MET3/YJR010W Summary Help

Standard Name MET3 1
Systematic Name YJR010W
Feature Type ORF, Verified
Description ATP sulfurylase; catalyzes the primary step of intracellular sulfate activation, essential for assimilatory reduction of sulfate to sulfide, involved in methionine metabolism (2, 3 and see Summary Paragraph)
Name Description METhionine requiring 1
Chromosomal Location
ChrX:456239 to 457774 | ORF Map | GBrowse
Gbrowse
Genetic position: 3 cM
Gene Ontology Annotations All MET3 GO evidence and references
  View Computational GO annotations for MET3
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 10 genes
Resources
Pathways
Classical genetics
null
Large-scale survey
null
Resources
20 total interaction(s) for 14 unique genes/features.
Physical Interactions
  • Co-crystal Structure: 1
  • PCA: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 5

Genetic Interactions
  • Negative Genetic: 1
  • Phenotypic Enhancement: 1
  • Positive Genetic: 5
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 511
Molecular Weight (Da) 57,724
Isoelectric Point (pI) 5.67
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrX:456239 to 457774 | ORF Map | GBrowse
SGD ORF map
Genetic position: 3 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1536 456239..457774 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003771
SUMMARY PARAGRAPH for MET3

MET3 encodes ATP sulfurylase, which catalyzes the initial step of the sulfur assimilation pathway (2 and reviewed in 4). The sulfur assimilation pathway leads to the formation of hydrogen sulfide, a precursor in the biosynthesis of homocysteine, cysteine, and methionine (5 and reviewed in 4). Met3p activates inorganic sulfate in an ATP-dependent reaction and forms the products adenosine-5'-phosphosulfate (APS) and pyrophosphate (PPi) (3 and references therein). The ATP sulfurylase enzyme is comprised of six Met3p subunits arranged in a formation of two stacked rings (3) and Met3p homooligomerazation is mediated by a domain in its C-terminus (6). The presence of methionine strongly represses the transcription of MET3, and this regulation occurs through the action of the transcription factors Met4p, Met31p, and Met32p on the weak but tightly controlled MET3 promoter (2, 7, 8, 9, 10). Cells with met3 null mutations are methionine, cysteine, homocysteine, AdoMet, and sulfite auxotrophs and can grow when supplied with these sulfur nutrients but are unable to grow on sulfate (1, 11). ATP sulfurylases are found in many organisms including bacteria, other fungi, and plants (12, 13, 14, 15, 16).

Last updated: 2011-02-07 Contact SGD

References cited on this page View Complete Literature Guide for MET3
1) Masselot M and De Robichon-Szulmajster H  (1975) Methionine biosynthesis in Saccharomyces cerevisiae. I. Genetical analysis of auxotrophic mutants. Mol Gen Genet 139(2):121-32
2) Cherest H, et al.  (1985) Transcriptional regulation of the MET3 gene of Saccharomyces cerevisiae. Gene 34(2-3):269-81
3) Ullrich TC, et al.  (2001) Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation. EMBO J 20(3):316-29
4) Mendoza-Cozatl D, et al.  (2005) Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. FEMS Microbiol Rev 29(4):653-71
5) Cherest H, et al.  (1969) Genetic and regulatory aspects of methionine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 97(1):328-36
6) Lalor DJ, et al.  (2003) Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity. Protein Eng 16(12):1071-9
7) Mountain HA, et al.  (1991) Four major transcriptional responses in the methionine/threonine biosynthetic pathway of Saccharomyces cerevisiae. Yeast 7(8):781-803
8) Blaiseau PL and Thomas D  (1998) Multiple transcriptional activation complexes tether the yeast activator Met4 to DNA. EMBO J 17(21):6327-36
9) Mao X, et al.  (2002) MET3 promoter: a tightly regulated promoter and its application in construction of conditional lethal strain. Curr Microbiol 45(1):37-40
10) Blaiseau PL, et al.  (1997) Met31p and Met32p, two related zinc finger proteins, are involved in transcriptional regulation of yeast sulfur amino acid metabolism. Mol Cell Biol 17(7):3640-8
11) Thomas D and Surdin-Kerjan Y  (1997) Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 61(4):503-32
12) Murillo M and Leustek T  (1995) Adenosine-5'-triphosphate-sulfurylase from Arabidopsis thaliana and Escherichia coli are functionally equivalent but structurally and kinetically divergent: nucleotide sequence of two adenosine-5'-triphosphate-sulfurylase cDNAs from Arabidopsis thaliana and analysis of a recombinant enzyme. Arch Biochem Biophys 323(1):195-204
13) Foster BA, et al.  (1994) Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain. J Biol Chem 269(31):19777-86
14) Simonics T and Maraz A  (2008) Cloning of the ATP sulphurylase gene of Schizosaccharomyces pombe by functional complementation. Can J Microbiol 54(1):71-4
15) Borges-Walmsley MI, et al.  (1995) Isolation and characterisation of genes for sulphate activation and reduction in Aspergillus nidulans: implications for evolution of an allosteric control region by gene duplication. Mol Gen Genet 247(4):423-9
16) Leustek T, et al.  (1994) Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae. Plant Physiol 105(3):897-902