Characterization of the archaeal membrane-associated Lon protease

• Applicant: Dr. Peter Zwickl
• Subject Area: Metabolism, Biochemistry and Genetics of Microorganisms
• Term: from 2002 to 2005
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 5362975

While significant advances have been made in elucidating the struture and enzymatic mechanism of the soluble 20S proteasome in archaea, the archaeal membrane-associated Lon protease was not studied at all. Since the membrane-bound protease FtsH, which is essential in bacteria, is absent from archaea, its function may be assumed by the archaeal Lon protease. It is our goal to purify and characterize the Lon protease from Thermoplasma acidophilum cells. Simultaneously, we want to express the Lon wildtype gene and various mutants of it in E. coli. Moreover, we will analyze whether the archaeal membrane-associated Lon protease can replace the E. coli Lon or FtsH protease or the yeast mitochondrial AAA proteases.

• DFG Programme: Priority Programmes
• Subproject of: SPP 1132: Proteolysis in Prokaryotes: Protein Quality Control and Regulatory Principle