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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Amino acid sensing by Ssy1.

P Poulsen¹, B Wu, R F Gaber

¹Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, Denmark.

Biochemical Society Transactions

|January 26, 2005

Summary

Saccharomyces cerevisiae senses amino acids using Ssy1, a protein that doesn't transport them. Gain-of-function mutations in SSY1 reveal sensing occurs independently of transport, likely via direct amino acid interaction.

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Area of Science:

Molecular and Cellular Biology
Yeast Genetics
Signal Transduction

Background:

Saccharomyces cerevisiae utilizes Gap1 and Ssy1 for sensing extracellular amino acids.
Ssy1, despite structural similarity to transporters, does not facilitate amino acid transport.
Amino acid sensing by Ssy1 triggers transcriptional induction of genes, including those for amino acid transporters, with leucine being a potent inducer.

Purpose of the Study:

To investigate the mechanism of amino acid sensing by Ssy1 in Saccharomyces cerevisiae.
To determine if amino acid transport is a prerequisite for Ssy1-mediated signaling.
To develop quantitative assays for measuring Ssy1-dependent amino acid sensing.

Main Methods:

Generation and characterization of gain-of-function mutations in the SSY1 gene using a potassium uptake selection system.
Analysis of Ssy1 function in response to various amino acids.
Development of quantitative sensing assays involving Stp1 proteolytic processing and Western blot analysis.

Main Results:

Gain-of-function mutations in SSY1 were identified, with some conferring inducer-independent signaling and others increasing apparent inducer affinity.
These findings demonstrate that amino acid transport is not required for Ssy1-mediated signaling.
Evidence supports direct interaction between Ssy1 and extracellular amino acids for sensing.

Conclusions:

Ssy1 functions as a direct sensor of extracellular amino acids, independent of transport activity.
The signal transduction pathway involves the proteolytic removal of an inhibitory domain from the transcriptional activator Stp1.
Quantitative assays utilizing Stp1 processing provide a method for measuring Ssy1-mediated sensing.