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
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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
EE - Microbiology, virology
OECD FORD branch
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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
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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
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