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General Information
Symbol
Dmel\Hsp26
Species
D. melanogaster
Name
Heat shock protein 26
Annotation Symbol
CG4183
Feature Type
FlyBase ID
FBgn0001225
Gene Model Status
Stock Availability
Gene Summary
Heat shock protein 26 (Hsp26) encodes a protein involved in protein folding. It contributes to lifespan determination and the response to cold and heat. [Date last reviewed: 2019-09-12] (FlyBase Gene Snapshot)
Also Known As

Hsp 26, DmHsp26, 26

Key Links
Genomic Location
Cytogenetic map
Sequence location
Recombination map
3-29
RefSeq locus
NT_037436 REGION:9376418..9377427
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Gene Ontology (GO) Annotations (9 terms)
Molecular Function (2 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
inferred from physical interaction with FLYBASE:Myo10A; FB:FBgn0263705
inferred from direct assay
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from sequence model
Biological Process (5 terms)
Terms Based on Experimental Evidence (5 terms)
CV Term
Evidence
References
inferred from direct assay
involved_in cold acclimation
inferred from expression pattern
inferred from mutant phenotype
involved_in protein refolding
inferred from direct assay
involved_in response to heat
inferred from direct assay
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from sequence model
Cellular Component (2 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
located_in cytoplasm
inferred from high throughput direct assay
located_in cytosol
inferred from direct assay
Terms Based on Predictions or Assertions (0 terms)
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the small heat shock protein (HSP20) family. (P02517)
Summaries
Gene Snapshot
Heat shock protein 26 (Hsp26) encodes a protein involved in protein folding. It contributes to lifespan determination and the response to cold and heat. [Date last reviewed: 2019-09-12]
Gene Group (FlyBase)
SMALL HEAT SHOCK PROTEINS -
The small Heat Shock Protein (sHSP) family is characterized by the presence of an α-crystallin domain. sHSPs play a crucial role in protein folding. Most sHSPs have the ability to prevent protein aggregation and to maintain substrate proteins in a refoldable state. (Adapted from FBrf0228040 and FBrf0231212).
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Hsp22 - Hsp-G3
There are seven closely related heat-shock genes at 67B (Ayme and Tissieres, 1985; Pauli, Arrigo, Vasquez, Tonka, and Tissieres, 1989, Genome 31: 671-76). In addition to the four small heat-shock genes previously identified (Hsp22, Hsp23, Hsp26, and Hsp27), three more genes (Hsp-G1, Hsp-G2, and Hsp-G3, formerly called Gene1, Gene2, and Gene3) have been found clustered within 15 kb of DNA at the same 67B cytological location. All seven genes are heat-shock inducible in almost all cells at the stages tested (Ayme and Tissieres, 1985). The genes are also transcribed during certain developmental stages in the absence of heat shock (Sirotkin and Davidson, 1982, Dev. Biol. 89: 196-210). Pauli et al (1989) report that the maximum accumulation of developmental rRNA in a majority of these small heat-shock genes occurs in the white pupae stage; in Hsp-G2, however, a small transcipt is found in embryos, first and second instar larvae, and young pupae; and a larger transcript in the pupal and adult stages of males (Pauli and Tonka, 1987, J. Mol. Biol. 198: 235-40; Pauli, Tonka, and Ayme-Southgate, 1988, J. Mol. Biol. 200: 47-53). In absence of stress, the expression of Hsp26 has been observed in spermatocytes, nurse cells, epithelium, imaginal discs, proventriculus, and neurocytes (Glaser, Wolfner, and Lis, 1986, EMBO 5: 747-54). Transcripts of Hsp26 and Hsp27 accumulate in adult ovaries, apparently originating in nurse cells (Zimmerman, Petri, and Meselson, 1983, Cell 32: 1161-70).
Gene Model and Products
Number of Transcripts
2
Number of Unique Polypeptides
1

Please see the JBrowse view of Dmel\Hsp26 for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model

Gene model reviewed during 5.55

Gene model reviewed during 5.46

Gene model reviewed during 5.56

Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0076496
958
208
FBtr0346539
1010
208
Additional Transcript Data and Comments
Reported size (kB)

1.1 (northern blot)

1.05 (northern blot)

Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0076224
23.0
208
7.64
FBpp0312157
23.0
208
7.64
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

208 aa isoforms: Hsp26-PA, Hsp26-PB
Additional Polypeptide Data and Comments
Reported size (kDa)

208 (aa); 22.997 (kD predicted)

26.618 (kD predicted)

26 (kD observed)

Comments
External Data
Crossreferences
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Hsp26 using the Feature Mapper tool.

