Regulation of histidine uptake by specific feedback inhibition of two histidine permeases in Saccharomyces cerevisiae.
TLDR
It is concluded that the his-p1 mutant is histidine-permease-less, and that the activity of the histidine permeases are regulated by specific feedback inhibition.Abstract:
Although a large fraction of the histidine accumulated from the medium remains free and intact in Saccharomyces cerevisiae, it is not exchangeable with external histidine. Hence, the steady state concentration level of histidine is not determined by a balance between rates of inflow and outflow.
Preloading the cells with histidine results in a rapid inhibition of histidine uptake, whereas preloading with other amino acids has no effect on histidine uptake.
The inhibition by internal histidine affects the activity, and not the synthesis, of two specific histidine permeases. The histidine permease with high affinity for histidine is much more sensitive to this inhibition than the second histidine permease.
A mutant (his-p1) specifically affected in histidine uptake was isolated.
Criteria for demonstrating that a mutation or a feedback control directly affect an uptake system are discussed.
It is concluded that the his-p1 mutant is histidine-permease-less, and that the activity of the histidine permeases are regulated by specific feedback inhibition.read more
Citations
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Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. II. Evidence for a specific lysine-transporting system.
TL;DR: Kinetic and genetic evidences are presented to show that, in addition to specific amino acid permeases, Saccharomyces cerevisiae has a general amino acids permease which catalyzes the transport of basic and neutral amino acids, but most probably not that of proline.
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The regulation of amino acid transport in animal cells.
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Multiplicity of the Amino Acid Permeases in Saccharomyces cerevisiae IV. Evidence for a General Amino Acid Permease
M. Grenson,C. Hou,M. Crabeel +2 more
TL;DR: Kinetic and genetic evidences are presented to show that, in addition to specific amino acid permeases, Saccharomyces cerevisiae has a general amino acids permease which catalyzes the transport of basic and neutral amino acids, but most probably not that of proline.
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Nitrogen catabolite repression in yeasts and filamentous fungi.
Wiame Jm,Grenson M,Arst Hn +2 more
TL;DR: A brief description of nitrogen catabolite repression in Saccharomyces cerevisiae is provided and a mechanism, nitrogen metabolite repression of the syntheses of many enzymes and permeases involved in nitrogen nutrition, has been extensively studied in two filamentous fungi.
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An overview of membrane transport proteins in Saccharomyces cerevisiae.
TL;DR: All eukaryotic cells contain a wide variety of proteins embedded in the plasma and internal membranes, which ensure transmembrane solute transport, and a large proportion of these transport proteins can be grouped into families apparently conserved throughout organisms.
References
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Journal ArticleDOI
Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. II. Evidence for a specific lysine-transporting system.
TL;DR: Kinetic and genetic evidences are presented to show that, in addition to specific amino acid permeases, Saccharomyces cerevisiae has a general amino acids permease which catalyzes the transport of basic and neutral amino acids, but most probably not that of proline.
Journal ArticleDOI
Multiplicity of the amino acid permeases in Saccharomyces cerevisiae
Journal ArticleDOI
Chromosome Mapping in Saccharomyces: Centromere-Linked Genes.
Journal ArticleDOI
Uptake of amino acids by salmonella typhimurium.
TL;DR: The transport systems of Salmonella typhimurium for histidine and for the aromatic amino acids have been studied and a new parameter is introduced: the limit concentration, which represents the minimal external concentration of an amino acid at which the organism utilizes exclusively the external supply and completely stops the biosynthetic production of that amino acid.
Journal ArticleDOI
Mutations Affecting the Repressibility of Arginine Biosynthetic Enzymes in Sacchromyces cerevisiae
TL;DR: A method is described for isolating mutants of Saccharomyces cerevisiae which have lost repressibility by exogenous arginine for ornithine transcarbamylase and three complementary classes of mutations were found: argRI, argRII and argRIII which are recessive and define three loci.
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