The 93D heat shock locus of Drosophila melanogaster: modulation by genetic and developmental factors

Genome ◽  
1989 ◽  
Vol 31 (2) ◽  
pp. 677-683 ◽  
Author(s):  
S. C. Lakhotia
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Developmental Regulation ◽  
Sequence Divergence ◽  
Unique Region ◽  
Reading Frame ◽  
Beta Alanine ◽  
Functional Conservation ◽  
Duplicate Loci ◽  
93D Locus

The 93D locus in Drosophila melanogaster and the 93D-like loci in other species of Drosophila, collectively termed hsr ω (heat shock RNA omega) locus, display several unique and intriguing features: (i) developmental regulation and selective induction by several agents like benzamide, colchicine, thiamphenicol, vit-B6; (ii) functional conservation in the genus but a very rapid DNA base sequence divergence; (iii) in spite of the rapid DNA sequence divergence, a strong conservation of organization (a 5′ unique region and a 3′ long tandem repeat region) and the pattern of multiple ω transcripts in the genus; (iv) a general nontranslatability of all the three major species of ω transcripts (an ~ 10-kb ω1, a 2.0-kb ω2, and a 1.2-kb ω3 species) although some recent evidence favours translatability of a small open reading frame (~ 23 – 27 amino acid long) in the ω3 transcript; (v) dispensability of the hsr ω locus for heat shock protein synthesis but indispensability for viability of flies. The heat shock inducibility of the 93D locus of D. melanogaster is selectively repressed by (i) combination of heat shock with another inducer of 93D; (ii) rearing of larvae at 10 °C; (iii) heterozygous deficiency for the 93D region; and (iv) conditions that alter levels of beta-alanine. In all cases of repression of the 93D locus during heat shock, the 87A and 87C loci (the two duplicate loci harbouring multiple copies for hsp70 and the alpha–beta repeat sequences (at 87C)) develop unequal puffs. The hsr ω locus appears to be under a complex system of regulation involving autoregulation as well as regulation by other factors in the cell which possibly operate through different control elements on the locus.Key words: benzamide, colchicine, beta-alanine, hsr ω, heat shock puffs, Drosophila.

scholarly journals Conservation of gene architecture and domains amidst sequence divergence in thehsrωlncRNA gene across theDrosophilagenus: Anin silicoanalysis

2019 ◽  
Author(s):  
Ranjan Kumar Sahu ◽  
Eshita Mutt ◽  
Subhash Chandra Lakhotia
Keyword(s):  
Drosophila Melanogaster ◽  
Tandem Repeat ◽  
Tandem Repeats ◽  
Sequence Divergence ◽  
Splice Junction ◽  
Proximal Part ◽  
Order Structure ◽  
Repeat Region ◽  
Functional Conservation ◽  
Splice Junctions

AbstractThe developmentally active and cell-stress responsivehsrω locus inDrosophila melanogastercarries two exons, oneomegaintron, one short translatable open reading frame ORFω, long stretch of unique tandem repeats and an overlappingmir-4951near its 3’ end. It produces multiple lncRNAs using two transcription start and four termination sites. Earlier studies revealed functional conservation in severalDrosophilaspecies but with little sequence conservation, in three experimentally examined species, of ORFω, tandem repeat and other regions but ultra-conservation of 16nt at 5’ and 60nt at 3’ splice-junctions of theomegaintron. Present bioinformatic study, using the splice-junction landmarks inDrosophila melanogaster hsrω, identified orthologues in publicly available 34Drosophilaspecies genomes. Each orthologue carries the short ORFω, ultra-conserved splice junctions ofomegaintron, repeat region, conserved 3’-end locatedmir-4951, and syntenic neighbours. Multiple copies of conserved nonamer motifs are seen in the tandem repeat region, despite a high variability in repeat sequences. Intriguingly, only the intron sequences in different species show evolutionary relationships matching the general phylogenetic history in the genus. Search in other known insect genomes did not reveal sequence homology although a locus with similar functional properties is suggested inChironomusandCeratitisspecies. Amidst the high sequence divergence, the conserved organization of exons, ORFω andomegaintron in this gene’s proximal part and tandem repeats in distal part across theDrosophilagenus is remarkable and possibly reflects functional importance of higher order structure ofhsrω lncRNAs and the small Omega peptide.

scholarly journals Heat shock and ecdysterone activation of the Drosophila melanogaster hsp23 gene; a sequence element implied in developmental regulation.

