A Trapping Approach Reveals Novel Substrates and Physiological Functions of the Essential Protease FtsH in Escherichia coli

• Published in: The Journal of biological chemistry Vol. 287; no. 51; pp. 42962 - 42971
• Main Authors: Westphal, Kai, Langklotz, Sina, Thomanek, Nikolas, Narberhaus, Franz
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 14.12.2012; American Society for Biochemistry and Molecular Biology
• Subjects: ATP-dependent Protease; ATP-Dependent Proteases - isolation & purification; ATP-Dependent Proteases - metabolism; Bacteria; Enzyme Turnover; Escherichia coli; Escherichia coli - cytology; Escherichia coli - enzymology; Escherichia coli - growth & development; Escherichia coli Proteins - isolation & purification; Escherichia coli Proteins - metabolism; Iron-Sulfur Protein; Lipopolysaccharide (LPS); Microbial Viability; Microbiology; Models, Biological; Osmotic Pressure; Oxygen - metabolism; Phenotype; Protein Stability; Proteolysis; Proteome - metabolism; Proteomics - methods; Reproducibility of Results; Substrate Specificity; Bacteria; Iron-Sulfur Protein; Escherichia coli; Enzyme Turnover; ATP-dependent Protease; Lipopolysaccharide (LPS)

Proteolysis is a universal strategy to rapidly adjust the amount of regulatory and metabolic proteins to cellular demand. FtsH is the only membrane-anchored and essential ATP-dependent protease in Escherichia coli. Among the known functions of FtsH are the control of the heat shock response by prote...