Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. IV. Evidence for a general amino acid permease.
Kinetic and genetic evidences are presented to show that, in addition to specific amino acid permeases, Saccharomyces cerevisiae has a general amino acid permease which catalyzes the transport of basic and neutral amino acids, but most probably not that of proline. The general amino acid permease appears to be constitutive, and its activity is inhibited when ammonium ions are added to the culture medium. A mutant which has lost the general amino acid permease activity was isolated. Its mutation, named gap (general amino acid permease), is not allelic to the aap (amino acid permease) mutation of Surdin et al., which has a quite different phenotype and cannot be considered as having selectively lost the general amino acid permease activity.
D000596:Amino Acids / Q000378:metabolism; D002247:Carbon Isotopes; D003470:Culture Media; D005827:Genetics, Microbial; D007700:Kinetics; D049990:Membrane Transport Modulators; D026901:Membrane Transport Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008967:Molecular Biology; D009154:Mutation; D011392:Proline / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology; D012440:Saccharomyces / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D013431:Sulfates
D000596:Amino Acids; D002247:Carbon Isotopes; D003470:Culture Media; D049990:Membrane Transport Modulators; D026901:Membrane Transport Proteins; D000644:Quaternary Ammonium Compounds; D013431:Sulfates; D011392:Proline