1986 ◽  
Vol 5 (7) ◽  
pp. 1667-1673 ◽  
Author(s):  
R. Mestril ◽  
P. Schiller ◽  
J. Amin ◽  
H. Klapper ◽  
J. Ananthan ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Developmental Regulation ◽  
Sequence Element

Correct temperature induction and developmental regulation of a cloned heat shock gene transformed into the Drosophila germ line

1984 ◽  
Vol 4 (12) ◽  
pp. 2883-2889
Author(s):  
E P Hoffman ◽  
V G Corces
Keyword(s):  
Heat Shock ◽  
Germ Line ◽  
Developmental Regulation ◽  
Heat Shock Gene ◽  
Coding Region ◽  
Chromosomal Locus ◽  
Base Pairs ◽  
Protein Coding ◽  
Reading Frame ◽  
Altered Gene

We have constructed a size variant of the Drosophila hsp28 gene by deleting 207 base pairs of the protein coding region, beginning 33 base pairs downstream of the ATG protein initiation codon. After transformation of Drosophila melanogaster rosy (ry506) flies with this altered gene, using the P transposable element system, it was found that the transformed gene was regulated correctly both after temperature elevation and during the development of the flies. Levels of the variant mRNA were as high as those of the endogenous hsp28 during all patterns of expression, and the variant mRNA appeared in all cases to be processed correctly and to be as stable as the endogenous mRNA. Nevertheless, the chromosomal locus of the transformed gene did not puff after heat shock, suggesting that normal transcription of the gene does not require puffing of the locus. The deleted hsp28 gene retained the reading frame of the endogenous one, and a protein of the expected molecular weight of 18,500 was made after heat shock at levels comparable to those of the endogenous hsp28.

scholarly journals Correct temperature induction and developmental regulation of a cloned heat shock gene transformed into the Drosophila germ line.

1984 ◽  
Vol 4 (12) ◽  
pp. 2883-2889 ◽  
Author(s):  
E P Hoffman ◽  
V G Corces
Keyword(s):  
Heat Shock ◽  
Germ Line ◽  
Developmental Regulation ◽  
Heat Shock Gene ◽  
Coding Region ◽  
Chromosomal Locus ◽  
Base Pairs ◽  
Protein Coding ◽  
Reading Frame ◽  
Altered Gene

We have constructed a size variant of the Drosophila hsp28 gene by deleting 207 base pairs of the protein coding region, beginning 33 base pairs downstream of the ATG protein initiation codon. After transformation of Drosophila melanogaster rosy (ry506) flies with this altered gene, using the P transposable element system, it was found that the transformed gene was regulated correctly both after temperature elevation and during the development of the flies. Levels of the variant mRNA were as high as those of the endogenous hsp28 during all patterns of expression, and the variant mRNA appeared in all cases to be processed correctly and to be as stable as the endogenous mRNA. Nevertheless, the chromosomal locus of the transformed gene did not puff after heat shock, suggesting that normal transcription of the gene does not require puffing of the locus. The deleted hsp28 gene retained the reading frame of the endogenous one, and a protein of the expected molecular weight of 18,500 was made after heat shock at levels comparable to those of the endogenous hsp28.

