Expression of the small heat shock genes during Drosophila development: comparison of the accumulation of hsp23 and hsp27 mRNAs and polypeptides

Genome ◽  
1989 ◽  
Vol 31 (2) ◽  
pp. 671-676 ◽  
Author(s):  
Daniel Pauli ◽  
André-Patrick Arrigo ◽  
Julio Vazquez ◽  
Chia-Hua Tonka ◽  
Alfred Tissières
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Normal Development ◽  
Pupal Stage ◽  
External Stress ◽  
Messenger Rnas ◽  
Heat Shock Genes ◽  
Drosophila Development ◽  
Chromosomal Site ◽  
Shock Proteins

Seven heat shock genes are clustered within 15 kilobases of DNA at the Drosophila melanogaster chromosomal site 67B. They show a complex pattern of expression in the absence of external stress during normal development of this organism. In this paper, we quantitatively compare the abundance of the messenger RNAs for these seven genes at all major stages of Drosophila development and then focus on hsp23 and hsp27 for which available antibodies allow the comparison between the accumulation of the mRNAs and that of their corresponding polypeptides. Transcripts for both genes are maximally abundant in white prepupae. We observe that the amount of hsp23 message decreases more rapidly than that of hsp27 mRNA throughout the pupal period. The maximal abundance of the proteins occurs at the middle of the pupal stage, when their corresponding RNAs have almost completely disappeared. The peaks of expression of the proteins are also broader than those of their transcripts, indicating that the half-lives of the polypeptides are longer. These observations suggest that complex mechanisms regulate the expression of the small heat shock genes during Drosophila development.Key words: Drosophila, development, heat shock, heat shock proteins, heat shock RNA.

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 Expression of heat shock protein 70 is insufficient to extend Drosophila melanogaster longevity

2019 ◽  
Author(s):  
Chengfeng Xiao ◽  
Danna Hull ◽  
Shuang Qiu ◽  
Joanna Yeung ◽  
Jie Zheng ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Resistance ◽  
Heat Shock Protein 70 ◽  
Biological Effect ◽  
Hsp70 Expression ◽  
Gene Encoding ◽  
Shock Proteins

AbstractIt has been known for over 20 years that Drosophila melanogaster flies with twelve additional copies of the hsp70 gene encoding the 70 kDa heat shock protein lives longer after a non-lethal heat treatment. Since the heat treatment also induces the expression of additional heat shock proteins, the biological effect can be due either to HSP70 acting alone or in combination. This study used the UAS/GAL4 system to determine whether hsp70 is sufficient to affect the longevity and the resistance to thermal, oxidative or desiccation stresses of the whole organism. We observed that HSP70 expression in the nervous system or muscles has no effect on longevity or stress resistance but ubiquitous expression reduces the life span of males. We also observed that the down-regulation of Hsp70 using RNAi did not affect longevity.

Morphological and molecular modifications induced by heat shock in Drosophila melanogaster embryos

Development ◽  
1983 ◽  
Vol 77 (1) ◽  
pp. 167-182
Author(s):  
Giorgio Graziosi ◽  
Franco de Cristini ◽  
Angelo di Marcotullio ◽  
Roberto Marzari ◽  
Fulvio Micali ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Dna Synthesis ◽  
Histological Analysis ◽  
Developmental Stages ◽  
Early Embryo ◽  
Direct Relation ◽  
Hsp 70 ◽  
Survival Pattern ◽  
Shock Proteins

The early embryo of Drosophila melanogaster did not survive treatment at 37 °C (heat shock) for 25 min. The histological analysis of eggs treated in this way showed that the heat shock caused disintegration of nuclei and of cytoplasmic islands, displacement and swelling of nuclei and blocked mitoses. These effects were not observed in embryos treatedafter blastoderm formation. After this stage, we noticed that development was slowed down. The heat shock proteins (hsp 83,70 and 68) were, under shock, synthesized at all developmental stages. There was little or no synthesis of hsp 70 and 68 in unfertilized eggs, but synthesis increased in proportion to the number of nuclei present. Most probably, hsp 70 synthesis was directed by zygotic mRNA. DNA synthesis was not blocked by the heat shock though the overall incorporation of [3H]thymidine was substantially reduced, presumably because of the block of mitoses. We did not find a direct relation between survival pattern and hsp synthesis. We concluded that some, at least, of the heat shock genes can be activated at all developmental stages and that heat shock could be used for synchronizing mitoses.

The expression of heat-shock genes in higher plants

1986 ◽  
Vol 314 (1166) ◽  
pp. 453-468 ◽  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Higher Plants ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
Heat Shock Gene ◽  
Regulatory Sequences ◽  
Heat Shock Genes ◽  
Control Of Gene Expression ◽  
Shock Proteins

High-temperature stress or heat shock induces the vigorous synthesis of heat-shock proteins in many organisms including the higher plants. This response has been implicated in the acquisition of thermotolerance. The biological importance of a group of low-molecular-mass proteins in the response of plants is indicated by the conservation of the corresponding genes. The steady-state levels of mRNAs for these proteins shift from undetectable levels at normal temperature to about 20 000 molecules per gene in the cell after heat shock. The analysis of ‘run-off’ transcripts from isolated soybean nuclei suggests a transcriptional control of gene expression. The DNA sequence analysis of soybean heat-shock genes revealed a conservation of promoter sequences and 5'-upstream elements. A comparison of the deduced amino acid sequences of polypeptides showed a conservation of structural features in heat-shock proteins between plants and animals. The implication of a common regulatory concept in the heat-shock response makes genes belonging to this family (15-18 kDa proteins) in soybean favourable candidates for investigating thermoregulation of transcription. We have exploited the natural gene transfer system of Agrobacterium tumefaciens to introduce a soybean heat-shock gene into the genomes of sunflower and tobacco. The gene is thermoinducibly transcribed and transcripts are faithfully initiated in transgenic plants. Experiments are in progress to define the regulatory sequences 5'-upstream from the gene. The expression of heat-shock genes in a heterologous genetic background also provides the basis for studying the function of the proteins and their possible role in thermoprotection.

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