Y. Jiang et al., BTS1 ENCODES A GERANYLGERANYL DIPHOSPHATE SYNTHASE IN SACCHAROMYCES-CEREVISIAE, The Journal of biological chemistry, 270(37), 1995, pp. 21793-21799
Protein prenylation utilizes different types of isoprenoids groups, na
mely 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 protein
s are geranylgeranylated. Geranylgeranylation is catalyzed by two diff
erent prenyltransferases, the type I and type II geranylgeranyl transf
erases, both of which utilize geranylgeranyl diphosphate as a lipid do
nor. In the yeast Saccharomyces cerevisiae, the BET2 gene encodes the
beta-subunit of the type II geranylgeranyl transferase. Mutations in t
his gene cause a defect in the geranylgeranylation of small GTP-bindin
g proteins that mediate vesicular traffic. In an attempt to analyze th
ose genes whose products may interact with Bet2, we isolated a suppres
sor of the bet2-1 mutant. This suppressor gene, called BTS1, encodes t
he yeast geranylgeranyl diphosphate synthase. BTS1 is not essential fo
r the vegetative growth of cells; however, disrupting it impedes the g
eranylgeranylation of many cellular proteins and renders cells cold se
nsitive for growth. Our findings imply that BTS1 suppresses the bet2-1
mutant by increasing the intracellular pool of geranylgeranyl diphosp
hate.