Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae.
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.
Panni
Simona
S
Department of Biology, University of Rome Tor Vergata, Rome, Italy. panni@uniroma2.it
Landgraf
Christiane
C
Volkmer-Engert
Rudolf
R
Cesareni
Gianni
G
Castagnoli
Luisa
L
D048948:14-3-3 Proteins / Q000494:pharmacology*; D004268:DNA-Binding Proteins; D004789:Enzyme Activation / Q000187:drug effects*; D015966:Gene Expression Regulation, Fungal / Q000187:drug effects; D005800:Genes, Fungal; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism; D014198:Trehalase / Q000235:genetics / Q000378:metabolism*; D014199:Trehalose / Q000378:metabolism
D048948:14-3-3 Proteins; D004268:DNA-Binding Proteins; D014199:Trehalose; D014198:Trehalase