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J Biol Chem, Vol. 274, Issue 29, 20060-20063, July 16, 1999
From the Department of Pharmacology, University of South Alabama,
Mobile, Alabama 36688
The sequential binding of heat shock protein 90 (hsp90) to a series of tetratricopeptide repeat (TPR) proteins is
critical to its function as a molecular chaperone. We have used
site-directed mutagenesis to clarify the structural basis for the
binding of hsp90 to the TPR domain of phosphoprotein phosphatase 5 (PP5). This TPR domain was chosen for study because its
three-dimensional structure is known. We examined
co-immunoprecipitation of hsp90 with wild type and mutant TPR
constructs from transfected cells. Only mutations located on one face
of the TPR domain affected hsp90 binding. This allowed the
identification of a binding groove. Three basic residues that are
highly conserved in hsp90-binding TPR proteins extend prominently into
this groove. Lys-97 and Arg-101 were absolutely required for hsp90
binding, while mutation of Arg-74 diminished, but did not abrogate,
hsp90 binding. Mutation of Lys-32, another conserved basic residue in
the binding groove, also blocked hsp90 binding. The TPR domain of PP5
bound specifically to a 12-kDa C-terminal fragment of hsp90. This
binding was reduced by mutation of acidic residues in the hsp90
fragment. These data suggest conservation, among hsp90-binding TPR
proteins, of a binding groove containing basic residues that interact
with acidic residues near the C terminus of hsp90.
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