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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

  • Czech description

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

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

  • 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