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The Assembly and Intermolecular Properties of the Hsp70-Tomm34-Hsp90 Molecular Chaperone Complex*

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10286928" target="_blank" >RIV/00216208:11310/14:10286928 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/14:00440365 RIV/00209805:_____/14:#0000511

  • Result on the web

    <a href="http://dx.doi.org/10.1074/jbc.M113.526046" target="_blank" >http://dx.doi.org/10.1074/jbc.M113.526046</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M113.526046" target="_blank" >10.1074/jbc.M113.526046</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The Assembly and Intermolecular Properties of the Hsp70-Tomm34-Hsp90 Molecular Chaperone Complex*

  • Original language description

    Background: Hsp70 and Hsp90 molecular chaperones associate with the network of co-chaperone proteins. Results: Tomm34 protein interacts with both Hsp70 and Hsp90 chaperones. Conclusion: Tomm34 scaffolds Hsp70/Hsp90 chaperones by their simultaneous binding. Significance: Tomm34 represents a novel Hsp70/Hsp90 co-chaperone. Maintenance of protein homeostasis by molecular chaperones Hsp70 and Hsp90 requires their spatial and functional coordination. The cooperation of Hsp70 and Hsp90 is influenced by theirinteraction with the network of co-chaperone proteins, some of which contain tetratricopeptide repeat (TPR) domains. Critical to these interactions are TPR domains that target co-chaperone binding to the EEVD-COOH motif that terminates Hsp70/Hsp90. Recently, the two-TPR domain-containing protein, Tomm34, was reported to bind both Hsp70 and Hsp90. Here we characterize the structural basis of Tomm34-Hsp70/Hsp90 interactions. Using multiple methods, including pull-down assays, fluorescence

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/ED2.1.00%2F03.0101" target="_blank" >ED2.1.00/03.0101: Regional Centre for Applied Molecular Oncology (RECAMO)</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2014

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    289

  • Issue of the periodical within the volume

    14

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    15

  • Pages from-to

    9887-9901

  • UT code for WoS article

    000333807000038

  • EID of the result in the Scopus database