Protein prenylation utilizes different types of isoprenoids groups, namely farnesyl and geranylgeranyl, to modify proteins. These lipophilic moieties attach to carboxyl-terminal cysteine residues to promote the association of soluble proteins to membranes. Most prenylated proteins are geranylgeranylated. Geranylgeranylation is catalyzed by two different prenyltransferases, the type I and type II geranylgeranyl transferases, both of which utilize geranylgeranyl diphosphate as a lipid donor. In the yeast Saccharomyces cerevisiae, the BET2 gene encodes the beta-subunit of the type II geranylgeranyl transferase. Mutations in this gene cause a defect in the geranylgeranylation of small GTP-binding proteins that mediate vesicular traffic. In an attempt to analyze those genes whose products may interact with Bet2, we isolated a suppressor of the bet2-1 mutant. This suppressor gene, called BTS1, encodes the yeast geranylgeranyl diphosphate synthase. BTS1 is not essential for the vegetative growth of cells; however, disrupting it impedes the geranylgeranylation of many cellular proteins and renders cells cold sensitive for growth. Our findings imply that BTS1 suppresses the bet2-1 mutant by increasing the intracellular pool of geranylgeranyl diphosphate.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Annotation Extension||Reference|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Assay||Construct||Conditions||Strain Background||Reference|