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J Biol Chem, Vol. 273, Issue 18, 10819-10822, May 1, 1998

COMMUNICATION
The Peptidyl-prolyl Isomerase Domain of the CyP-40 Cyclophilin Homolog Cpr7 Is Not Required to Support Growth or Glucocorticoid Receptor Activity in Saccharomyces cerevisiae

Andrea A. Duina, James A. Marsh, Richard B. Kurtz, Hui-Chen Jane Chang^¶, Susan Lindquist^¶, and Richard F. Gaber

From the  Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208 and the ^¶ Department of Molecular Genetics and Cell Biology and the Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois 60637

CyP-40 cyclophilins are found in association with molecular chaperone Hsp90·steroid receptor complexes. The amino-terminal portion of these cyclophilins harbors the characteristic peptidyl-prolyl isomerase (PPIase) domain, whereas three copies of the tetratricopeptide (TPR) motif, a structure shown to be involved in protein-protein interactions, and a putative calmodulin-binding domain are located in the carboxyl-terminal half of the protein. The TPR domains mediate binding to Hsp90, but a requirement for the PPIase domain has not been established. To address this, we have investigated the effects of mutations that alter the PPIase domain of the Saccharomyces cerevisiae CyP-40 homolog, Cpr7. Because Cpr7 is required for rapid growth and full Hsp90 activity, a functional assessment of the PPIase domain could be performed in vivo. A mutation in the catalytic domain altering a conserved site predicted to be essential for isomerase activity did not compromise Cpr7 function. Furthermore, deletion of the entire PPIase domain did not significantly affect growth or Hsp90-mediated steroid receptor activity. These results indicate that the TPR-containing carboxyl terminus of Cpr7 is sufficient for fundamental Cpr7-dependent activity.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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