Expression of Drosophila heat-shock cognate genes during heat shock and development

Craig, Elizabeth A.; Ingolia, Thomas D.; Manseau, Lynn J.

doi:10.1016/0012-1606(83)90291-9

Cited by 166 publications

(97 citation statements)

References 28 publications

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“…All of these genes are known to be responsive to heat shock (20). The heat-shock cognate genes (Hsc) have been reported to be expressed at normal temperatures but are not further induced by heat shock (21,22). In accordance with this, we observed no marked change in expression level for Hsc70-1, Hsc70-4, and Hsc70-5.…”

Section: Quantitative Transcript Imaging Of Heat-shocked Compared Withsupporting

confidence: 84%

Quantitative transcript imaging in normal and heat-shocked Drosophila embryos by using high-density oligonucleotide arrays

Leemans

Egger

Loop

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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Embryonic development in Drosophila is characterized by an early phase during which a cellular blastoderm is formed and gastrulation takes place, and by a later postgastrulation phase in which key morphogenetic processes such as segmentation and organogenesis occur. We have focused on this later phase in embryogenesis with the goal of obtaining a comprehensive analysis of the zygotic gene expression that occurs during development under normal and altered environmental conditions. For this, a functional genomic approach to embryogenesis has been developed that uses highdensity oligonucleotide arrays for large-scale detection and quantification of gene expression. These oligonucleotide arrays were used for quantitative transcript imaging of embryonically expressed genes under standard conditions and in response to heat shock. In embryos raised under standard conditions, transcripts were detected for 37% of the 1,519 identified genes represented on the arrays, and highly reproducible quantification of gene expression was achieved in all cases. Analysis of differential gene expression after heat shock revealed substantial expression level changes for known heat-shock genes and identified numerous heat shock-inducible genes. These results demonstrate that highdensity oligonucleotide arrays are sensitive, efficient, and quantitative instruments for the analysis of large scale gene expression in Drosophila embryos. R ecently the genome of the first multicellular eukaryote Caenorhabditis elegans was completely elucidated (1). Sequencing of the Drosophila melanogaster genome has now also been carried out, and currently the corresponding putative open reading frames are being defined and verified (2). On the basis of this complete genomic information, it will now be important to determine the complex expression of all encoded genes and to analyze physiological as well as pathological phenomena from a global genetic perspective. Large-scale transcript analysis is made possible by DNA micro-or oligonucleotide arrays (3, 4), both of which allow the simultaneous monitoring of hundreds of mRNA expression profiles (5, 6). In this study, we used Drosophila high-density oligonucleotide arrays to monitor the simultaneous expression of zygotically active genes during the later postgastrulation stages of embryonic development (7-9). We analyzed the relative abundance levels of hundreds of embryonically expressed genes under normal physiological conditions and in response to heat shock (10). In embryos raised under normal conditions, we obtained highly reproducible quantification for 563 expressed genes corresponding to different functional classes. After a 36°C heat shock, we detected increases in expression levels for known heat-shock genes and identified numerous heat-shock-inducible genes. Materials and MethodsEmbryos. D. melanogaster Oregon R stocks were kept on standard cornmeal͞yeast͞agar medium at 25°C. Embryos were collected overnight on grape-juice plates for 12 h and were kept for a further 5 h at 25°C before RNA isolation...

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Section: Quantitative Transcript Imaging Of Heat-shocked Compared Withsupporting

confidence: 84%

Quantitative transcript imaging in normal and heat-shocked Drosophila embryos by using high-density oligonucleotide arrays

Leemans

Egger

Loop

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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“…This is the third case of a homolog of one of the members of the E. coli htpR regulon (38,51) being identified in eucaryotes. However, while hsp70 and its cognates (homologs to the dnaK-encoded protein [2]) and hsp80 (related to (9,11,39), only a single form of hsp58 has been detected (34) and it apparently functions during both nonstress and stress conditions. In this regard, it behaves much more like its bacterial homolog.…”

Section: Resultsmentioning

confidence: 99%

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.

McMullin¹,

Hallberg²

1988

Mol. Cell. Biol.

225

122

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We recently reported that a Tetrahymena thermophila 58-kilodaltodi (kDa) mitochondrial protein (hsp58) was selectively synthesized during heat shock. In this study, we show that hsp58 displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae (64 kDa), Xenopus laevis (60 kDa), Zea mays (62 kDa), and human cells (59 kDa). Furthermore, a 58-kDa protein from Eschenchia coli also exhibited antigenic cross-reactivity to an antiserum directed against the T. thermophila mitochondrial protein. The proteins from S. cerevisiae and E. coli antigenically related to hsp58 were studied in detail and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes. The T. thermophila, S. cerevisiae, and E. coli macromolecular complexes containing these related proteins had similar sedimentation characteristics and virtually identical morphologies as seen with the electron microscope. The distinctive properties of the E. coli homolog to T. thermophila hsp58 indicate that it is most likely the product of the groEL gene.Most organisms subjected to sublethal heat shock-inducing temperatures become conditioned to survive at even higher, normally lethal, temperatures. The acquisition of this thermotolerant state is accompanied by the production of specific arrays of polypeptides, collectively known as heat shock proteins (HSPs), which are thought to be involved in protecting the organism from hyperthermic stress (for reviews, see references 8 and 32). Several of these proteins have been shown to exhibit a relatively high degree of evolutionary conservation in their DNA and amino acid sequences (2-5, 12, 24-26, 28), as well as in their subcellular compartmentalization (1,30,45,47). This conservation of structure and localization within the cell strongly suggests that these proteins perform similar functions in the different species in which these proteins are found.In Tetrahymena thermophila, shifting cells to 37 through 41°C induces the selective synthesis of a specific array of HSPs (16,18,19,33,49). Recently, we purified and characterized a minor member of this set of proteins. We find that not only is this protein, hsp58, one of the proteins selectively synthesized and accumulated early in heat shock, but it is also a normal component of the mitochondria of this organism. Heat shock causes the level of hsp58 to increase approximately two-to threefold, and this protein also accumulates specifically in mitochondria. Another interesting property of hsp58 is that it assembles into large oligomeric complexes consisting primarily of the hsp58 protein (34).Since at least two of the HSPs of T. thermophila, hsp73 and hsp80, exhibit evolutionary conservation with HSPs of other species (18), we decided to ask whether homologs of hsp58 also exist in other organisms. This was done by using an antiserum prepared against highly purified hsp58 (34) to probe protein samples from several diverse species. In this study, ...

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“…Three of these are known only by their subunit molecular weights: HSP90, HSP70, and HSP 20-30. The precise molecular weight varies slightly among different organisms, In the eukaryotic cell, each group appears to constitute a gene family consisting of closely related protein isoforms and genes encoding sequences regulated by different promoters (14,16,19,46,50,59,79). The fourth HSP is ubiquitin, a protein of 8,000 mol wt.…”

mentioning

confidence: 99%

Heat shock proteins: the search for functions.

Schlesinger¹

1986

The Journal of Cell Biology

369

109

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Expression of Drosophila heat-shock cognate genes during heat shock and development

Cited by 166 publications

References 28 publications

Quantitative transcript imaging in normal and heat-shocked Drosophila embryos by using high-density oligonucleotide arrays

Quantitative transcript imaging in normal and heat-shocked Drosophila embryos by using high-density oligonucleotide arrays

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene.

Heat shock proteins: the search for functions.

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