrane region. |
| Links |
PubMed PMC123021 Online version:10.1073/pnas.122616899 |
| Keywords |
ATP-Dependent Proteases; Adenosine Triphosphatases/metabolism; Bacterial Proteins/metabolism; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology; Cell Membrane/enzymology; Endopeptidases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Hydrogen-Ion Concentration; Kinetics; Membrane Proteins/metabolism; Plasmids; Recombinant Proteins/metabolism |
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