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J. Biol. Chem., Vol. 277, Issue 8, 5804-5809, February 22, 2002
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From the Chemical Resources Laboratory, Tokyo Institute of
Technology, Nagatsuta 4259, Yokohama 226-8503, Japan
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, and
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.
Roles of the Two ATP Binding Sites of ClpB from Thermus
thermophilus*
,
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a research fellowship from the Japan Society for the
Promotion of Science for Young Scientists.
§
To whom correspondence should be addressed. Fax: 81-45-924-5277;
E-mail: myoshida@res.titech.ac.jp.
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