Gene: Dmel\Hsp83
Hsp90, hsp82, l(3)j5C2, E(sev)3A, E(sina)2
Please see the JBrowse view of Dmel\Hsp83 for information on other features
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Gene model reviewed during 5.46
3.05 (northern blot)
83 (kD)
Homodimer (By similarity). Forms a complex with Hop and piwi; probably Hop mediates the interaction between piwi and Hsp83 (PubMed:21186352). Forms a complex including sicily, ND-42 and Hsp83; the complex is necessary to chaperone ND-42 in the cytoplasm before mitochondrial import; the interaction with sicily is direct and is dependent on its ATPase activity (PubMed:23509070). Interacts with shu (PubMed:22902557). Interacts with Nup358 (via TPR repeats); the interaction is required for the nuclear import of the sesquiterpenoid juvenile hormone receptor Met (PubMed:27979731). Forms a complex with Dpit47 and Hsp70aa (PubMed:11493638).
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Hsp83 using the Feature Mapper tool.
Comment: maternally deposited
Comment: anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm anlage
Comment: reported as ventral nerve cord anlage
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as dorsal/lateral sensory complexes
Hsp83 protein colocalizes with cup protein in the cytoplasm of germline stem cells in region 1, is nearly absent in the anterior of region 2 (cystoblast cleavage stage), but rises to high levels in the posterior part of region 2, and in the maturing germline cysts of region 3. Hsp83 protein is distributed in the cytoplasm of both somatic and germline derived cells throughout oogenesis.
GBrowse - Visual display of RNA-Seq signals
View Dmel\Hsp83 in GBrowse 2
3-6
3-6.4
3-13 +/- 4
3-55
3-5
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.
Source for identity of: Hsp83 CG1242
Source for merge of: Hsp83 ms(3)08445
Source for merge of: Hsp83 l(3)j5C2
Source for merge of: Hsp83 anon-WO0140519.209
Source for merge of Hsp83 anon-WO0140519.209 was sequence comparison ( date:051113 ).
Hsp83 is a potent capacitor of behavioral variation.
RNAi screen using dsRNA made from templates generated with primers directed against this gene results in chromosome misalignment on the metaphase spindle and spindles that are aberrantly long when assayed in S2 cells. This phenotype can be observed when the screen is performed with or without Cdc27 dsRNA.
dsRNA made from templates generated with primers directed against this gene results in a change in cell proliferation and cell size.
Expression is enriched in embryonic gonads.
When Hsp83 alleles are combined in transheterozygotes, there are both cumulative and complementary effects on thoracic and variable bristle trait numbers, depending on the allelic combination.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
RNAi screen using dsRNA made from templates generated with primers directed against this gene causes a phenotype when assayed in Kc167 cells: change from round to spindle-shaped, with the formation of F-actin puncta and microtubule extensions. S2R+ cells are unaffected.
Hsp83 may have a role in ensuring proper centrosome function.
The joint action of two RNA degradation pathways (a maternally encoded and a zygotic pathway) controls maternal transcript degradation and its timing in the early embryo. Hsp83 transcripts (relatively high in abundance) require the action of both pathways in order to be eliminated prior to the midblastula transition.
Hsp83 is required for normal spermatogenesis.
Homologous genetic loci in D.subobscura and D.melanogaster tend to show a similar ultrastructure in the two species.
In a sample of 79 genes with multiple introns, 33 showed significant heterogeneity in G+C content among introns of the same gene and significant positive correspondence between the intron and the third codon position G+C content within genes. These results are consistent with selection adding against preferred codons at the start of genes.
Identification: Enhancer trap screen designed to discover genes involved in the cellular aspects of defense mechanisms, as well as in melanotic tumor formation processes linked to blood cell disregulation.
There is significant variation among 74 different 2nd chromosome lines and 70 different 3rd chromosome lines in response to heat shock, measured by mRNA accumulation.
Su(Raf)3A encodes Hsp83 as demonstrated by phenotypic rescue and nucleotide sequence of the mutations.
Wild-type and mutant forms of Hsp83 bind to activated phl but the mutant Hsp83 protein causes a reduction in the kinase activity of phl. Results indicate Hsp83 is essential for phl function in vivo. Location of the E(sev) and Su(Raf) mutations of Hsp83 indicates a weak correlation between the site of mutation and its genetic nature: all but one of the hypomorphs and none of the antimorphs map to the C-terminal domain known to be involved in dimerisation.
Identified in a genetic screen for modifiers of the phl::tor12D.sev rough eye mutant phenotype. Clonal analysis failed to recover any Hsp83 mutant clones suggesting that is required for cell proliferation.
