B. Holst et al., GUP1 and its close homologue GUP2, encoding multimembrane-spanning proteins involved in active glycerol uptake in Saccharomyces cerevisiae, MOL MICROB, 37(1), 2000, pp. 108-124
Many yeast species can utilize glycerol, both as a sole carbon source and a
s an osmolyte. In Saccharomyces cerevisiae, physiological studies have prev
iously shown the presence of an active uptake system driven by electrogenic
proton symport. We have used transposon mutagenesis to isolate mutants aff
ected in the transport of glycerol into the cell. Here we present the ident
ification of YGL084c, encoding a multimembrane-spanning protein, as being e
ssential for proton symport of glycerol into S. cerevisiae. The gene is nam
ed GUP1 (glycerol uptake) and, for growth on glycerol, is important as a ca
rbon and energy source. In addition, in strains deficient in glycerol produ
ction it also provides osmotic protection by the addition of glycerol. Anot
her open reading frame (ORF), YPL189w, presenting a high degree of homology
to YGL084c, similarly appears to be involved in active glycerol uptake in
salt-containing glucose-based media in strains deficient in glycerol produc
tion. Analogously, this gene is named GUP2. To our knowledge, this is the f
irst report on a gene product involved in active transport of glycerol in y
easts. Mutations with the same phenotypes occurred in two other ORFs of pre
viously unknown function, YDL074c and YPL180w.