Gene Symbol: CPR6
Description: peptidylprolyl isomerase CPR6
Alias: CYP40, peptidylprolyl isomerase CPR6
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Duina A, Chang H, Marsh J, Lindquist S, Gaber R. A cyclophilin function in Hsp90-dependent signal transduction. Science. 1996;274:1713-5 pubmed
    b>Cpr6 and Cpr7, the Saccharomyces cerevisiae homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways...
  2. Johnson J, Zuehlke A, Tenge V, Langworthy J. Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones. Curr Genet. 2014;60:265-76 pubmed publisher
    ..Negative effects of CPR6 overexpression were similarly observed in cells expressing the temperature-sensitive mutation cns1-G90D...
  3. Li J, Richter K, Reinstein J, Buchner J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat Struct Mol Biol. 2013;20:326-31 pubmed publisher
    ..yeast Hsp90 chaperone cycle and identified a critical ternary Hsp90 complex containing the co-chaperones Aha1 and Cpr6. Aha1 accelerates the intrinsically slow conformational transitions of Hsp90 to an N-terminally associated state ..
  4. Ansari H, Greco G, Luban J. Cyclophilin A peptidyl-prolyl isomerase activity promotes ZPR1 nuclear export. Mol Cell Biol. 2002;22:6993-7003 pubmed
    ..Our results demonstrate a functional interaction between Cpr1p, Zpr1p, and EF1alpha, a role for Cpr1p in Zpr1p nuclear export, and a biological function for Cpr1p PPIase activity. ..
  5. Richter K, Walter S, Buchner J. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol. 2004;342:1403-13 pubmed
    ..Ternary complexes of Hsp90Sba1 could be formed with the prolyl isomerase Cpr6, but not with Sti1...
  6. Beaufour M, Godin F, Vallee B, Cadene M, Bénédetti H. Interaction proteomics suggests a new role for the Tfs1 protein in yeast. J Proteome Res. 2012;11:3211-8 pubmed publisher
    ..Integration of these results with known functional partners of Tfs1p shows that two subnetworks meet through the Tfs1p node, suggesting that it may act as a bridge between cell signaling and intermediate metabolism in yeast. ..
  7. Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J Biol Chem. 2003;278:10328-33 pubmed
    ..The first 24 amino acids of Hsp90, a region shown previously to be important for the association of the N-terminal domains and stimulation of ATP hydrolysis, seems to be important for this interaction. ..
  8. Zuehlke A, Johnson J. Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics. 2012;191:805-14 pubmed publisher
    ..Hsp90 undergoes a complex series of conformational changes and interacts with partner co-chaperones such as Sba1, Cpr6, Cpr7, and Cns1 as it binds and hydrolyzes ATP...
  9. Johnson J, Halas A, Flom G. Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol Cell Biol. 2007;27:768-76 pubmed
    ..interactions with cochaperone proteins, we monitored assembly of wild-type and mutant Hsp90 with Sti1, Sba1, and Cpr6 in Saccharomyces cerevisiae cell extracts...

More Information


  1. Li J, Richter K, Buchner J. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol. 2011;18:61-6 pubmed publisher
    ..This mechanism, which is strictly conserved between the yeast and human Hsp90 systems, presents an example of how, in a cyclic process, directionality of assembly and disassembly of protein complexes can be achieved. ..
  2. Catlett M, Kaplan K. Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J Biol Chem. 2006;281:33739-48 pubmed
    ..The multidomain nature of Sgt1p and its ability to bridge the interaction between Skp1p and Hsp82p argue that Sgt1p acts as a "client adaptor" recruiting specific clients to Hsp82p co-chaperone complexes. ..
  3. Zuehlke A, Wren N, Tenge V, Johnson J. Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis. J Biol Chem. 2013;288:27406-14 pubmed publisher
    ..Many of the Hsp90 co-chaperones, including Cpr6 and Cpr7, contain tetratricopeptide repeat (TPR) domains that bind a common acceptor site at the carboxyl terminus ..
  4. Mayr C, Richter K, Lilie H, Buchner J. Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J Biol Chem. 2000;275:34140-6 pubmed
    ..In Saccharomyces cerevisiae, two closely related large Hsp90-associated PPIases, Cpr6 and Cpr7, exist...
  5. Arevalo Rodriguez M, Cardenas M, Wu X, Hanes S, Heitman J. Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J. 2000;19:3739-49 pubmed
    ..Our findings support a model in which Ess1 and cyclophilin A modulate the activity of the Sin3-Rpd3 complex, and excess histone deacetylation causes mitotic arrest in ess1 mutants. ..
  6. Warth R, Briand P, Picard D. Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation. Biol Chem. 1997;378:381-91 pubmed
    ..At the amino acid level, this novel yeast cyclophilin, termed Cyp40, is 47% identical to human cyclophilin-40...
  7. Duina A, Marsh J, Gaber R. Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth. Yeast. 1996;12:943-52 pubmed
    We report the analysis of two Saccharomyces cerevisiae cyclophilins, Cpr6 and Cpr7, identified by their ability to interact in vivo with the transcriptional regulator Rpd3...
  8. Prodromou C, Siligardi G, O Brien R, Woolfson D, Regan L, Panaretou B, et al. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J. 1999;18:754-62 pubmed
    ..We have now analysed the interaction of the yeast TPR-domain co-chaperones Sti1 and Cpr6 with yeast Hsp90 by isothermal titration calorimetry, circular dichroism spectroscopy and analytical ..
  9. Paul A, Garcia Y, Zierer B, Patwardhan C, Gutierrez O, Hildenbrand Z, et al. The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors. J Biol Chem. 2014;289:15297-308 pubmed publisher
    ..Taken together, our data suggest a role for SGTA at distinct steps in the chaperone-dependent modulation of androgen, glucocorticoid, and progesterone receptor activity...
  10. Tenge V, Zuehlke A, Shrestha N, Johnson J. The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome. Eukaryot Cell. 2015;14:55-63 pubmed publisher
    ..We found that Cpr6, Cpr7, and Cns1 interact with the intact ribosome and that Saccharomyces cerevisiae lacking CPR7 or containing ..