Chromosome homologies of Muller's element D (J chromosome in the Paleartic species and XR chromosome arm in Nearctic species) and of element E (O chromosome in the Paleartic species and 2 chromosome in Nearctic species) have been confirmed by single copy probes in the species of the obscura group and in D.melanogaster.
The in vitro binding of Hsf protein to the promoter region of a number of heat shock genes has been analysed.
Germline clone analysis demonstrates that Hsp83 plays an essential role in germline development.
Synthesis of heat shock proteins is inhibited by both short-chain fatty acids and their corresponding alcohols, compounds which have no observable effect on histone acetylation.
Growth phase defect locus.
Maternal mRNA localises to the pole region of the embryo.
Hsp83 RNA is expressed in a dynamic fashion during oogenesis. Maternally synthesised Hsp83 transcripts are protected from degradation at the posterior pole of the early embryo and is a component of the posterior pole plasm. Zygotic transcription is restricted to the anterior third of the embryo, expression is controlled by bcd.
The product of Hsp83 and its homologs shows a specific nuclear localization in different species of Drosophila and Chironomus. Besides being abundant in the cytoplasm, the Hsp83 product is associated with specific chromosomal loci, such as Hsrω and Dhyd\Hsrω, the telomeric Balbiani rings in Chironomus thummi and the heat-induced puff I-1C in C.tentans.
Nascent chain nuclear run-on assays in KC161 cells reveal different responses to heat shock for different genes. Transcription of His1 is severely inhibited under mild heat shocks, of Act5C decreases proportionally with increasing temperature while that of the core histone genes or the heat shock cognates is repressed only under extreme 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. Hsrω is transcribed at a very high rate under non-heat shock conditions, and its response to elevated temperatures is different from that of the protein coding heat shock genes.
Studies of splicing thermotolerance in Schneider cells with Hsp83 show that Hsp83 transcript is made during heat shock but not processed until the heat shock is over. As little as 10 mins of pretreatment can induce thermotolerance. In the absence of thermotolerant factors, premRNA-containing complexes leave the splicing pathway and exit to the cytoplasm. Induced thermotolerance lasts for approximately 8 hours.
Probes from D.melanogaster were used in chromosome in situ hybridisation to study response to heat shock in D.guanche, D.madeirensis and D.subobscura. Results suggest that the 18C, 94A, 89A and 27A loci of the three obscura group species are homologous to the D.melanogaster loci Hsp83, Hsp70A, Hsp68 and the small Hsp group Hsp22, Hsp23, Hsp26 and Hsp27 respectively.
Hsp83 is required for cell growth and viability.
The subcellular distribution of Hsp83 protein under normal temperature conditions and after heat shock has been determined.
Sequence analysis of the Hsp83 gene in several species reveals a conserved 5' 34 base pair imperfect dyad made up of three overlapping copies of the consensus heat shock regulatory sequence. The heat inducible Hsp83 gene is flanked on both sides by transcription units not induced by heat shock, CG14965 and anon-63BC-T2.
Even though Hsp83 and anon-63BC-T2 are separated by only one thousand base pairs they display strikingly different regulatory properties. anon-63BC-T2 is not heat inducible, whereas Hsp83 is.
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. However, mitochondrial- and histone-gene activities persist (Spradling, Pardue and Penman, 1977). This 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 (Tissieres, Mitchell and Tracy, 1974). Similar response inducible by other stressful treatments. The response may be elicited at all stages of the life cycle and in cultured cells. Stage specific phenocopies result from heat shocking early stages of Drosophila development (Mitchell and Petersen, 1982). In polytene cells existing puffs regress and a novel group quickly appears at 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D (Ashburner, 1970; Tissieres et al., 1974). Activation of transcription of Hsp genes apparently involves the sequential binding of two or more protein factors in vicinity of TATA box (Wu, 1984). Binding sites for these proteins are multiple short upstream sequence elements called HSEs or heat shock consensus elements (Pelham, 1982; Xiao and Lis, 1988). Polymerase II dissociates from most chromosome regions and accumulates at the new puff sites (Bonner and Kerby, 1982). 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. The effects of heat shock may be abrogated to some degree by pretreatment with a pulse of a slightly lower temperature (Mitchell et al., 1979; Peterson and Mitchell, 1981). For reviews of the heat-shock response see Ashburner and Bonner (1978).
The structural gene for the 83,000 dalton heat-shock protein (HSP83). During development, the gene is expressed at high levels in the absence of heat shock in many tissues, especially ovaries where it apparently originates in nurse cells (Zimmerman, Petri, and Meselson, 1983). During heat shock, however, the expression level is only raised several fold (Xiao and Lis, 1989). Deletion of sequences upstream from the coding region eliminates normal developmental expression and results in regulation of Hsp83 in a manner similar to that of Hsp70 which is activated only in response to heat shock.
