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Gene Review

SHM2  -  glycine hydroxymethyltransferase SHM2

Saccharomyces cerevisiae S288c

Synonyms: Glycine hydroxymethyltransferase, L2156, SHMT, SHMT2, Serine hydroxymethyltransferase, cytosolic, ...
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High impact information on SHM2

  • The genome-wide response to glycine revealed that several other genes are rapidly co-induced with the GCV genes, including SHM2, which encodes cytoplasmic serine hydroxymethyltransferase [1].
  • Unexpectedly, mutation of both cytosolic serine hydroxymethyltransferase (SHM2) and one-carbon tetrahydrofolate synthase (ADE3) was required to achieve synthetic lethality with srp40Delta [2].
  • Animals homozygous for the SHMT mutations have no observable mutant phenotype, but their offspring display an embryonic lethal phenotype [3].
  • The SHM2 gene but not the SHM1 gene has putative GCN4 sites upstream of the putative TATA box, suggesting regulation of its transcription by the general amino acid control system [4].
  • Complementation of the glycine auxotrophy using a yeast genomic library retrieved the SHM1 and SHM2 genes and a third gene designated GLY1 [4].

Biological context of SHM2

  • The genes encoding both the cytosolic and mitochondrial serine hydroxymethyltransferases (SHM2 and SHM1, respectively) and a third unidentified gene of the yeast Saccharomyces cerevisiae have been isolated and their nucleotide sequences determined [4].

Associations of SHM2 with chemical compounds

  • A number of genes, including BAS1 were required for activation by glycine but only the SHM2 gene was required for repression in the absence of glycine [5].
  • Glycine regulation was also found to be dependent on an intact SHM2 gene, which encodes cytoplasmic serine hydroxymethyltransferase [5].
  • Genes encoding the mitochondrial (SHM1) and cytosolic (SHM2) serine hydroxymethyltransferases, and the L-threonine aldolase gene (GLY1) from Candida albicans were cloned and sequenced [6].
  • Real-time quantitative PCR analyses comparing the wild type and the Deltabas1 mutant revealed that AgBAS1 was responsible for the adenine-mediated regulation of the purine and glycine pathways, since the transcription of the ADE4 and SHM2 genes was virtually abolished in the Deltabas1 mutant [7].
  • Northern analysis reveals that regulation of SHM2 and MTD1 expression by adenine takes place at the transcriptional level [8].


  1. Identification of a novel one-carbon metabolism regulon in Saccharomyces cerevisiae. Gelling, C.L., Piper, M.D., Hong, S.P., Kornfeld, G.D., Dawes, I.W. J. Biol. Chem. (2004) [Pubmed]
  2. Genetic interaction between a chaperone of small nucleolar ribonucleoprotein particles and cytosolic serine hydroxymethyltransferase. Yang, Y., Meier, U.T. J. Biol. Chem. (2003) [Pubmed]
  3. Serine hydroxymethyltransferase is maternally essential in Caenorhabditis elegans. Vatcher, G.P., Thacker, C.M., Kaletta, T., Schnabel, H., Schnabel, R., Baillie, D.L. J. Biol. Chem. (1998) [Pubmed]
  4. Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine. McNeil, J.B., McIntosh, E.M., Taylor, B.V., Zhang, F.R., Tang, S., Bognar, A.L. J. Biol. Chem. (1994) [Pubmed]
  5. Transcriptional regulation of the one-carbon metabolism regulon in Saccharomyces cerevisiae by Bas1p. Subramanian, M., Qiao, W.B., Khanam, N., Wilkins, O., Der, S.D., Lalich, J.D., Bognar, A.L. Mol. Microbiol. (2005) [Pubmed]
  6. Glycine metabolism in Candida albicans: characterization of the serine hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1) genes. McNeil, J.B., Flynn, J., Tsao, N., Monschau, N., Stahmann, K., Haynes, R.H., McIntosh, E.M., Pearlman, R.E. Yeast (2000) [Pubmed]
  7. Purine biosynthesis, riboflavin production, and trophic-phase span are controlled by a Myb-related transcription factor in the fungus Ashbya gossypii. Mateos, L., Jiménez, A., Revuelta, J.L., Santos, M.A. Appl. Environ. Microbiol. (2006) [Pubmed]
  8. Synthesis of glutamine, glycine and 10-formyl tetrahydrofolate is coregulated with purine biosynthesis in Saccharomyces cerevisiae. Denis, V., Daignan-Fornier, B. Mol. Gen. Genet. (1998) [Pubmed]
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