Novel entropically driven conformation-specific interactions with Tomm34 modulate Hsp70 folding and ATPase activities
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F16%3AN0000021" target="_blank" >RIV/00209805:_____/16:N0000021 - isvavai.cz</a>
Result on the web
<a href="http://www.mcponline.org/content/15/5/1710.long" target="_blank" >http://www.mcponline.org/content/15/5/1710.long</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/mcp.M116.058131" target="_blank" >10.1074/mcp.M116.058131</a>
Alternative languages
Result language
angličtina
Original language name
Novel entropically driven conformation-specific interactions with Tomm34 modulate Hsp70 folding and ATPase activities
Original language description
Co-chaperones containing TPR domains enable cooperation between Hsp70 and Hsp90 to maintain cellular proteostasis. Whilst details of the molecular interactions between some TPR domains and Hsps are known, we describe a novel mechanism by which Tomm34 interacts with and coordinates Hsp70 activities. In contrast to previously defined Hop, Tomm34 interaction is dependent on the Hsp70 chaperone cycle. Tomm34 binds Hsp70 in a complex process: anchorage of the Hsp70 C-terminus by TPR1 domain is accompanied by additional contacts formed exclusively in ATP-bound state of Hsp70 resulting in a high-affinity entropically driven interaction. Tomm34 induces structural changes in determinants within the Hsp70-lid subdomain, modulates Hsp70/Hsp40-mediated refolding and Hsp40-stimulated Hsp70 ATPase activity. Since Tomm34 recruits Hsp90 through its TPR2 domain, we propose a model in which Tomm34 enables Hsp70/Hsp90 scaffolding and influences the Hsp70 chaperone cycle, providing an additional role for co-chaperones that contain multiple TPR domains in regulating protein homeostasis.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Molecular and cellular proteomics
ISSN
1535-9476
e-ISSN
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Volume of the periodical
15
Issue of the periodical within the volume
5
Country of publishing house
US - UNITED STATES
Number of pages
18
Pages from-to
1710-1727
UT code for WoS article
000375686100017
EID of the result in the Scopus database
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