Allosteric activation of yeast enzyme neutral trehalase by Calcium and 14-3-3 Protein

Title:

Allosteric activation of yeast enzyme neutral trehalase by Calcium and 14-3-3 Protein

Creator:

Alblova, M. , Smidova, A., Kalabova, D., Lentini Santo, D., Obsil, T., and Obsilova, V.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:ff19b326-76c6-4cae-9423-39769b057f7d
uuid:ff19b326-76c6-4cae-9423-39769b057f7d
doi:10.33549/physiolres.933950

Subject:

14-3-3 protein, Trehalase, Calcium, Trehalose, Allostery, Conformation, Enzyme, and Crystal structure

Type:

model:article and TEXT

Format:

bez média and svazek

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.

Language:

English

Rights:

http://creativecommons.org/publicdomain/mark/1.0/
policy:public

Coverage:

147-160

Source:

Physiological research | 2019 Volume:68 | Number:2

Harvested from:

CDK

Metadata only:

false