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J. Biol. Chem., Vol. 278, Issue 19, 17388-17394, May 9, 2003
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From the S. C. Johnson Research Center, Mayo Clinic Scottsdale,
Scottsdale, Arizona 85259
Hsp90 assembles with steroid receptors and
other client proteins in association with one or more Hsp90-binding
cochaperones, some of which contain a common tetratricopeptide repeat
(TPR) domain. Included in the TPR cochaperones are the
Hsp70-Hsp90-organizing protein Hop, the FK506-binding immunophilins
FKBP52 and FKBP51, the cyclosporin A-binding immunophilin CyP40, and
protein phosphatase PP5. The TPR domains from these proteins have
similar x-ray crystallographic structures and target cochaperone
binding to the MEEVD sequence that terminates Hsp90. However, despite
these similarities, the TPR cochaperones have distinctive properties
for binding Hsp90 and assembling with Hsp90·steroid receptor
complexes. To identify structural features that differentiate binding
of FKBP51 and FKBP52 to Hsp90, we generated an assortment of truncation
mutants and chimeras that were compared for coimmunoprecipitation with
Hsp90. Although the core TPR domain (approximately amino acids
260-400) of FKBP51 and FKBP52 is required for Hsp90 binding, the
C-terminal 60 amino acids (~400-end) also influence Hsp90 binding.
More specifically, we find that amino acids 400-420 play a critical
role for Hsp90 binding by either FKBP. Within this 20-amino acid
region, we have identified a consensus sequence motif that is also
present in some other TPR cochaperones. Additionally, the final 30 amino acids of FKBP51 enhance binding to Hsp90, whereas the
corresponding region of FKBP52 moderates binding to Hsp90. Taking into
account the x-ray crystal structure for FKBP51, we conclude that the
C-terminal regions of FKBP51 and FKBP52 outside the core TPR domains
are likely to assume alternative conformations that significantly impact Hsp90 binding.
C-terminal Sequences outside the Tetratricopeptide Repeat Domain
of FKBP51 and FKBP52 Cause Differential Binding to Hsp90*
*
This work was supported by National Institutes of Health
Grant DK48218 (to D. F. S.) and the Mayo Foundation.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 Clinic Scottsdale, 13400 E. Shea Blvd.,
Scottsdale, AZ 85259. Tel.: 480-301-6595; Fax: 480-301-3384; E-mail: smith.david26@mayo.edu.
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