ADE12/YNL220W Summary Help

Standard Name ADE12 1
Systematic Name YNL220W
Alias BRA9 2
Feature Type ORF, Verified
Description Adenylosuccinate synthase; catalyzes the first step in synthesis of adenosine monophosphate from inosine 5'monophosphate during purine nucleotide biosynthesis; exhibits binding to single-stranded autonomously replicating (ARS) core sequence (3, 4, 5 and see Summary Paragraph)
Name Description ADEnine requiring
Chromosomal Location
ChrXIV:234413 to 235714 | ORF Map | GBrowse
Genetic position: -151 cM
Gene Ontology Annotations All ADE12 GO evidence and references
  View Computational GO annotations for ADE12
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 12 genes
Classical genetics
reduction of function
Large-scale survey
31 total interaction(s) for 26 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 10
  • Affinity Capture-RNA: 4
  • Protein-peptide: 8
  • Reconstituted Complex: 2
  • Two-hybrid: 1

Genetic Interactions
  • Phenotypic Enhancement: 1
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 4

Expression Summary
Length (a.a.) 433
Molecular Weight (Da) 48,279
Isoelectric Point (pI) 8.34
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIV:234413 to 235714 | ORF Map | GBrowse
Genetic position: -151 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1302 234413..235714 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005164

ADE12 encodes adenylosuccinate synthase (1, 3), which catalyzes the first step in the conversion of inosine monophosphate (IMP) to adenosine monophosphate (AMP) in the purine nucleotide biosynthetic pathway (see pathway diagram). Ade12p also exhibits single-stranded DNA-binding activity, with high specificity for the single-stranded T-rich region of the core ARS (autonomously replicating sequence; 6, 5). The DNA binding activity, but not the enzymatic activity, is abolished by dephosphorylation of Ade12p, suggesting that binding could be regulated by phosphorylation state (5). Ade12p has been localized to the cytoplasm, and the significance of the DNA binding activity is unclear (7).

Mutations in ade12 that reduce or abolish enzymatic activity cause adenine auxotrophy, and even when supplemented with adenine cultures of mutant cells do not exhibit wild-type growth rates (1). ade12 mutants also accumulate inosine and excrete hypoxanthine (1), and they germinate poorly (2, 1).

Expression of ADE12 and most of the other purine biosynthetic genes is repressed by adenine and activated by transcription factors Bas1p and Pho2p (8, 9). The main mechanism of ADE12 regulation appears to be transcriptional, as studies of purified overexpressed Ade12p indicate that adenylosuccinate synthase activity is not tightly regulated by precursors, intermediates or products of the purine-synthesizing pathway (3).

Ade12p orthologs have been identified in archaea, E. coli, S. pombe, D. discoideum, and humans (10, 11, 12). The enzymes from E. coli and Dictyostelium do not exhibit single-stranded ARS-specific binding (5).

Last updated: 2007-04-06 Contact SGD

References cited on this page View Complete Literature Guide for ADE12
1) Dorfman BZ  (1969) The isolation of adenylosuccinate synthetase mutants in yeast by selection for constitutive behavior in pigmented strains. Genetics 61(2):377-89
2) Guetsova ML, et al.  (1997) The isolation and characterization of Saccharomyces cerevisiae mutants that constitutively express purine biosynthetic genes. Genetics 147(2):383-97
3) Lipps G and Krauss G  (1999) Adenylosuccinate synthase from Saccharomyces cerevisiae: homologous overexpression, purification and characterization of the recombinant protein. Biochem J 341 ( Pt 3)():537-43
4) Jones EW and Fink GR  (1982) "Regulation of amino acid and nucleotide biosynthesis in yeast." Pp.181-299 in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
5) Gallert KC, et al.  (1996) Enzymatic properties and inhibition by single-stranded autonomously replicating sequences of adenylosuccinate synthase from Saccharomyces cerevisiae. Eur J Biochem 239(2):487-93
6) Zeidler R, et al.  (1993) Characterization of two novel single-stranded DNA-specific autonomously replicating sequence-binding proteins from Saccharomyces cerevisiae, one of which is adenylosuccinate synthetase. J Biol Chem 268(27):20191-7
7) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
8) Daignan-Fornier B and Fink GR  (1992) Coregulation of purine and histidine biosynthesis by the transcriptional activators BAS1 and BAS2. Proc Natl Acad Sci U S A 89(15):6746-50
9) Denis V, et al.  (1998) Role of the myb-like protein bas1p in Saccharomyces cerevisiae: a proteome analysis. Mol Microbiol 30(3):557-66
10) Powell SM, et al.  (1992) Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett 303(1):4-10
11) Bouyoub A, et al.  (1996) The adenylosuccinate synthetase from the hyperthermophilic archaeon Pyrococcus species displays unusual structural features. J Mol Biol 261(2):144-54
12) Nagy M, et al.  (1973) Regulation of the biosynthesis of purine nucleotides in Schizosaccharomyces pombe. 3. Kinetic studies of adenylosuccinate synthetase. Biochim Biophys Acta 309(1):1-10