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HSP26 chaperone protein HSP26 [ Saccharomyces cerevisiae S288C ]

Gene ID: 852364, updated on 2-Nov-2024

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_001134.8Genomic Context describing neighboring genes Neighboring gene N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase anchoring subunit ALG14 Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene DNA-dependent ATPase RDH54

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. The effects of 5'-capping, 3'-polyadenylation and leader composition upon the translation and stability of mRNA in a cell-free extract derived from the yeast Saccharomyces cerevisiae. Gerstel B, et al. Mol Microbiol, 1992 Aug. PMID 1406273
  2. Purification and characterization of the chaperone-like Hsp26 from Saccharomyces cerevisiae. Ferreira RM, et al. Protein Expr Purif, 2006 Jun. PMID 16603379
  3. Matrix-assisted refolding of oligomeric small heat-shock protein Hsp26. Franzmann TM. Int J Biol Macromol, 2006 Aug 15. PMID 16626802
  4. Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. White HE, et al. Structure, 2006 Jul. PMID 16843901
  5. Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain. Franzmann TM, et al. Mol Cell, 2008 Feb 1. PMID 18243115

See all (152) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
  9. 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

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 PubMed 
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasmic stress granule HDA PubMed 
located_in cytoplasmic stress granule IDA
Inferred from Direct Assay
more info
 PubMed 
located_in mitochondrion HDA 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

  1. NC_001134.8 Reference assembly

    Range
    382030..382674
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. 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]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P15992.3

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