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1: J Biol Chem. 1995 Sep 15;270(37):21793-9.Click here to read Links

BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisiae.

Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06536, USA.

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.

PMID: 7665600 [PubMed - indexed for MEDLINE]