External Data
Crossreferences
Linkouts
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
organism

Comment: maternally deposited

northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

Hsp26 transcript is detected in early embryos, and disappears by 2-3 hrs of development. Maximal expression is in white prepupae.

Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Marker for
 
Subcellular Localization
CV Term
Evidence
References
located_in cytoplasm
inferred from high throughput direct assay
located_in cytosol
inferred from direct assay
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\Hsp26 in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 4-6
  • Stages(s) 9-10
  • Stages(s) 11-12
  • Stages(s) 13-16
Alleles, Insertions, Transgenic Constructs, and Aberrations
Classical and Insertion Alleles ( 8 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 12 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of Hsp26
Transgenic constructs containing regulatory region of Hsp26
Aberrations (Deficiencies and Duplications) ( 4 )
Alleles Representing Disease-Implicated Variants
Phenotypes
Orthologs
Human Orthologs (via DIOPT v8.0)
Homo sapiens (Human) (11)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
6 of 15
Yes
No
6 of 15
Yes
No
6  
5 of 15
No
Yes
2  
5 of 15
No
Yes
Hsap\CRYAA2
4 of 15
No
No
3 of 15
No
Yes
3 of 15
No
No
3 of 15
No
Yes
4  
2 of 15
No
Yes
2 of 15
No
Yes
1  
2 of 15
No
Yes
Model Organism Orthologs (via DIOPT v8.0)
Mus musculus (laboratory mouse) (9)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
7 of 15
Yes
No
6 of 15
No
No
5 of 15
No
Yes
4 of 15
No
Yes
4 of 15
No
No
3 of 15
No
Yes
2 of 15
No
Yes
2 of 15
No
No
2 of 15
No
No
Rattus norvegicus (Norway rat) (9)
6 of 13
Yes
No
5 of 13
No
No
5 of 13
No
Yes
4 of 13
No
Yes
4 of 13
No
No
3 of 13
No
Yes
3 of 13
No
Yes
2 of 13
No
Yes
2 of 13
No
Yes
Xenopus tropicalis (Western clawed frog) (14)
5 of 12
Yes
No
5 of 12
Yes
No
5 of 12
Yes
No
4 of 12
No
Yes
4 of 12
No
No
4 of 12
No
Yes
4 of 12
No
No
3 of 12
No
Yes
3 of 12
No
Yes
2 of 12
No
Yes
2 of 12
No
Yes
2 of 12
No
Yes
2 of 12
No
No
1 of 12
No
Yes
Danio rerio (Zebrafish) (13)
6 of 15
Yes
No
6 of 15
Yes
No
6 of 15
Yes
Yes
5 of 15
No
No
5 of 15
No
Yes
5 of 15
No
Yes
4 of 15
No
No
4 of 15
No
Yes
4 of 15
No
Yes
4 of 15
No
Yes
3 of 15
No
Yes
3 of 15
No
Yes
2 of 15
No
Yes
Caenorhabditis elegans (Nematode, roundworm) (19)
8 of 15
Yes
No
8 of 15
Yes
No
7 of 15
No
No
7 of 15
No
Yes
6 of 15
No
No
6 of 15
No
No
6 of 15
No
No
5 of 15
No
No
5 of 15
No
Yes
5 of 15
No
Yes
5 of 15
No
No
5 of 15
No
No
5 of 15
No
No
4 of 15
No
No
4 of 15
No
Yes
4 of 15
No
No
4 of 15
No
Yes
3 of 15
No
No
1 of 15
No
Yes
Arabidopsis thaliana (thale-cress) (17)
4 of 9
Yes
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
2 of 9
No
Yes
1 of 9
No
Yes
1 of 9
No
Yes
Saccharomyces cerevisiae (Brewer's yeast) (1)
1 of 15
Yes
No
Schizosaccharomyces pombe (Fission yeast) (2)
2 of 12
Yes
No
1 of 12
No
No
Ortholog(s) in Drosophila Species (via OrthoDB v9.1) ( EOG09190FXG )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila virilis
Drosophila mojavensis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG09150CM2 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Lucilia cuprina
Australian sheep blowfly
Mayetiola destructor
Hessian fly
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W0F0S )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Cimex lectularius
Bed bug
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X0HK6 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G0USC )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Ciona intestinalis
Vase tunicate
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v8.0)
Drosophila melanogaster (Fruit fly) (10)
8 of 10
7 of 10
7 of 10
7 of 10
6 of 10
5 of 10
5 of 10
5 of 10
5 of 10
4 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
Disease Model Summary Ribbon
Disease Ontology (DO) Annotations
Models Based on Experimental Evidence ( 0 )
Allele
Disease
Evidence
References
Potential Models Based on Orthology ( 10 )
Modifiers Based on Experimental Evidence ( 1 )
Allele
Disease
Interaction
References
Disease Associations of Human Orthologs (via DIOPT v8.0 and OMIM)
Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
Functional Complementation Data
Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
Interactions
Summary of Physical Interactions
esyN Network Diagram
Show neighbor-neighbor interactions:
Select Layout:
Legend:
Protein
RNA
Selected Interactor(s)
Interactions Browser

