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J. Biol. Chem., Vol. 275, Issue 44, 34140-34146, November 3, 2000
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From the Hsp90 is an abundant cytosolic molecular
chaperone. It controls the folding of target proteins including steroid
hormone receptors and kinases in complex with several partner proteins.
Prominent members of this protein family are large peptidyl prolyl
cis/trans isomerases (PPIases), which catalyze the cis/trans
isomerization of prolyl peptide bonds in proteins and possess chaperone
activity. In Saccharomyces cerevisiae, two closely related
large Hsp90-associated PPIases, Cpr6 and Cpr7, exist. We show here that
these homologous proteins bind with comparable affinity to Hsp90 but
exhibit significant structural and functional differences. Cpr6 is more
stable than Cpr7 against thermal denaturation and displays an up to
100-fold higher PPIase activity. In contrast, the chaperone activity of Cpr6 is much lower than that of Cpr7. Based on these results we suggest
that the two immunophilins perform overlapping but not identical tasks
in the Hsp90 chaperone cycle.
Cpr6 and Cpr7, Two Closely Related Hsp90-associated Immunophilins
from Saccharomyces cerevisiae, Differ in Their
Functional Properties*
,,¶
Institut für Organische Chemie und
Biochemie, Technische Universität München, 85747 Garching
and § Institut für Biotechnologie, Universität
Halle-Wittenberg, 06114 Halle, Germany
*
This work was supported by the Bundes ministerium für
Forschung und Technologic (BMBF), the SFB 521, and the Fonds du
Chemischen Industrie.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.
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