Background: Hsp90 and co-chaperones are critical for the folding and activation of client proteins. Results: Hsp90 and Cpr6, but not other tetratricopeptide repeat (TPR)-containing co-chaperones, interact with Ura2. Conclusion: The TPR domain of Cpr6 has unique functions, including interaction with Ura2, an enzyme required for pyrimidine biosynthesis. Significance: Identification of co-chaperone-specific interactions is crucial to understanding how to selectively target Hsp90 functions.

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