Please see the Physical Interaction reports below for full details
protein-protein
Physical Interaction
Assay
References
Summary of Genetic Interactions
esyN Network Diagram
esyN Network Key:
Suppression
Enhancement

Please look at the allele data for full details of the genetic interactions
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
External Data
Linkouts
BioGRID - A database of protein and genetic interactions.
DroID - A comprehensive database of gene and protein interactions.
MIST (protein-protein) - An integrated Molecular Interaction Database
Pathways
Signaling Pathways (FlyBase)
Metabolic Pathways
FlyMet - A comprehensive tissue-specific metabolomics resource for Drosophila.
External Data
Linkouts
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Genomic Location and Detailed Mapping Data
Chromosome (arm)
3L
Recombination map
3-29
Cytogenetic map
Sequence location
FlyBase Computed Cytological Location
Cytogenetic map
Evidence for location
67B2-67B2
Limits computationally determined from genome sequence between P{PZ}l(3)0162901629&P{PZ}mRpL1210534 and P{EP}Hsp26EP3336&P{EP}Hsp26EP3315
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
67B-67B
(determined by in situ hybridisation)
A probe containing both Hsp22 and Hsp26 hybridises to cytological locations 67B1--67B2 and 67B4--67B5.
Experimentally Determined Recombination Data
Location
Left of (cM)
Right of (cM)
Notes
Stocks and Reagents
Stocks (44)
Genomic Clones (17)
 

Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete

cDNA Clones (124)
 

Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

cDNA clones, fully sequenced
BDGP DGC clones
Other clones
Drosophila Genomics Resource Center cDNA clones

For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

cDNA Clones, End Sequenced (ESTs)
Other clones
RNAi and Array Information
Linkouts
DRSC - Results frm RNAi screens
GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
Antibody Information
Laboratory Generated Antibodies
Commercially Available Antibodies
 
Other Information
Relationship to Other Genes
Source for database identify of
Source for database merge of
Additional comments
Other Comments

Expression is enriched in embryonic gonads.

Shows particularly robust cycling of transcription in adult heads, as assessed by expression analysis using high density oligonucleotide arrays with probe generated during three 12-point time course experiments over the course of 6 days.

Co-immunoprecipitation with an antibody raised against lwr confirms interaction with Hsp23 and Hsp26 and preferentially with Hsp27.

Using Hsp26 as a model it is demonstrated that histone acetylation significantly affects the ability of RNA pol II to initiate transcription on a chromatin template by facilitating the access of key regulators to the promoter in chromatin. This finding establishes a causal relationship between histone acetylation and transcription by RNA pol II.

d(GA.TC)n sequences can be found in the promoters of Hsp26 and the Hsp70 genes. In vitro assembly of mononucleosomes into short DNA fragments carrying d(GA.TC)n sequences of different lengths is very efficient. Nucleosome assembly is inhibited strongly when the d(GA.TC)n sequence forms a triple-stranded conformation. Triplex formation requires partial destabilisation of the nucleosome. Results indicate nucleosome assembly and triplex formation are competing processes.

DNA elimination as a mechanism for the loss of gene expression associated with PEV is studied using insertions of an Hsp26 construct. No significant DNA elimination is observed in diploid tissue. Heterochromatic transgenes are underrepresented in polytene tissue. Data suggests DNA loss does not correlate with the reduction in gene expression associated with PEV at pericentric and fourth chromosome sites.

The nucleosome region is not essential for heat shock induction of transcription.

