Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein
Jazyk angličtina Země Česko Médium print-electronic
Typ dokumentu časopisecké články, přehledy
PubMed
30628830
DOI
10.33549/physiolres.933950
PII: 933950
Knihovny.cz E-zdroje
- MeSH
- alosterická regulace fyziologie MeSH
- proteiny 14-3-3 chemie metabolismus MeSH
- Saccharomyces cerevisiae MeSH
- sekundární struktura proteinů MeSH
- trehalasa chemie metabolismus MeSH
- vápník chemie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- proteiny 14-3-3 MeSH
- trehalasa MeSH
- vápník MeSH
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 Ca(2+) 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.
Citace poskytuje Crossref.org