scholarly journals MUTATIONAL ANALYSIS OF THE REGION SURROUNDING THE 93D HEAT SHOCK LOCUS OF DROSOPHILA MELANOGASTER

Genetics ◽  
1984 ◽  
Vol 106 (2) ◽  
pp. 249-265
Author(s):  
Jym Mohler ◽  
Mary Lou Pardue
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Mutational Analysis ◽  
Point Mutations ◽  
Γ Irradiation ◽  
Lethal Mutations ◽  
Complementation Groups ◽  
In Trans ◽  
Shock Locus ◽  
Shock Proteins

ABSTRACT The region containing subdivisions 93C, 93D and 93E on chromosome 3 of Drosophila melanogaster has been screened for visible and lethal mutations. Treatment with three mutagens, γ irradiation, ethyl methanesulfonate and diepoxybutane, has produced mutations that fall into 20 complementation groups, including the previously identified ebony locus. No point mutations affecting the heat shock locus in 93D were detected; however, a pair of deficiencies that overlap in the region of this locus was isolated. Flies heterozygous in trans for this pair of deficiencies are capable of producing all of the major heat shock puffs (except 93D) and the major heat shock proteins. In addition, these flies show recovery of normal protein synthesis following a heat shock.

scholarly journals Perturbation of chromatin architecture on ecdysterone induction of Drosophila melanogaster small heat shock protein genes.

1989 ◽  
Vol 9 (1) ◽  
pp. 332-335 ◽  
Author(s):  
S E Kelly ◽  
I L Cartwright
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Intergenic Region ◽  
Small Heat Shock Protein ◽  
Dnase I ◽  
Developmentally Regulated ◽  
Regulatory Interactions ◽  
Chromatin Architecture ◽  
Heat Shock Protein Genes

Alterations in the pattern of DNase I hypersensitivity were observed on ecdysterone-stimulated transcription of Drosophila melanogaster small heat shock protein genes. Perturbations were induced near hsp27 and hsp22, coupled with an extensive domain of chromatin unfolding in the intergenic region between hsp23 and the developmentally regulated gene 1. These regions represent candidates for ecdysterone regulatory interactions.

scholarly journals Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein.

1989 ◽  
Vol 9 (6) ◽  
pp. 2615-2626 ◽  
Author(s):  
E Hickey ◽  
S E Brandon ◽  
G Smale ◽  
D Lloyd ◽  
L A Weber
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Normal Growth ◽  
Gene Families ◽  
Growth Conditions ◽  
Complete Sequence ◽  
Start Codon ◽  
Hybridization Probe ◽  
Reading Frame ◽  
Alpha Gene

Vertebrate cells synthesize two forms of the 82- to 90-kilodalton heat shock protein that are encoded by distinct gene families. In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. Only the larger form, hsp89 alpha, is induced by the adenovirus E1A gene product (M. C. Simon, K. Kitchener, H. T. Kao, E. Hickey, L. Weber, R. Voellmy, N. Heintz, and J. R. Nevins, Mol. Cell. Biol. 7:2884-2890, 1987). We have isolated a human hsp89 alpha gene that shows complete sequence identity with heat- and E1A-inducible cDNA used as a hybridization probe. The 5'-flanking region contained overlapping and inverted consensus heat shock control elements that can confer heat-inducible expression on a beta-globin reporter gene. The gene contained 10 intervening sequences. The first intron was located adjacent to the translation start codon, an arrangement also found in the Drosophila hsp82 gene. The spliced mRNA sequence contained a single open reading frame encoding an 84,564-dalton polypeptide showing high homology with the hsp82 to hsp90 proteins of other organisms. The deduced hsp89 alpha protein sequence differed from the human hsp89 beta sequence reported elsewhere (N. F. Rebbe, J. Ware, R. M. Bertina, P. Modrich, and D. W. Stafford (Gene 53:235-245, 1987) in at least 99 out of the 732 amino acids. Transcription of the hsp89 alpha gene was induced by serum during normal cell growth, but expression did not appear to be restricted to a particular stage of the cell cycle. hsp89 alpha mRNA was considerably more stable than the mRNA encoding hsp70, which can account for the higher constitutive rate of hsp89 synthesis in unstressed cells.

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