UV cross linking technique has been used to study the in vivo distribution of Trl protein on Hsp70 and Hsp26. Prior to heat shock Trl protein is associated with the promoter regions of the uninduced Hsp70 and Hsp26 genes. Upon heat shock induction Trl protein is recruited to their transcription units with its distribution coincident with that of RNA polymerase II.

Analysis of transcription from Hsp26 promoter deletion constructs indicates that Trl mediates anti-repression of the Hsp26 promoter in extracts from unstressed embryos, while Hsf activates the Hsp26 promoter in extracts from heat shocked embryos.

Assembly of chromatin on the Hsp26 promoter in embryonic extracts has been used to determine the contribution of transcription factors to promoter architecture in chromatin. Analysis of nucleosome rearrangements by transcription factors indicates the nucleosomes are not disrupted. The basis for the observed chromatin rearrangements is energy driven nucleosome sliding. Hsf and Trl can cause nucleosome rearrangements which may lead to a refinement of nucleosome positions, nucleosome remodeling is ATP-dependent.

Hsp26 RNA levels do not increase with age.

The wild-type Hsp26 TATA box is essential for correct binding of TFIID and for inducible expression, but not for the formation of DNase I-hypersensitive sites.

Gene contains an RNA polymerase II complex which pauses after synthesis of a short transcript. In vivo ultraviolet crosslinking techniques demonstrate phosphorylation of the carboxy terminal domain (CTD) of the large subunit of RNA polymerase II could either regulate the transition of polymerase from a paused to an elongated complex or be a consequence of the transition from paused to elongated.

The TFIID complex interacts with the promoter of Hsp26 making contacts at the TATA element, initiator, +18 and +28 regions.

Chromosome staining reveals that Trl and heat shock transcription factors (HSF) colocalises at Hsp26.

Distal (CT)n sequence contributes to the levels of heat shock inducibility of Hsp26 and contributes significantly to the formation of the DNase I hypersensitive (DH) sites. The (CT)n sequences are bound by Trl. Deletion of the HSEs severely reduced heat shock inducibility but only has a minor effect n the formation of DH sites.

In vivo UV cross-linking and nuclear run-on assays shows that RNA polymerase II density on the Hsp26 gene is rapidly increased by heat shock.

TATA complex formation on the Hsp70Bb core promoter shows sequence dependence at the TATA element, at the transcription start site and further downstream. Similar interactions contribute to TATA complexes formed on the Hsp26 and His4 promoters.

In unshocked cells Hsp83 is moderately transcribed while transcription from the other heat shock genes is undetectable. Engaged but paused RNA molecules are found at the various Hsp70 and Hsp26 genes but not at the other heat shock genes. Increased transcription of the heat shock genes is observed within 1-2 mins of heat shock and maximal rates were reached within 2-5 minutes. Rates of transcription vary over a 20-fold range.

Exposure of cells to pulses of elevated temperature initiates the heat-shock response. A restricted subset of genes, the Hsp genes, is activated and the majority of transcription and translation is shut down. 3H-uridine incorporation ceases at its usual positions and commences at new puff sites. Preexisting polysomes disaggregate and within a few minutes a new population of polysomes appears containing newly transcribed mRNA; this RNA hybridizes to some of the heat-shock puffs. Similar response inducible by other stressful treatments. The response may be elicited at all stages of the life cycle and in cultured cells.

Translation of Hsp70 mRNAs and to a lesser extent the mRNAs for the small heat shock proteins is almost independent of eIF-4E.

Mutations at br reduce the transcription rate or stability of the small heat shock protein mRNAs.

Three regions of 5' DNA contribute to Hsp26 heat induced transcription, HSEs 1, 2 and 6 and the CT.GA region. The homopurine/homopyrimidine sequences in the promoter forms H-DNA in vitro.

The binding sites for the protein factors required for activation of transcription of Hsp genes are multiple short upstream sequence elements called HSEs or heat shock consensus elements.

In absence of stress, the expression of Hsp26 has been observed in spermatocytes, nurse cells, epithelium, imaginal discs, proventriculus, and neurocytes.

Heat-shock inducible in almost all cells at the stages tested.

Studies demonstrate that heat shock puffs at the site of a construct insertion can be formed if the inserted segment contains a functional heat shock promoter and the active promoter is joined to long transcription units.

Activation of transcription of Hsp genes apparently involves the sequential binding of two or more protein factors in vicinity of TATA box.

