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PMID: 10409731 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Ssy1p and Ptr3p are plasma membrane components of a yeast system that senses extracellular amino acids.

Molecular and cellular biology ·Vol. 19 ·No. 8 ·1999-08-00 ·Pages 5405-16

Klasson H, Fink GR, Ljungdahl PO

Abstract

Mutations in SSY1 and PTR3 were identified in a genetic selection for components required for the proper uptake and compartmentalization of histidine in Saccharomyces cerevisiae. Ssy1p is a unique member of the amino acid permease gene family, and Ptr3p is predicted to be a hydrophilic protein that lacks known functional homologs. Both Ssy1p and Ptr3p have previously been implicated in relaying signals regarding the presence of extracellular amino acids. We have found that ssy1 and ptr3 mutants belong to the same epistasis group; single and ssy1 ptr3 double-mutant strains exhibit indistinguishable phenotypes. Mutations in these genes cause the nitrogen-regulated general amino acid permease gene (GAP1) to be abnormally expressed and block the nonspecific induction of arginase (CAR1) and the peptide transporter (PTR2). ssy1 and ptr3 mutations manifest identical differential effects on the functional expression of multiple specific amino acid transporters. ssy1 and ptr3 mutants have increased vacuolar pools of histidine and arginine and exhibit altered cell growth morphologies accompanied by exaggerated invasive growth. Subcellular fractionation experiments reveal that both Ssy1p and Ptr3p are localized to the plasma membrane (PM). Ssy1p requires the endoplasmic reticulum protein Shr3p, the amino acid permease-specific packaging chaperonin, to reach the PM, whereas Ptr3p does not. These findings suggest that Ssy1p and Ptr3p function in the PM as components of a sensor of extracellular amino acids.

MeSH Terms
Alleles Amino Acid Transport Systems Amino Acids/metabolism Arginine/metabolism Biological Transport Carrier Proteins/genetics,physiology Diploidy Fungal Proteins/genetics,physiology Gene Expression Regulation, Fungal Haploidy Histidine/metabolism,pharmacology Intracellular Signaling Peptides and Proteins Macromolecular Substances Membrane Proteins/genetics,physiology Nitrogen/metabolism Protein Biosynthesis Proteins/genetics RNA, Fungal/biosynthesis RNA, Messenger/biosynthesis Recombinant Fusion Proteins/metabolism Saccharomyces cerevisiae/genetics,growth & development,metabolism Saccharomyces cerevisiae Proteins Sequence Deletion Signal Transduction/genetics,physiology Vacuoles/metabolism Vesicular Transport Proteins ras GTPase-Activating Proteins
Chemicals
Amino Acid Transport Systems Amino Acids Carrier Proteins Fungal Proteins GAP1 protein, S cerevisiae Intracellular Signaling Peptides and Proteins Macromolecular Substances Membrane Proteins PTR3 protein, S cerevisiae Proteins RNA, Fungal RNA, Messenger Recombinant Fusion Proteins SHR3 protein, S cerevisiae SSY1 protein, S cerevisiae Saccharomyces cerevisiae Proteins Vesicular Transport Proteins ras GTPase-Activating Proteins Histidine Arginine Nitrogen
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Klasson H
Ludwig Institute for Cancer Research, S-171 77 Stockholm, Sweden.
Fink G R
Ljungdahl P O
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1999-08-00
Pages
5405-16
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC84383
Subset
IM
Grants
NIGMS NIH HHS · R01 GM035010 · United States
NIGMS NIH HHS · R01 GM040266 · United States
NIGMS NIH HHS · GM35010 · United States
NIGMS NIH HHS · GM40266 · United States
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