title: Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.
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.
authors.affiliation: Department of Molecular Genetics and Biotechnology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.
authors.forename: Y
authors.initials: Y
authors.lastname: Shotland
authors.forename: S
authors.initials: S
authors.lastname: Koby
authors.forename: D
authors.initials: D
authors.lastname: Teff
authors.forename: N
authors.initials: N
authors.lastname: Mansur
authors.forename: D A
authors.initials: DA
authors.lastname: Oren
authors.forename: K
authors.initials: K
authors.lastname: Tatematsu
authors.forename: T
authors.initials: T
authors.lastname: Tomoyasu
authors.forename: M
authors.initials: M
authors.lastname: Kessel
authors.forename: B
authors.initials: B
authors.lastname: Bukau
authors.forename: T
authors.initials: T
authors.lastname: Ogura
authors.forename: A B
authors.initials: AB
authors.lastname: Oppenheim
mesh_terms: D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000378:metabolism* / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000378:metabolism* / Q000648:ultrastructure; D010582:Bacteriophage lambda; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000821:virology; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000378:metabolism* / Q000648:ultrastructure; D014157:Transcription Factors / Q000378:metabolism*; D014764:Viral Proteins
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D014157:Transcription Factors; D014764:Viral Proteins; C039000:cII protein, bacteriophage lambda; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; C513383:FtsH protein, E coli; D000251:Adenosine Triphosphatases