The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range.
Adenosine Triphosphatases
/ metabolism
Amino Acid Sequence
HSP90 Heat-Shock Proteins
/ chemistry
Heat-Shock Response
/ physiology
Ligands
Models, Molecular
Molecular Chaperones
/ chemistry
Protein Binding
Protein Conformation
Protein Folding
Protein Isoforms
/ chemistry
Protein Stability
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ chemistry
Sequence Alignment
Stress, Physiological
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
09 08 2019
09 08 2019
Historique:
received:
24
01
2019
accepted:
19
07
2019
entrez:
11
8
2019
pubmed:
11
8
2019
medline:
18
12
2019
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31399574
doi: 10.1038/s41467-019-11518-w
pii: 10.1038/s41467-019-11518-w
pmc: PMC6689086
doi:
Substances chimiques
HSP82 protein, S cerevisiae
0
HSP90 Heat-Shock Proteins
0
Ligands
0
Molecular Chaperones
0
Protein Isoforms
0
Saccharomyces cerevisiae Proteins
0
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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