HSP104 chaperone ATPase HSP104 [Saccharomyces cerevisiae S288C] - Gene

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, Dec 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_001144.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
Title: Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.
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.
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.
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.
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.
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.
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.
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.
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.

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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

Orthologs from OrthoDB

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 more info	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