Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum
- 21 August 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 574 (1-3) , 161-166
- https://doi.org/10.1016/j.febslet.2004.08.021
Abstract
The Lon protease from the archaeon Thermoplasma acidophilum (TaLon) is composed of an N-terminal ATPase associated with various cellular activities (AAA+) domain and a C-terminal Lon protease domain. Although related in sequence to the soluble Lon proteases, TaLon was shown to be membrane-bound in its native host and also when expressed in Escherichia coli. Recombinant TaLon was purified as a functional high-molecular weight complex displaying ATPase and proteolytic activity. Mutagenesis of conserved AAA+ residues revealed that the Walker A and B motifs, and the sensor 1 and sensor 2′ residues were essential for the ATPase activity, while the sensor 2 and the arginine finger were involved in activation of the protease domainKeywords
This publication has 42 references indexed in Scilit:
- Membrane Protein Degradation by FtsH Can Be Initiated from Either EndJournal of Bacteriology, 2002
- A Membrane-Bound Archaeal Lon Protease Displays ATP-Independent Proteolytic Activity towards Unfolded Proteins and ATP-Dependent Activity for Folded ProteinsJournal of Bacteriology, 2002
- Structure and mechanism of the RuvB holliday junction branch migration motorJournal of Molecular Biology, 2001
- Surviving StarvationScience, 2001
- Characterization of the N‐terminal repeat domain of Escherichia coli ClpA—A class I Clp/HSP100 ATPaseProtein Science, 2001
- Characterization of a conserved α-helical, coiled-coil motif at the C-terminal domain of the ATP-dependent FtsH (HflB) protease of Escherichia coli 1 1Edited by J. KarnJournal of Molecular Biology, 2000
- FtsH – a single-chain charonin?FEMS Microbiology Reviews, 1999
- Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum is a proline iminopeptidaseFEBS Letters, 1996
- The mechanism and functions of ATP‐dependent proteases in bacterial and animal cellsEuropean Journal of Biochemistry, 1992
- The P-loop — a common motif in ATP- and GTP-binding proteinsTrends in Biochemical Sciences, 1990