ArticleThe Journal of biological chemistry2010
Amino acid signaling in yeast: post-genome duplication divergence of the Stp1 and Stp2 transcription factors.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 28 citations in OpenAlex.
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Coordinated regulation of pH alkalinization by two transcription factors promotes fungal commensalism and pathogenicity.Nature communications · 2025Article
- Research progress on the function and regulatory pathways of amino acid permeases in fungi.World journal of microbiology & biotechnology · 2024Review
- A universal system for boosting gene expression in eukaryotic cell-lines.Nature communications · 2024Article
- TheInternational journal of molecular sciences · 2023Article
- Spatial and temporal regulation of the endoproteolytic activity of the SPS-sensor-controlled Ssy5 signaling protease.Molecular biology of the cell · 2019Article
- Ssy5 is a signaling serine protease that exhibits atypical biogenesis and marked S1 specificity.The Journal of biological chemistry · 2018Article
- Regulation of Sensing, Transportation, and Catabolism of Nitrogen Sources in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2018Review
- Nutrient Sensing at the Plasma Membrane of Fungal Cells.Microbiology spectrum · 2017Review
- Reduced Ssy1-Ptr3-Ssy5 (SPS) signaling extends replicative life span by enhancing NAD+ homeostasis in Saccharomyces cerevisiae.The Journal of biological chemistry · 2015Article
- Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.FEMS microbiology reviews · 2014Review
- One Hand Clapping: detection of condition-specific transcription factor interactions from genome-wide gene activity data.Nucleic acids research · 2012Article
- Regulation of amino acid, nucleotide, and phosphate metabolism in Saccharomyces cerevisiae.Genetics · 2012Article
- A phosphodegron controls nutrient-induced proteasomal activation of the signaling protease Ssy5.Molecular biology of the cell · 2011Article
- Amino acid signaling in yeast: activation of Ssy5 protease is associated with its phosphorylation-induced ubiquitylation.The Journal of biological chemistry · 2011Article
- Differential regulation of transcription factors Stp1 and Stp2 in the Ssy1-Ptr3-Ssy5 amino acid sensing pathway.The Journal of biological chemistry · 2011Article
- Uga3 and Uga35/Dal81 transcription factors regulate UGA4 transcription in response to gamma-aminobutyric acid and leucine.Eukaryotic cell · 2010Article
- The prodomain of Ssy5 protease controls receptor-activated proteolysis of transcription factor Stp1.Molecular and cellular biology · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When yeast cells detect external amino acids via their permease-like Ssy1 sensor, the cytosolic precursor forms of Stp1 and Stp2 transcription factors are activated by endoproteolytic removal of their N-terminal domains, a reaction catalyzed by the Ssy5 endoprotease. The processed Stp factors then migrate into the nucleus, where they activate transcription of several amino acid permease genes including AGP1. We report here that the STP1 and STP2 genes most likely derive from the whole genome duplication that occurred in a yeast ancestor. Although Stp1 and Stp2 have been considered redundant, we provide evidence that they functionally diverged during evolution. Stp2 is the only factor processed when amino acids are present at low concentration, and the transcriptional activation of AGP1 promoted by Stp2 is moderate. Furthermore, only Stp2 can sustain Agp1-dependent utilization of amino acids at low concentration. In contrast, Stp1 is only processed when amino acids are present at high concentration, and it promotes higher level transcriptional activation of AGP1. Domain swapping experiments show that the N-terminal domains of Stp1 and Stp2 are responsible for these proteins being cleaved at different amino acid concentrations. Last, induction of the DIP5 permease gene by amino acids depends on Stp2 but not Stp1. We propose that post-whole genome duplication co-conservation of the STP1 and STP2 genes was favored by functional divergence of their products, likely conferring to cells an increased ability to adapt to various amino acid supply conditions.
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