Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein.

Allosteric activation of yeast enzyme neutral trehalase by calcium and 14-3-3 protein.
Physiol Res. 2019 Jan 10;
Authors: Alblova M, Smidova A, Kalabova D, Lentini Santo D, Obsil T, Obsilova V
Abstract
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.
PMID: 30628830 [PubMed - as supplied by publisher]

Source: Physiological Research - January 10, 2019 Category: Physiology Authors: Alblova M, Smidova A, Kalabova D, Lentini Santo D, Obsil T, Obsilova V Tags: Physiol Res Source Type: research