title: The putative monocarboxylate permeases of the yeast Saccharomyces cerevisiae do not transport monocarboxylic acids across the plasma membrane.
abstract: We have characterized the monocarboxylate permease family of Saccharomyces cerevisiae comprising five proteins. We could not find any evidence that the monocarboxylate transporter-homologous (Mch) proteins of S. cerevisiae are involved in the uptake or secretion of monocarboxylates such as lactate, pyruvate or acetate across the plasma membrane. A yeast mutant strain deleted for all five MCH genes exhibited no growth defects on monocarboxylic acids as the sole carbon and energy sources. Moreover, the uptake and secretion rates of monocarboxylic acids were indistinguishable from the wild-type strain. Additional deletion of the JEN1 lactate transporter gene completely blocked uptake of lactate and pyruvate. However, uptake of acetate was not even affected after the additional deletion of the gene YHL008c, which had been proposed to code for an acetate transporter. The mch1-5 mutant strain showed strongly reduced biomass yields in aerobic glucose-limited chemostat cultures, pointing to the involvement of Mch transporters in mitochondrial metabolism. Indeed, intracellular localization studies indicated that at least some of the Mch proteins reside in intracellular membranes. However, pyruvate uptake into isolated mitochondria was not affected in the mch1-5 mutant strain. It is concluded that the yeast monocarboxylate transporter-homologous proteins perform other functions than do their mammalian counterparts.
authors.affiliation: Institut für Mikrobiologie, Heinrich-Heine-Universität, Universitätsstrasse 1, 40225 Düsseldorf, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Makuc
authors.forename: S
authors.initials: S
authors.lastname: Paiva
authors.forename: M
authors.initials: M
authors.lastname: Schauen
authors.forename: R
authors.initials: R
authors.lastname: Krämer
authors.forename: B
authors.initials: B
authors.lastname: André
authors.forename: M
authors.initials: M
authors.lastname: Casal
authors.forename: C
authors.initials: C
authors.lastname: Leão
authors.forename: E
authors.initials: E
authors.lastname: Boles
mesh_terms: D018533:Biomass; D002264:Carboxylic Acids / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal / Q000502:physiology; D005800:Genes, Fungal; D005947:Glucose / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism / Q000502:physiology; D027501:Monocarboxylic Acid Transporters / Q000235:genetics / Q000378:metabolism*; D016296:Mutagenesis; D016366:Open Reading Frames; D010101:Oxygen Consumption; D019289:Pyruvic Acid / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D001616:beta-Galactosidase / Q000032:analysis
chemical_list: D002264:Carboxylic Acids; D005656:Fungal Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D027501:Monocarboxylic Acid Transporters; D019289:Pyruvic Acid; D001616:beta-Galactosidase; D005947:Glucose