HSP42 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: HSP42
Primary source: SGD:S000002578
Locus tag: YDR171W
See related: AllianceGenome:SGD:S000002578; FungiDB:YDR171W; VEuPathDB:YDR171W
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 protein sequestering activity. Involved in cytoskeleton organization and positive regulation of cell growth. Located in cytoplasm. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (806621..807748)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins.
Title: Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins.
Hsp42 and Btn2 sequestrases constitute a stress rescue system that is essential for viability upon misfolded protein overload, by mitigating the burden on the Hsp70 chaperone machinery.
Title: Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis.
The Hsp42-stationary phase granule is a common machinery allowing chronologically aged cells to contend with changing environments when available energy is limited.
Title: Misfolding-prone proteins are reversibly sequestered to an Hsp42-associated granule upon chronological aging.
Hsp42 prion-like domain and intrinsically disordered domain are both crucial for cellular fitness during heat stress, demonstrating the need for sequestering misfolded proteins in a regulated manner.
Title: A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.
Hsp42 acts as aggregase to promote protein aggregation and specifically ensures cellular fitness during heat stress. Hsp26 in contrast lacks aggregase function but is superior in facilitating Hsp70/Hsp100-dependent post-stress refolding.
Title: Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.
Cue5 and Hsp42 provide a quality control checkpoint in yeast directed at recycling dysfunctional 26S proteasomes
Title: Autophagic Turnover of Inactive 26S Proteasomes in Yeast Is Directed by the Ubiquitin Receptor Cue5 and the Hsp42 Chaperone.
the Hsp42 chaperone mediates an alternative pathway, the accumulation of these subunits in cytoprotective compartments. Thus, we show that proteasome homeostasis is controlled through probing the level of proteasome assembly
Title: The protein quality control machinery regulates its misassembled proteasome subunits.
Cytosolic deposition of misfolded protein is mediated by the Hsp42 aggregase.
Title: Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition.
Among the identified components of Hos2 "stationary-phase granules" (SPGs), Hsp42 is the first and last member observed in the Hos2 SPG assembly and disassembly processes.
Title: The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells.
The Hsp42 acts via its amino-terminal domain to coaggregate with misfolded proteins and perhaps link such complexes to further sorting factors.
Title: Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae.

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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 protein sequestering activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed

Process	Evidence Code	Pubs
involved_in cytoskeleton organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein complex oligomerization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to heat	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to hydrogen peroxide	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to salt stress	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed

General protein information

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Preferred Names: heat shock protein HSP42

NP_010456.1

Compartment-specific sequestrase chaperone; small heat shock protein (sHSP) with chaperone activity; targets and sequesters proteins to cytoplasmic inclusions (CytoQ); sumoylated during DNA damage; forms barrel-shaped oligomers that suppress unfolded protein aggregation; involved in cytoskeleton reorganization after heat shock; protein abundance increases and forms cytoplasmic foci 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

NC_001136.10 Reference assembly

Range

806621..807748

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180478.1 → NP_010456.1 TPA: heat shock protein HSP42 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010456.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VSF3, Q12329

UniProtKB/TrEMBL

B3LGB2, B5VG66, C7GN26

Conserved Domains (1) summary

COG0071
Location:222 → 356

IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]