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    GSH1 glutamate--cysteine ligase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853344, updated on 28-Oct-2024

    Summary

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    Official Symbol
    GSH1
    Official Full Name
    glutamate--cysteine ligase
    Primary source
    SGD:S000003637
    Locus tag
    YJL101C
    See related
    AllianceGenome:SGD:S000003637; FungiDB:YJL101C; VEuPathDB:YJL101C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables glutamate-cysteine ligase activity. Involved in glutathione biosynthetic process; response to cadmium ion; and response to hydrogen peroxide. Located in cytoplasm. Human ortholog(s) of this gene implicated in cystic fibrosis; glutamate-cysteine ligase deficiency; hemolytic anemia; and myocardial infarction. Orthologous to human GCLC (glutamate-cysteine ligase catalytic subunit). [provided by Alliance of Genome Resources, Oct 2024]
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    Genomic context

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    See GSH1 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (234320..236356, complement)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Mef2p Neighboring gene tRNA-Arg Neighboring gene 1-phosphatidylinositol 4-kinase LSB6 Neighboring gene Chs6p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001142.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Glutathione as an endogenous sulphur source in the yeast Saccharomyces cerevisiae. Elskens MT, et al. J Gen Microbiol, 1991 Mar. PMID 1674526
    2. The essential and ancillary role of glutathione in Saccharomyces cerevisiae analysed using a grande gsh1 disruptant strain. Lee JC, et al. FEMS Yeast Res, 2001 Apr. PMID 12702463
    3. Glutathione is necessary to ensure benefits of calorie restriction during ageing in Saccharomyces cerevisiae. Mannarino SC, et al. Mech Ageing Dev, 2008 Dec. PMID 18840459
    4. Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase. Biterova EI, et al. J Biol Chem, 2009 Nov 20. PMID 19726687, Free PMC Article
    5. Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. Biterova EI, et al. J Biol Chem, 2010 May 7. PMID 20220146, Free PMC Article

    See all (155) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. GSH1 and GSH2 gene mutations affect glutathione synthetase activity in Saccharomyces cerevisiae.
      Title: Effects of GSH1 and GSH2 Gene Mutation on Glutathione Synthetases Activity of Saccharomyces cerevisiae.
    2. crystallographic analysis of Saccharomyces cerevisiae glutamate cysteine ligase
      Title: Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glutamate-cysteine ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutamate-cysteine ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutamate-cysteine ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glutamate-cysteine ligase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in glutathione biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glutathione biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in glutathione biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutathione biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to cadmium ion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in response to hydrogen peroxide IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    glutamate--cysteine ligase
    NP_012434.1
    • Gamma glutamylcysteine synthetase; catalyzes the first step in glutathione (GSH) biosynthesis; expression induced by oxidants, cadmium, and mercury; protein abundance increases in response to DNA replication stress

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001142.9 Reference assembly

      Range
      234320..236356 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181534.1 → NP_012434.1  TPA: glutamate--cysteine ligase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012434.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VW83, P32477
      UniProtKB/TrEMBL
      B3LQ12, C7GR13, C8ZB62, E9P9M0, G2WGR7, N1P8E6
      Conserved Domains (1) summary
      pfam03074
      Location:253 → 645
      GCS; Glutamate-cysteine ligase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32477.1

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