The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range

Hannah Girstmair, Franziska Tippel, Abraham Lopez, Katarzyna Tych, Frank Stein, Per Haberkant, Philipp Werner Norbert Schmid, Dominic Helm, Matthias Rief, Michael Sattler and Johannes Buchner ()
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Hannah Girstmair: Technische Universität München
Franziska Tippel: Technische Universität München
Abraham Lopez: Technische Universität München
Katarzyna Tych: Technische Universität München
Frank Stein: Proteomics Core Facility, EMBL Heidelberg
Per Haberkant: Proteomics Core Facility, EMBL Heidelberg
Philipp Werner Norbert Schmid: Technische Universität München
Dominic Helm: Proteomics Core Facility, EMBL Heidelberg
Matthias Rief: Technische Universität München
Michael Sattler: Technische Universität München
Johannes Buchner: Technische Universität München

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract The molecular chaperone Hsp90 is an important regulator of proteostasis. It has remained unclear why S. cerevisiae possesses two Hsp90 isoforms, the constitutively expressed Hsc82 and the stress-inducible Hsp82. Here, we report distinct differences despite a sequence identity of 97%. Consistent with its function under stress conditions, Hsp82 is more stable and refolds more efficiently than Hsc82. The two isoforms also differ in their ATPases and conformational cycles. Hsc82 is more processive and populates closed states to a greater extent. Variations in the N-terminal ATP-binding domain modulate its dynamics and conformational cycle. Despite these differences, the client interactomes are largely identical, but isoform-specific interactors exist both under physiological and heat shock conditions. Taken together, changes mainly in the N-domain create a stress-specific, more resilient protein with a shifted activity profile. Thus, the precise tuning of the Hsp90 isoforms preserves the basic mechanism but adapts it to specific needs.

Date: 2019
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DOI: 10.1038/s41467-019-11518-w

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