Open AccessRole of 14‐3‐3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae
Author(s) -
Panni Simona,
Landgraf Christiane,
VolkmerEngert Rudolf,
Cesareni Gianni,
Castagnoli Luisa
Publication year - 2008
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2007.00312.x
Subject(s) - trehalase , saccharomyces cerevisiae , yeast , biology , biochemistry , enzyme , trehalose , gene isoform , phosphorylation , microbiology and biotechnology , gene
In higher eukaryotes, 14‐3‐3 proteins participate in numerous cellular processes, and carry out their function through a variety of different molecular mechanisms, including regulation of protein localization and enzyme activation. Here, it is shown that the two yeast 14‐3‐3 homologues, Bmh1p and Bmh2p, form a complex with neutral trehalase (Nth1p), an enzyme that is responsible for trehalose degradation and is required in a variety of stress conditions. In a purified in vitro system, either one of the two 14‐3‐3 yeast isoforms are necessary for complete activation of neutral trehalase (Nth1p) after phosphorylation by PKA. It is further demonstrated that Bmh1p and Bmh2p bind to the amino‐terminal region of phosphorylated trehalase, thereby modulating its enzymatic activity. This work represents the first demonstration of enzyme activation mediated by 14‐3‐3 binding in yeast.