PMID:9218777
| Citation |
Shotland, Y, Koby, S, Teff, D, Mansur, N, Oren, DA, Tatematsu, K, Tomoyasu, T, Kessel, M, Bukau, B, Ogura, T and Oppenheim, AB (1997) Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli. Mol. Microbiol. 24:1303-10 |
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| Abstract |
Rapid proteolysis plays an important role in regulation of gene expression. Proteolysis of the phage lambda CII transcriptional activator plays a key role in the lysis-lysogeny decision by phage lambda. Here we demonstrate that the E. coli ATP-dependent protease FtsH, the product of the host ftsH/hflB gene, is responsible for the rapid proteolysis of the CII protein. FtsH was found previously to degrade the heat-shock transcription factor sigma32. Proteolysis of sigma32 requires, in vivo, the presence of the DnaK-DnaJ-GrpE chaperone machine. Neither DnaK-DnaJ-GrpE nor GroEL-GroES chaperone machines are required for proteolysis of CII in vivo. Purified FtsH carries out specific ATP-dependent proteolysis of CII in vitro. The degradation of CII is at least 10-fold faster than that of sigma32. Electron microscopy revealed that purified FtsH forms ring-shaped structures with a diameter of 6-7 nm. |
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| Keywords |
ATP-Dependent Proteases; Adenosine Triphosphatases/metabolism; Adenosine Triphosphatases/ultrastructure; Bacterial Proteins/metabolism; Bacterial Proteins/ultrastructure; Bacteriophage lambda; Endopeptidases/metabolism; Escherichia coli/enzymology; Escherichia coli/virology; Escherichia coli Proteins; Membrane Proteins/metabolism; Membrane Proteins/ultrastructure; Transcription Factors/metabolism; Viral Proteins |
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