SAM2/YDR502C Summary Help

SAM2 BASIC INFORMATION

Standard Name SAM2 1
Systematic Name YDR502C
Alias ETH2
Feature Type ORF, Verified
Description S-adenosylmethionine synthetase, catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; one of two differentially regulated isozymes (Sam1p and Sam2p) (2, 3 and see Summary Paragraph)
Name Description S-AdenosylMethionine requiring 4
GO Annotations All SAM2 GO evidence and references
    View Computational GO annotations for SAM2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Pathways
Mutant Phenotype All SAM2 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions SAM2 All interactions details and references
34 total interaction(s) for 20 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-Western: 1
  • Two-hybrid: 3
Genetic Interactions
  • Dosage Rescue: 2
  • Phenotypic Enhancement: 3
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 4
Sequence Information
ChrIV:1454457 to 1453303 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2008-06-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1155 1454457..1453303 2008-06-05 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002910

SAM2 RESOURCES

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SGD ORF map
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for SAM2

SUMMARY PARAGRAPH for SAM2

SAM1 and SAM2 encode S-adenosylmethionine (AdoMet) synthetases (also known as methionine adenosyl transferases (MAT)), which catalyze the biosynthesis of AdoMet from methionine and ATP (4). AdoMet is involved in the methylation of proteins, RNAs, and lipids (5) as well as in the biosynthesis of biotin (6) and polyamines (7, 8). AdoMet is believed to participate in more reactions than any other cofactor with the exception of ATP (5).

Mutations in SAM1 or SAM2 do not affect growth; however, a sam1 sam2 double mutant results in AdoMet auxotrophy (4). Although SAM1 and SAM2 encode functionally equlvalent AdoMet synthetases, they are regulated differently (2). Both SAM1 and SAM2 are repressed by excess AdoMet, but expression of SAM2 increases during growth, which overrides the AdoMet-mediated repression (2). In addition, SAM2 is repressed by the addition of myo-inositol and choline, similar to a number of genes encoding enzymes involved in phospholipid biosynthesis (3). In contrast, SAM1 is not subject to the inositol-choline regulation suggesting that SAM2, but not SAM1, may be involved in phospholipid biosynthesis (3).

AdoMet synthetase is well conserved through evolution (from 2). In humans, deficiency in AdoMet synthetase results in the metabolic disease, hypermethioninemia (OMIM)(9).

Last updated: 2009-02-26

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for SAM2]

1) Rosenberg, N. and Rothstein, R.  (1992) Personal Communication, Mortimer Map Edition 11
2) Thomas D and Surdin-Kerjan Y  (1991) The synthesis of the two S-adenosyl-methionine synthetases is differently regulated in Saccharomyces cerevisiae. Mol Gen Genet 226(1-2):224-32
3) Kodaki T, et al.  (2003) Differential transcriptional regulation of two distinct S-adenosylmethionine synthetase genes (SAM1 and SAM2) of Saccharomyces cerevisiae. Nucleic Acids Res Suppl(3):303-4
4) Cherest H and Surdin-Kerjan Y  (1978) S-adenosyl methionine requiring mutants in Saccharomyces cerevisiae: evidences for the existence of two methionine adenosyl transferases. Mol Gen Genet 163(2):153-67
5) Thomas D and Surdin-Kerjan Y  (1997) Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 61(4):503-32
6) Phalip V, et al.  (1999) Characterization of the biotin biosynthesis pathway in Saccharomyces cerevisiae and evidence for a cluster containing BIO5, a novel gene involved in vitamer uptake. Gene 232(1):43-51
7) Chattopadhyay MK, et al.  (2006) Methylthioadenosine and polyamine biosynthesis in a Saccharomyces cerevisiae meu1delta mutant. Biochem Biophys Res Commun 343(1):203-7
8) Subhi AL, et al.  (2003) Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites. J Biol Chem 278(50):49868-73
9) Foury F  (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10