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    HSP104 chaperone ATPase HSP104 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850633, updated on 2-Nov-2024

    Summary

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    Official Symbol
    HSP104
    Official Full Name
    chaperone ATPase HSP104
    Primary source
    SGD:S000003949
    Locus tag
    YLL026W
    See related
    AllianceGenome:SGD:S000003949; FungiDB:YLL026W; VEuPathDB:YLL026W
    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 several functions, including ATP hydrolysis activity; adenyl ribonucleotide binding activity; and unfolded protein binding activity. Involved in several processes, including cellular response to heat; protein folding; and protein unfolding. Located in cytoplasm and nuclear periphery. Part of TRC complex. Human ortholog(s) of this gene implicated in 3-methylglutaconic aciduria type 7a; 3-methylglutaconic aciduria type 7b; and severe congenital neutropenia. Orthologous to human CLPB (ClpB family mitochondrial disaggregase). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See HSP104 in Genome Data Viewer
    Location:
    chromosome: XII
    Exon count:
    1
    Sequence:
    Chromosome: XII; NC_001144.5 (88623..91349)

    Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene polyamine transporter TPO1 Neighboring gene Fe-binding Fe/S cluster assembly protein ISA1 Neighboring gene tRNA-Pro Neighboring gene seripauperin PAU17

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001144.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Tessarz P, et al. Mol Microbiol, 2008 Apr. PMID 18312264
    2. Molecular characterization of rice hsp101: complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types. Agarwal M, et al. Plant Mol Biol, 2003 Mar. PMID 12650620
    3. Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation. Yokom AL, et al. Nat Struct Mol Biol, 2016 Sep. PMID 27478928, Free PMC Article
    4. Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Cashikar AG, et al. Mol Cell, 2002 Apr. PMID 11983167
    5. Over-expression of the molecular chaperone Hsp104 in Saccharomyces cerevisiae results in the malpartition of [PSI(+) ] propagons. Ness F, et al. Mol Microbiol, 2017 Apr. PMID 28073182

    See all (401) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The middle domain of Hsp104 can ensure substrates are functional after processing.
      Title: The middle domain of Hsp104 can ensure substrates are functional after processing.
    2. Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
      Title: Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
    3. Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [PSI[+]] Curing by Hsp104 Overexpression.
      Title: Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [PSI(+)] Curing by Hsp104 Overexpression.
    4. Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain.
      Title: Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain.
    5. Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.
      Title: Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation.
    6. A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors.
      Title: A conserved strategy for structure change and energy transduction in Hsp104 and other AAA+ protein motors.
    7. Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
      Title: Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.
    8. Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.
      Title: Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.
    9. Hsp104-dependent ability to assimilate mannitol and sorbitol conferred by a truncated Cyc8 with a C-terminal polyglutamine in Saccharomyces cerevisiae.
      Title: Hsp104-dependent ability to assimilate mannitol and sorbitol conferred by a truncated Cyc8 with a C-terminal polyglutamine in Saccharomyces cerevisiae.
    10. ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.
      Title: ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo.
    Submit: New GeneRIF Correction See all GeneRIFs (80)

    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 ADP binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 protein-folding chaperone binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein-folding chaperone binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular heat acclimation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cellular heat acclimation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cellular response to heat IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in chaperone cofactor-dependent protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in chaperone cofactor-dependent protein refolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding in endoplasmic reticulum IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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 
    involved_in stress granule disassembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in trehalose metabolism in response to heat stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of TRC complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nuclear periphery IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    chaperone ATPase HSP104
    NP_013074.1
    • Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate denatured, protein aggregates; responds to stresses (heat, ethanol, and sodium arsenite); required for the protein aggregate solid-to-liquid phase transition and dispersal of liquid condensates; involved in [PSI+] propagation; potentiated variants eliminate TDP-43 cytoplasmic aggregates to reduce proteotoxicity; becomes more abundant and forms cytoplasmic foci during 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_001144.5 Reference assembly

      Range
      88623..91349
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181846.1 → NP_013074.1  TPA: chaperone ATPase HSP104 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013074.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VXX8, P31539
      UniProtKB/TrEMBL
      A7A0N1, B3LTE4, B5VMS0, C7GQD8, C8ZCU6, N1NZK6
      Conserved Domains (1) summary
      TIGR03346
      Location:7 → 863
      chaperone_ClpB; ATP-dependent chaperone ClpB
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P31539.2

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