Role of the EF-hand-like Motif in the 14-3-3 Protein-mediated Activation of Yeast Neutral Trehalase Nth1*

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10210830" target="_blank" >RIV/00216208:11310/14:10210830 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/14:00428949 RIV/61388971:_____/14:00428949 RIV/00216208:11130/14:10210830
Result on the web
<a href="http://www.jbc.org/content/early/2014/04/08/jbc.M113.544551.full.pdf+html" target="_blank" >http://www.jbc.org/content/early/2014/04/08/jbc.M113.544551.full.pdf+html</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M113.544551" target="_blank" >10.1074/jbc.M113.544551</a>

Result language
angličtina
Original language name
Role of the EF-hand-like Motif in the 14-3-3 Protein-mediated Activation of Yeast Neutral Trehalase Nth1*
Original language description
Trehalases hydrolyze the non-reducing disaccharide trehalose amassed by cells as a universal protectant and storage carbohydrate. Recently, it has been shown that the activity of neutral trehalase Nth1 from Saccharomyces cerevisiae is mediated by the 14-3-3 protein binding that modulates the structure of both the catalytic domain and the region containing the EFhand-like motif, whose role in the activation of Nth1 is unclear. In this work, the structure of the Nth114-3-3 complex and the importance of the EF-hand-like motif were investigated using site-directed mutagenesis, hydrogen/deuterium exchange coupled to mass spectrometry, chemical cross-linking, and small angle x-ray scattering. The low resolution structural views of Nth1 alone and the Nth114-3-3 complex show that the 14-3-3 protein binding induces a significant structural rearrangement of the whole Nth1 molecule. The EF-hand-like motif containing region forms a separate domain that interacts with both the 14-3-3 protein and th
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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