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Papers In Press, published online ahead of print December 10, 2001
Chemical Resources Laboratory, Tokyo Institute of Technology, Yokohama 226-8503
Corresponding Author: myoshida{at}res.titech.ac.jp
As a member of molecular chaperone Hsp100/Clp family, TClpB from Thermus thermophilus has two nucleotide-binding domains (NBD1 and NBD2) in a single polypeptide, each containing WalkerA and WalkerB consensus motifs. To probe their roles, mutations were introduced into the WalkerA or WalkerB motifs of each or both of the NBDs. The results are as follows. (1) For each of the NBDs, the ability of nucleotide binding is lost by mutations in the WalkerA motif but is retained by mutations in the WalkerB motif. (2) Each NBD has a casein-stimulatable, small basic ATPase activity that is lost when the WalkerB motif is mutated. (3) TClpB assembles into a uniform 580 kDa oligomer when ATP is present at 55 ?C. Only the mutants in the WalkerA motif in NBD1 fail to assemble, indicating that ATP binding to NBD1, but not hydrolysis, is necessary and sufficient for the assembly. (4) Chaperone function of TClpB was lost when the WalkerA motif in each of the NBDs was mutated. Mutants in the WalkerB motifs of each NBD retained some chaperone activity.
J. Biol. Chem, 10.1074/jbc.M109349200
Submitted on September 27, 2001
Revised on November 9, 2001
Accepted on December 9, 2001
Roles of the two ATP-binding sites of ClpB from Thermus thermophilus
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