Transcripts of Hsp26 and Hsp27 accumulate in adult ovaries, apparently originating in nurse cells.

Polymerase II dissociates from most chromosome regions and accumulates at the new heat shock puff sites upon heat shock.

Hsp26 is transcribed during certain developmental stages in the absence of heat shock.

The effects of heat shock may be abrogated to some degree by pretreatment with a pulse of a slightly lower temperature.

Mitochondrial and histone-gene activities persist transcription and translation.

In polytene cells, during heat shock response, existing puffs regress and a novel group quickly appear at 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D.

The heat shock response follows a pulse of 36oC to 40oC; treatments above 40oC inhibit all activity and lead to death; treatments of 30oC-35oC induce heat-shock-protein synthesis without repressing normal protein synthesis.

In polytene cells, during heat shock response, existing puffs regress and a novel group quickly appear at cytological locations 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D.

Origin and Etymology
Discoverer
Etymology
Identification
External Crossreferences and Linkouts ( 52 )
Sequence Crossreferences
NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
Other crossreferences
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
FlyMet - A comprehensive tissue-specific metabolomics resource for Drosophila.
GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
KEGG Genes - Molecular building blocks of life in the genomic space.
MARRVEL_MODEL - MARRVEL (model organism gene)
modMine - A data warehouse for the modENCODE project
Linkouts
BioGRID - A database of protein and genetic interactions.
DroID - A comprehensive database of gene and protein interactions.
DRSC - Results frm RNAi screens
FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
FlyMine - An integrated database for Drosophila genomics
MIST (protein-protein) - An integrated Molecular Interaction Database
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Synonyms and Secondary IDs (15)
Reported As
Symbol Synonym
Dmel23.0
Hsp26
(Ahmed-Braimah et al., 2021, Cattenoz et al., 2021, Lindsey et al., 2021, McDonough-Goldstein et al., 2021, Baral et al., 2020, Cho et al., 2020, Seong et al., 2020, Engel et al., 2019, Greenblatt et al., 2019, Maitra et al., 2019, Michalak et al., 2019, Rivera et al., 2019, Sørensen et al., 2019, Tsakiri et al., 2019, Hall et al., 2018, Hemphill et al., 2018, Jagla et al., 2018, Kennerdell et al., 2018, Leow et al., 2018, Franz et al., 2017, Hu et al., 2017.6.13, Lei et al., 2017, Yang and Veraksa, 2017, Donovan and Marr, 2016, Fabre et al., 2016, Hu et al., 2016, Maistrenko et al., 2016, Sarov et al., 2016, Zhang et al., 2016, Chen et al., 2015, Grotewiel and Bettinger, 2015, Štětina et al., 2015, Van Bortle et al., 2015, Xie et al., 2015, Belozerov et al., 2014, Benbahouche et al., 2014, Gan et al., 2014, Lee et al., 2014, Marr et al., 2014, Radermacher et al., 2014, Taylor et al., 2014, Toshima et al., 2014, Kwon et al., 2013, Rallis et al., 2013, Schertel et al., 2013, Stefanatos et al., 2013, Telonis-Scott et al., 2013, Yoshigi et al., 2013, Eleftherianos and Castillo, 2012, Fredriksson et al., 2012, Guertin et al., 2012, Japanese National Institute of Genetics, 2012.5.21, Paré et al., 2012, Stern et al., 2012, Chan et al., 2011, Franco et al., 2011, Friedman et al., 2011, Gonsalves et al., 2011, Ren et al., 2011, Salamanca et al., 2011, Wang et al., 2011, Blanco et al., 2010, Chen et al., 2010, Colinet et al., 2010, Kallappagoudar et al., 2010, Kong et al., 2010, Kwon et al., 2010, Mosqueira et al., 2010, Müller