HSP26 chaperone protein HSP26 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: HSP26
Official Full Name: chaperone protein HSP26
Primary source: SGD:S000000276
Locus tag: YBR072W
See related: AllianceGenome:SGD:S000000276; FungiDB:YBR072W; VEuPathDB:YBR072W
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 mRNA binding activity and unfolded protein binding activity. Involved in cellular response to heat and protein folding. Located in cytoplasmic stress granule and nucleus. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See HSP26 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (382030..382674)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.
Title: Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.
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.
The results suggested that such a complicated mechanism of dynamic Hsp26p assembly and disassembly, as well as asymmetric segregation may contribute to fine tuning regulation of protein aggregates' refolding, cell fitness and survival.
Title: Asymmetric inheritance of the yeast chaperone Hsp26p and its functional consequences.
the small heat-shock protein Hsp26 is required for the high heat stress tolerance of the fil1 mutant, both in stationary phase cells as well as during active fermentation [Hsp26, strain not listed]
Title: Stress tolerance of the Saccharomyces cerevisiae adenylate cyclase fil1 (CYR1) mutant depends on Hsp26.
Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae.
Title: Functional rescue of mutant human cystathionine beta-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae.
the Hsp26 middle domain is a thermosensor and intrinsic regulator of chaperone activity.
Title: Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain.
Stress response transcription factors Msn2p/4p are repressed by protein kinase A, which alters HSP26 expression.
Title: Protein kinase A regulates constitutive expression of small heat-shock genes in an Msn2/4p-independent and Hsf1p-dependent manner in Saccharomyces cerevisiae.
Hsp26 plays an important role in pathways that defend cells against environmental stress and the types of protein misfolding seen in neurodegenerative disease
Title: A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104.
characterized the influence of Hsp104 and Ssa1 on the disassembly of Hsp26 x substrate complexes in vitro and in vivo
Title: Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.

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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 mRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded 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	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasmic stress granule	HDA more info	PubMed
located_in cytoplasmic stress granule	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: chaperone protein HSP26

NP_009628.1

Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; long-lived protein that is preferentially retained in mother cells and forms cytoplasmic foci; oligomer activation requires heat-induced conformational change; also has mRNA binding activity

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_001134.8 Reference assembly

Range

382030..382674

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178420.1 → NP_009628.1 TPA: chaperone protein HSP26 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009628.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQ71, P15992, Q6B1V5

UniProtKB/TrEMBL

A6ZL16, B3LN77, B5VE37, D3UEG8, G2W977, N1P6J1

Conserved Domains (1) summary

COG0071
Location:72 → 205

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