ArticleCurrent genetics1995
Molecular analysis of the yeast SER1 gene encoding 3-phosphoserine aminotransferase: regulation by general control and serine repression.
Article in Current genetics, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 25 citations in OpenAlex.
- Molecular Structure of Phosphoserine Aminotransferase fromInternational journal of molecular sciences · 2023Article
- A yeast-based complementation assay elucidates the functional impact of 200 missense variants in human PSAT1.Journal of inherited metabolic disease · 2020Article
- Vitamin requirements and biosynthesis in Saccharomyces cerevisiae.Yeast (Chichester, England) · 2020Review
- Natural Variation inG3 (Bethesda, Md.) · 2018Article
- Natural variation of chronological aging in theNPJ aging and mechanisms of disease · 2018Article
- Identifying and assessing the impact of wine acid-related genes in yeast.Current genetics · 2016Article
- Article
- Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast.Molecular and cellular biology · 2001Article
- A chemical genomics approach toward understanding the global functions of the target of rapamycin protein (TOR).Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Global regulatory functions of Oaf1p and Pip2p (Oaf2p), transcription factors that regulate genes encoding peroxisomal proteins in Saccharomyces cerevisiae.Molecular and cellular biology · 1998Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Although serine and glycine are ubiquitous amino acids the genetic and biochemical regulation of their synthesis has not been studied in detail. The SER1 gene encodes 3-phosphoserine aminotransferase which catalyzes the formation of phosphoserine from 3-phosphohydroxy-pyruvate, which is obtained by oxidation of 3-phosphoglycerate, an intermediate of glycolysis. Saccharomyces cerevisiae cells provided with fermentable carbon sources mainly use this pathway (glycolytic pathway) to synthesize serine and glycine. We report the isolation of the SER1 gene by complementation and the disruption of the chromosomal locus. Sequence analysis revealed an open reading frame encoding a protein with a predicted molecular weight of 43,401 Da. A previously described mammalian progesterone-induced protein shares 47% similarity with SER1 over the entire protein, indicating a common function for both proteins. We demonstrate that SER1 transcription is regulated by the general control of amino-acid biosynthesis mediated by GCN4. Additionally, DNaseI protection experiments proved the binding of GCN4 protein to the SER1 promoter in vitro and three GCN4 recognition elements (GCREs) were identified. Furthermore, there is evidence for an additional regulation by serine end product repression.
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