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SER1  -  O-phospho-L-serine:2-oxoglutarate...

Saccharomyces cerevisiae S288c

Synonyms: PSAT, Phosphohydroxythreonine aminotransferase, Phosphoserine aminotransferase, SERC, YOR184W
 
 
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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

 

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

 

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

  1. Ser3p (Yer081wp) and Ser33p (Yil074cp) are phosphoglycerate dehydrogenases in Saccharomyces cerevisiae. Albers, E., Laizé, V., Blomberg, A., Hohmann, S., Gustafsson, L. J. Biol. Chem. (2003) [Pubmed]
  2. Characterization of serine and leucine tRNAs in an asporogenic yeast Candida cylindracea and evolutionary implications of genes for tRNA(Ser)CAG responsible for translation of a non-universal genetic code. Suzuki, T., Ueda, T., Yokogawa, T., Nishikawa, K., Watanabe, K. Nucleic Acids Res. (1994) [Pubmed]
  3. Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis from Arabidopsis. Ho, C.L., Noji, M., Saito, M., Yamazaki, M., Saito, K. Plant J. (1998) [Pubmed]
  4. Genetics of the synthesis of serine from glycine and the utilization of glycine as sole nitrogen source by Saccharomyces cerevisiae. Sinclair, D.A., Dawes, I.W. Genetics (1995) [Pubmed]
  5. "Active" one-carbon generation in Saccharomyces cerevisiae. Ogur, M., Liu, T.N., Cheung, I., Paulavicius, I., Wales, W., Mehnert, D., Blaise, D. J. Bacteriol. (1977) [Pubmed]
  6. Molecular analysis of the yeast SER1 gene encoding 3-phosphoserine aminotransferase: regulation by general control and serine repression. Melcher, K., Rose, M., Künzler, M., Braus, G.H., Entian, K.D. Curr. Genet. (1995) [Pubmed]
  7. ade9 is an allele of SER1 and plays an indirect role in purine biosynthesis. Buc, P.S., Rolfes, R.J. Yeast (1999) [Pubmed]
  8. A gene from Saccharomyces cerevisiae which codes for a protein with significant homology to the bacterial 3-phosphoserine aminotransferase. Belhumeur, P., Fortin, N., Clark, M.W. Yeast (1994) [Pubmed]
  9. Genetic analysis of serine biosynthesis and glucose repression in yeast. Melcher, K., Entian, K.D. Curr. Genet. (1992) [Pubmed]
  10. Disruption of cytoplasmic and mitochondrial folylpolyglutamate synthetase activity in Saccharomyces cerevisiae. DeSouza, L., Shen, Y., Bognar, A.L. Arch. Biochem. Biophys. (2000) [Pubmed]
 
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