et al., 2010, Sun et al., 2010, Tian et al., 2010, Takemori and Yamamoto, 2009, Bettencourt et al., 2008, Blanco et al., 2008, Brandt and Corces, 2008, Duncan, 2008, Gilchrist et al., 2008, Mileva-Seitz et al., 2008, Petesch and Lis, 2008, Puri et al., 2008, Sudi et al., 2008, Curtis et al., 2007, Laayouni et al., 2007, Muse et al., 2007, Muse et al., 2007, Stuart et al., 2007, Baird et al., 2006, Neal et al., 2006, Shigenobu et al., 2006, Walser et al., 2006, Birch-Machin et al., 2005, Duncan, 2005, Kim and Lis, 2005, Qin et al., 2005, Geiger-Thornsberry and Mackay, 2004, Rehwinkel et al., 2004)
hsp26
(Hagen et al., 2021, Kwon et al., 2020, Zarubin et al., 2020, Sharma et al., 2018, Kwon et al., 2016, Jevtov et al., 2015, Pandey et al., 2014, Awofala et al., 2012, Chakrabarti et al., 2012, Sharma et al., 2012, Ardehali et al., 2011, Ghosh et al., 2011, He et al., 2011, Rose and Burke, 2011, Sala et al., 2011, Tower, 2011, Dialynas et al., 2010, Frydenberg et al., 2010, Melnikova et al., 2010, Moshkovich and Lei, 2010, Singh et al., 2010, Hines et al., 2009, Singh et al., 2009, Chopra et al., 2008, Kuhn-Parnell et al., 2008, Liao et al., 2008, Nisha and Csink, 2007, Haynes et al., 2006, Kahn et al., 2006, Schwartz et al., 2005, van der Knaap et al., 2005, Yagi and Ip, 2005, Gracheva et al., 2004, Kurapati et al., 2004, Lehmann, 2004, Loeschcke et al., 2004, Ni et al., 2004, Wang et al., 2004, Boehm et al., 2003, Kapetanaki et al., 2003, Lu et al., 2003, Schwartz et al., 2003, Aigaki et al., 2002, Andrulis et al., 2002, Badenhorst et al., 2002, Leibovitch et al., 2002, Leibovitch et al., 2002, Li et al., 2002, Wang and Benzer, 2002, Leibovitch et al., 2001, Seong et al., 2001, Sun et al., 2001, Akhtar and Becker, 2000, Akhtar et al., 2000, Farkas et al., 2000, Kurapati et al., 2000, Leach et al., 2000, Leibovitch et al., 2000, Sun and Elgin, 2000, Sun et al., 2000, Wallrath, 2000, Agianian et al., 1999, Cryderman et al., 1999, Cryderman et al., 1999, Elgin et al., 1999, King and Tower, 1999, Langst et al., 1999, Sun et al., 1999, Elgin et al., 1998, Farkas et al., 1998, Gregory and Horz, 1998, Lis, 1998, Sandaltzopoulos and Becker, 1998, Singh and Huskisson, 1998, Sun et al., 1998, Wallrath, 1998, Wallrath et al., 1998, Elgin et al., 1997, Elgin et al., 1997, Otsuka et al., 1997, Strutt et al., 1997, Wilkins and Lis, 1997, Shopland and Lis, 1996, Svaren and Hoerz, 1996, Fernandes et al., 1995, Granok et al., 1995, Heino et al., 1995, Rasmussen and Lis, 1995, Weiler and Wakimoto, 1995, Wheeler et al., 1995, Becker, 1994, Champlin and Lis, 1994, Elgin et al., 1994, Granok et al., 1994, Heino and Lahti, 1994, Lu et al., 1994, O'Brien et al., 1994, Segalat et al., 1994, Southgate, 1994.2.17, Ayme-Southgate, 1993.2.23, Giardina, 1993.4.1, Giardina and Lis, 1993, Heikkila, 1993, Lu et al., 1993, Marin et al., 1993, Molto et al., 1993, O'Brien and Lis, 1993, Parsell and Lindquist, 1993, Soeller et al., 1993, Svaren and Horz, 1993, Vazquez et al., 1993, Andres and Thummel, 1992, Berger et al., 1992, Lu et al., 1992, Pauli et al., 1992, Read and Manley, 1992, Dobens et al., 1991, Elgin and Lu, 1991, Vazquez, 1991, Zapata et al., 1991, Dietz et al., 1990, Elgin, 1990, Glaser and Lis, 1990, Haass et al., 1990, Lu et al., 1990, Ornelles and Penman, 1990, Spencer and Groudine, 1990, Thummel, 1990, Yost et al., 1990, Pauli et al., 1989, Pauli et al., 1988, Pauli and Tonka, 1987, Ayme-Southgate and Tissieres, 1985, Southgate et al., 1983, Ingolia and Craig, 1981)
small hsp locus 67B
Secondary FlyBase IDs
  • FBgn0010231
Datasets (0)
Study focus (0)
Experimental Role
Project
Project Type
Title
References (412)