The expression of heat shock genes during normal development in Drosophila melanogaster (heat shock/abundant transcripts/developmental regulation)

Mason, Philip J.; Hall, Lucinda M. C.; Gausz, János

doi:10.1007/bf00383500

Cited by 131 publications

(90 citation statements)

References 39 publications

(40 reference statements)

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“…mRNA for DmHsp22 has been reported to be expressed at different developmental stages and sequences required for expression of its gene during heat shock and normal development are partly defined (26,61). King and Tower (30) showed that DmHsp22 was one of the most abundant heat shock protein in aged flies.…”

Section: Dmhsp22: a Small Heat Shock Protein In D Melanogastermentioning

confidence: 99%

The Small Heat Shock Protein Hsp22 of Drosophila melanogaster Is a Mitochondrial Protein Displaying Oligomeric Organization

Morrow

Inaguma

Kato

et al. 2000

Journal of Biological Chemistry

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Drosophila melanogaster has four main small heat shock proteins (Hsps), D. melanogaster Hsp22 (DmHsp22), Hsp23 (DmHsp23), Hsp26 (DmHsp26), and Hsp27 (DmHsp27). These proteins, although they have high sequence homology, show distinct developmental expression patterns. The function(s) of each small heat shock protein is unknown. DmHsp22 is shown to localize in mitochondria both in D. melanogaster S2 cells and after heterologous expression in mammalian cells. Fractionation of mitochondria indicates that DmHsp22 resides in the mitochondrial matrix, where it is found in oligomeric complexes, as shown by sedimentation and gel filtration analysis and by cross-linking experiments. Deletion analysis using a DmHsp22-EGFP construct reveals that residues 1-17 and an unknown number of residues between 17-28 are necessary for import. Sitedirected mutagenesis within a putative mitochondrial motif (WRMAEE) at positions 8 -13 shows that the first four residues are necessary for mitochondrial localization. Immunoprecipitation results indicate that there is no interaction between DmHsp22 and the other small heat shock proteins. The mitochondrial localization of this small Hsp22 of Drosophila and its high level of expression in aging suggests a role for this small heat shock protein in protection against oxidative stress.Exposure of organisms to various stresses activates a subset of genes encoding for phylogenically conserved proteins known as the heat shock proteins (Hsps).1 These proteins are commonly divided into families on the basis of molecular weight and sequence homologies. Members of the Hsp70, Hsp90, and Hsp60 families have been shown to act as molecular chaperones in protein folding or refolding following aggregation, and some assist protein translocation through a number of cellular membrane systems. Their chaperone activities are ATP-dependent, and the process is often assisted by co-chaperones. The sHsps comprise a more diverse and less conserved group of proteins, the number and sequences of which vary between and within species. They share a common structural domain in their C termini that shows high homology to the ␣A-and ␣B-crystallins (1). There is evidence for a chaperone-like activity of some sHsps in vitro, where they have been shown to interact with nonnative proteins in an ATP-independent manner (2-5). However, sHsps seem to be rather inefficient chaperones, and they have been suggested to act as reservoirs of nonnative refoldable proteins, which can be refolded in collaboration with other chaperones, such as Hsp70 (6, 7).The role(s) of sHsps in vivo remain unclear. Landry et al. (8) reported that overexpression of human Hsp27 could protect cells from the adverse effects of heat, a phenomenon referred to as thermotolerance. One of the sHsps of Drosophila melanogaster, DmHsp27, also conferred thermal resistance in the same assay (9). This finding is consistent with an early report (10) showing that induction of the Drosophila sHsps by the molting hormone ecdysone was sufficient to confer a thermostable phe...

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Section: Dmhsp22: a Small Heat Shock Protein In D Melanogastermentioning

confidence: 99%

The Small Heat Shock Protein Hsp22 of Drosophila melanogaster Is a Mitochondrial Protein Displaying Oligomeric Organization

Morrow

Inaguma

Kato

et al. 2000

Journal of Biological Chemistry

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“…The HSP70 gene itself is not activated under this condition but proteins for two HSPT0 family members are induced (35). An HSP70-1ike protein is one of the first proteins synthesized after zygote formation in mouse embryogenesis (4), and several HSPs are induced during oogenesis and pupation in Drosophila (25,36,44,59,70). …”

Section: Life Cycles and Heat Shock Proteinsmentioning

confidence: 99%

Heat shock proteins: the search for functions.

Schlesinger¹

1986

The Journal of Cell Biology

368

109

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“…In animal systems, the greatest proportion of hsp synthesis is represented by the high molecular mass hsp of 68 to 110 kD, with polypeptides of 70 kD being the predominant species (see Ref. '21 for review). In Drosophila, it has been shown that several low mol wt hsp are synthesized in significant amounts during normal development (3,18). The functions of the hs proteins at control temperatures may not be the same as at the hs temperature (3).…”

mentioning

confidence: 99%

Synthesis of the Low Molecular Weight Heat Shock Proteins in Plants

Mansfield

Key²

1987

Plant Physiol.

134

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Heat shock of living tissue induces the synthesis of a unique group of proteins, the heat shock proteins. In plants, the major group of heat shock proteins has a molecular mass of 15 to 25 kilodaltons. Accumulation of these proteins to stainable levels has been reported in only a few species. To examine accumulation of the low molecular weight heat shock proteins in a broader range of species, two-dimensional electrophoresis was used to resolve total protein from the following species: soybean (Glycine max L. Merr., var Wayne), pea (Pisum sativum L., var Early Alaska), sunflower (Helianthus annuus L.), wheat (Triticum aestivum L.), rice (Oryza sativa L., cv IR-36), maize (Zea mays L.), pearl millet (Pennisetum americanum L. Leeke, line 23DB), and Panicum miliaceum L. When identified by both silver staining and incorporation of radiolabel, a diverse array of low molecular weight heat shock proteins was synthesized in each of these species. These proteins accumulated to significant levels after three hours of heat shock but exhibited considerable heterogeneity in isoelectric point, molecular weight, stainability, and radiolabel incorporation. Although most appeared to be synthesized only during heat shock, some were detectable at low levels in control tissue. Compared to the monocots, a higher proportion of low molecular weight heat shock proteins was detectable in control tissues from dicots.

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The expression of heat shock genes during normal development in Drosophila melanogaster (heat shock/abundant transcripts/developmental regulation)

Cited by 131 publications

References 39 publications

The Small Heat Shock Protein Hsp22 of Drosophila melanogaster Is a Mitochondrial Protein Displaying Oligomeric Organization

The Small Heat Shock Protein Hsp22 of Drosophila melanogaster Is a Mitochondrial Protein Displaying Oligomeric Organization

Heat shock proteins: the search for functions.

Synthesis of the Low Molecular Weight Heat Shock Proteins in Plants

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