Gene model reviewed during 5.46
Dicistronic transcript isoform(s) appear to be relatively rare based on RNA-Seq and/or EST data; may be stage- or tissue-specific.
Gene model reviewed during 5.54
Size determined by in vitro translation.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Hsp22 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Hsp22 in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
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.
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.
Dicistronic annotation CG32041 split out into separate annotations for each open reading frame, CG4456 and CG4460, in release 4.2 of the genome annotation. CG4456 corresponds to Hsp67Bb and CG4460 corresponds to Hsp22.
Increase in RNA levels is observed with aging.
In vivo UV cross-linking and nuclear run-on assays shows that RNA polymerase II density on the Hsp22 gene is rapidly increased by heat shock.
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.
Hsp22 regulatory regions involved in heat shock expression and ecdysterone-induced expression have been identified.
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.
Heat shock induces the accumulation of a dicistronic mRNA which contains both the Hsp22 and Hsp67Bb open reading frames. Overall orientation not stated: Hsp27- Hsp23- Hsp67Ba+ Hsp26+ Hsp22- Hsp67Bb- Hsp67Bc+
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.
Heat-shock inducible in almost all cells at the stages tested.
Activation of transcription of Hsp genes apparently involves the sequential binding of two or more protein factors in vicinity of TATA box.
Polymerase II dissociates from most chromosome regions and accumulates at the new heat shock puff sites upon heat shock.
Hsp22 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.