PMID:12667449
| Citation |
Herman, C, Prakash, S, Lu, CZ, Matouschek, A and Gross, CA (2003) Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Mol. Cell 11:659-69 |
|---|---|
| Abstract |
FtsH, a member of the AAA family of proteins, is the only membrane ATP-dependent protease universally conserved in prokaryotes, and the only essential ATP-dependent protease in Escherichia coli. We investigated the mechanism of degradation by FtsH. Other well-studied ATP-dependent proteases use ATP to unfold their substrates. In contrast, both in vitro and in vivo studies indicate that degradation by FtsH occurs efficiently only when the substrate is a protein of low intrinsic thermodynamic stability. Because FtsH lacks robust unfoldase activity, it is able to use the protein folding state of substrates as a criterion for degradation. This feature may be key to its role in the cell and account for its ubiquitous distribution among prokaryotic organisms. |
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| Keywords |
ATP-Dependent Proteases; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Cell Membrane/metabolism; Dose-Response Relationship, Drug; Escherichia coli/metabolism; Escherichia coli Proteins; Green Fluorescent Proteins; Heat-Shock Proteins/metabolism; Kinetics; Luminescent Proteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Molecular Sequence Data; Plasmids/metabolism; Protein Binding; Protein Folding; Protein Structure, Tertiary; RNA, Bacterial/metabolism; Recombinant Fusion Proteins/metabolism; Ribonucleases/metabolism; Sigma Factor; Substrate Specificity; Temperature; Thermodynamics; Time Factors; Transcription Factors/metabolism |
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