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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/67985823:_____/14:00428949 RIV/61388971:_____/14:00428949 RIV/00216208:11130/14:10210830

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Svazek periodika

289

Číslo periodika v rámci svazku

20

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

14

Strana od-do

13948-13961

Kód UT WoS článku

000335984600026

EID výsledku v databázi Scopus

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