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    HSP78 chaperone ATPase HSP78 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851845, updated on 18-Sep-2024

    Summary

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    Official Symbol
    HSP78
    Official Full Name
    chaperone ATPase HSP78
    Primary source
    SGD:S000002666
    Locus tag
    YDR258C
    See related
    AllianceGenome:SGD:S000002666; FungiDB:YDR258C; VEuPathDB:YDR258C
    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 ATP hydrolysis activity and misfolded protein binding activity. Involved in several processes, including protein refolding; protein stabilization; and protein unfolding. Located in mitochondrial matrix. Human ortholog(s) of this gene implicated in 3-methylglutaconic aciduria with cataracts, neurologic involvement and neutropenia. Orthologous to human CLPB (caseinolytic mitochondrial matrix peptidase chaperone subunit B). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See HSP78 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (971808..974243, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene catalase A Neighboring gene ribosomal lysine N-methyltransferase Neighboring gene Yap6p Neighboring gene Swm1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Structure and function of Hsp78, the mitochondrial ClpB homolog. Leidhold C, et al. J Struct Biol, 2006 Oct. PMID 16765060
    2. Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein. Krzewska J, et al. J Mol Biol, 2001 Dec 7. PMID 11734006
    3. The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. Schmitt M, et al. J Cell Biol, 1996 Sep. PMID 8830768, Free PMC Article
    4. Hsp60-independent protein folding in the matrix of yeast mitochondria. Rospert S, et al. EMBO J, 1996 Feb 15. PMID 8631298, Free PMC Article
    5. HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Leonhardt SA, et al. Mol Cell Biol, 1993 Oct. PMID 8413229, Free PMC Article

    See all (49) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Elucidation of the interaction proteome of mitochondrial chaperone Hsp78 highlights its role in protein aggregation during heat stress.
      Title: Elucidation of the interaction proteome of mitochondrial chaperone Hsp78 highlights its role in protein aggregation during heat stress.
    2. Hsp78 is indispensable for the resolubilization of protein aggregates generated by heat stress under in vivo conditions.
      Title: The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress.
    Submit: New GeneRIF Correction

    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 ATP hydrolysis activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP hydrolysis activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP hydrolysis activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables misfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular response to heat IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cellular response to heat IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in cellular response to heat IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mitochondrial genome maintenance IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein refolding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein stabilization IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein stabilization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein unfolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein unfolding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in mitochondrial matrix IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrial matrix IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    chaperone ATPase HSP78
    NP_010544.3
    • Oligomeric mitochondrial matrix chaperone; cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; prevents the aggregation of misfolded proteins as well as resolubilize protein aggregates; involved in response to ethanol 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_001136.10 Reference assembly

      Range
      971808..974243 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180566.3 → NP_010544.3  TPA: chaperone ATPase HSP78 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010544.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VSN8, P33416, Q12137
      UniProtKB/TrEMBL
      B3LG32, B5VGE2, C7GTJ3, C8Z5H0, N1P535
      Conserved Domains (1) summary
      TIGR03346
      Location:88 → 794
      chaperone_ClpB; ATP-dependent chaperone ClpB
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P33416.2

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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