Allosteric Activation of Yeast Enzyme Neutral Trehalase by Calcium and 14-3-3 Protein
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F19%3A00504680" target="_blank" >RIV/67985823:_____/19:00504680 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/19:10396023
Result on the web
<a href="http://www.biomed.cas.cz/physiolres/pdf/2019/68_147.pdf" target="_blank" >http://www.biomed.cas.cz/physiolres/pdf/2019/68_147.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.33549/physiolres.933950" target="_blank" >10.33549/physiolres.933950</a>
Alternative languages
Result language
angličtina
Original language name
Allosteric Activation of Yeast Enzyme Neutral Trehalase by Calcium and 14-3-3 Protein
Original language description
Neutral trehalase 1 (Nth1) from Saccharomyces cerevisiae catalyzes disaccharide trehalose hydrolysis and helps yeast to survive adverse conditions, such as heat shock, starvation or oxidative stress. 14-3-3 proteins, master regulators of hundreds of partner proteins, participate in many key cellular processes. Nth1 is activated by phosphorylation followed by 14-3-3 protein (Bmh) binding. The activation mechanism is also potentiated by Ca2+ binding within the EF-hand-like motif. This review summarizes the current knowledge about trehalases and the molecular and structural basis of Nth1 activation. The crystal structure of fully active Nth1 bound to 14-3-3 protein provided the first high-resolution view of a trehalase from a eukaryotic organism and showed 14-3-3 proteins as structural modulators and allosteric effectors of multi-domain binding partners.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
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
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Physiological Research
ISSN
0862-8408
e-ISSN
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Volume of the periodical
68
Issue of the periodical within the volume
2
Country of publishing house
CZ - CZECH REPUBLIC
Number of pages
14
Pages from-to
147-160
UT code for WoS article
000465948800003
EID of the result in the Scopus database
2-s2.0-85065504477