High impact information on SER1

• Thus, in cells grown on ethanol both expression and activity of all SER-encoded proteins are low, including the remaining enzymes of the phosphoglycerate pathway, Ser1p and Ser2p [1].
• One of the serine tRNAs (Ser1) has already been demonstrated to have the anticodon CAG and to be responsible for translation of the codon CUG in C.cylindracea [2].
• A cDNA encoding plastidic phosphoserine aminotransferase (PSAT) which catalyzes the formation of phosphoserine from phosphohydroxypyruvate has been isolated from Arabidopsis thaliana [3].
• The effect of mutations in LPD1 (L-subunit of GDC), SER1 (synthesis of serine from 3-phosphoglycerate), ADE3 (cytoplasmic synthesis of one-carbon units for the serine synthesis from glycine), and all combinations of each has been determined [4].
• A new mutation introducing a one-carbon requirement (e.g., formate) for the glycine-supplemented growth of a serine-glycine auxotroph (ser1) was correlated with a lack of glycine decarboxylase activity [5].

Biological context of SER1

• 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 [6].
• A minimal functional construct of SER1 is necessary and sufficient to complement both the adenine- and serine-requiring phenotypes of ade9 strains [7].
• The SER1 locus, encoding 3-phosphoserine aminotransferase required for serine biosynthesis, is located on chromosome XV and resides approximately where ade9 had previously been mapped genetically [7].
• In this report, we present the sequence for this yeast SERC, and evidence that its deletion from the yeast genome leads to serine dependency [8].
• During the sequencing of the gene GSP2 from Saccharomyces cerevisiae, we have encountered an adjacent open reading frame having strong homology to the 3-phosphoserine aminotransferase (E.C.2.6.1.52) from other organisms [8].

Associations of SER1 with chemical compounds

• Molecular analysis of the yeast SER1 gene encoding 3-phosphoserine aminotransferase: regulation by general control and serine repression [6].
• A previously described mammalian progesterone-induced protein shares 47% similarity with SER1 over the entire protein, indicating a common function for both proteins [6].
• ade9 is an allele of SER1 and plays an indirect role in purine biosynthesis [7].
• The ser1 ser2 ser10 triple mutants were totally serine auxotrophic on glucose media but serine prototrophic during growth on non-fermentable carbon sources [9].

Regulatory relationships of SER1

• We demonstrate that SER1 transcription is regulated by the general control of amino-acid biosynthesis mediated by GCN4 [6].
• A met7 ser1 strain cannot use glycine to suppress the serine auxotrophy of the ser1 phenotype [10].

Other interactions of SER1

• Additionally, DNaseI protection experiments proved the binding of GCN4 protein to the SER1 promoter in vitro and three GCN4 recognition elements (GCREs) were identified [6].
• Mutagenesis of a ser1 ser2 cat1 triple mutant facilitated the isolation of a mutation in a new gene, SER10 [9].

Analytical, diagnostic and therapeutic context of SER1

• In situ hybridization analysis of PSAT revealed that the gene is generally expressed in all types of cells with a significantly higher amount in the meristem tissue of root tips [3].

References