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J. Biol. Chem., Vol. 277, Issue 41, 38294-38304, October 11, 2002
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From the Department of Biochemistry and Molecular Biology, Mayo
Graduate School, Mayo Clinic, Rochester, Minnesota 55905
The highly coordinated interactions of several
molecular chaperones, including hsp70 and hsp90, are required for the
folding and conformational regulation of a variety of proteins in
eukaryotic cells, such as steroid hormone receptors and many other
signal transduction regulators. The protein called Hop serves as an
adaptor protein for hsp70 and hsp90 and is thought to optimize their
functional cooperation. Here we characterize the assembly of the
hsp70-Hop-hsp90 complex and reveal interactions that cause
conformational changes between the proteins in the complex. We found
that hsp40 plays an integral role in the assembly by enhancing the
binding of hsp70 to the Hop complex. This is accomplished by
stimulating the conversion of hsp70-ATP to hsp70-ADP, the hsp70
conformation favored for Hop binding. The hsp70-Hop-hsp90 complex is
highly dynamic, as has been observed previously for hsp90 in its
interaction with client proteins. Nonetheless, hsp90 binds with high
affinity to Hop (Kd = 90 nM), and this
binding is not affected by hsp70. hsp70 binds with lower affinity to
Hop (Kd = 1.3 µM) on its own, but
this affinity is increased (Kd = 250 nM) in the presence of hsp90. hsp90 also reduces the number of hsp70 binding sites on the Hop dimer from two sites in the absence
of hsp90 to one site in its presence. Hop can inhibit the ATP binding
and p23 binding activity of hsp90, yet this can be reversed if hsp70 is
present in the complex. Taken together, our results suggest that the
assembly of hsp70-Hop-hsp90 complexes is selective and influences the
conformational state of each protein.
The Assembly and Intermolecular Properties of the
hsp70-Hop-hsp90 Molecular Chaperone Complex*
*
This work was supported by National Institutes of Health
Grant DK59284.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.
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Biology, Mayo Graduate School, Mayo Clinic, 200 First St.
SW, Rochester, MN 55905. Tel.: 507-284-8401; Fax: 507-284-2053; E-mail:
toft.david@mayo.edu.
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