Maria Nagy and Hui-Chuan Wu contributed equally to this work.
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Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB†
Article first published online: 15 DEC 2008
DOI: 10.1002/pro.36
Copyright © 2008 The Protein Society
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How to Cite
Nagy, M., Wu, H.-C., Liu, Z., Kedzierska-Mieszkowska, S. and Zolkiewski, M. (2009), Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB. Protein Science, 18: 287–293. doi: 10.1002/pro.36
- †
Conflict of interest: The authors declare no competing interests.
Publication History
- Issue published online: 30 JAN 2009
- Article first published online: 15 DEC 2008
- Accepted manuscript online: 15 DEC 2008 12:00AM EST
- Manuscript Accepted: 10 NOV 2008
- Manuscript Received: 29 AUG 2008
Funded by
- Dystonia Medical Research Foundation, The National Institutes of Health. Grant Number: P20 RR016475
- The Polish Committee for Scientific Research. Grant Number: 0668/P01/2006/30
- The Kansas Agricultural Experiment Station. Grant Number: 08-72-J
References
- 1, , , ( 1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27–43.
- 2, ( 2005) AAA+ proteins: have engine, will work. Nat Rev Mol Cell Biol 6: 519–529.
- 3, ( 2001) AAA+ superfamily ATPases: common structure–diverse function. Genes Cells 6: 575–597.Direct Link:
- 4, , , , ( 2005) Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol Chem 386: 739–744.
- 5, , , , , , ( 2003) The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 115: 229–240.
- 6( 1999) ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J Biol Chem 274: 28083–28086.
- 7, , , ( 1999) Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci USA 96: 7184–7189.
- 8, , , , ( 1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96: 13732–13737.
- 9, , , , , , , , , , , ( 2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119: 653–665.
- 10, , , , , , , , , , , , , , ( 2004) Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119: 9–18.
- 11, , , , , , , , , , , ( 2004) Substrate recognition by the AAA+ chaperone ClpB. Nat Struct Mol Biol 11: 607–615.
- 12, , , ( 2005) The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. J Biol Chem 280: 34940–34945.
- 13, , , ( 2004) Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem 279: 29139–29146.
- 14, , ( 2007) Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell 25: 261–271.
- 15, , , ( 2003) Characterization of a trap mutant of the AAA+ chaperone ClpB. J Biol Chem 278: 32608–32617.
- 16, , , ( 2004) Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol 146: 11–31.
- 17, , , , , , , , , , , , , , ( 1997) The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein. Nat Genet 17: 40–48.
- 18, , , , ( 2002) The DnaC helicase loader is a dual ATP/ADP switch protein. EMBO J 21: 3148–3159.
- 19, , , ( 2003) Recombinant expression, purification, and comparative characterization of torsinA and its torsion dystonia-associated variant Delta E-torsinA. Biochemistry 42: 15333–15341.
- 20, , ( 2000) Structure and activity of ClpB from Escherichia coli. Role of the amino- and -carboxyl-terminal domains. J Biol Chem 275: 37565–37571.
- 21, , , ( 2004) Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. Protein Sci 13: 567–574.Direct Link:
- 22, , , , ( 2005) Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121: 1017–1027.
- 23, , , ( 1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179: 131–137.
- 24, ( 2002) Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity. J Mol Biol 318: 1127–1137.
- 25( 1999) Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases. Nat Cell Biol 1: E25–E27.
- 26, , ( 2004) Functional similarities and differences of an archaeal Hsp70(DnaK) stress protein compared with its homologue from the bacterium Escherichia coli. J Mol Biol 336: 539–549.
- 27, , , , ( 1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J Biol Chem 260: 7591–7598.
- 28, , . Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry 2003; 42: 14242–14248.
- 29, ( 2002) Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli. Protein Sci 11: 1192–1198.Direct Link:

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