Allosteric Activation of Yeast Enzyme Neutral Trehalase by Calcium and 14-3-3 Protein

0504680 - FGÚ 2020 RIV CZ eng J - Journal Article
Alblová, Miroslava - Šmídová, Aneta - Kalábová, Dana - Santo Lentini, D. - Obšil, Tomáš - Obšilová, Veronika
Allosteric Activation of Yeast Enzyme Neutral Trehalase by Calcium and 14-3-3 Protein.
Physiological Research. Roč. 68, č. 2 (2019), s. 147-160. ISSN 0862-8408. E-ISSN 1802-9973
R&D Projects: GA ČR(CZ) GA17-00726S; GA MŠMT(CZ) ED1.1.00/02.0109
Research Infrastructure: CIISB - 90043
Institutional support: RVO:67985823
Keywords : 14-3-3 protein * trehalase * calcium * allostery * conformation * enzyme * crystal structure
OECD category: Biochemistry and molecular biology
Impact factor: 1.655, year: 2019
Method of publishing: Open access
http://www.biomed.cas.cz/physiolres/pdf/2019/68_147.pdf

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.
Permanent Link: http://hdl.handle.net/11104/0296260