Genetic and molecular analysis in the 70CD region of the third chromosome of Drosophila melanogaster

Burmester, Thorsten; Mink, Mátyás; Pál, Margit; Lászlóffy, Zsolt; Lepesant, Jean Antoine; Maróy, Péter

doi:10.1016/s0378-1119(00)00066-4

Cited by 6 publications

(6 citation statements)

References 26 publications

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“…Similarly, mice that lack all Hsp70 genes are also viable (Hunt et al 2004). However, mutations in several of the constitutively expressed homologues of Hsp70 in Drosophila do cause lethality (Elefant and Palter 1999;Burmester et al 2000; http://flybase.bio.indiana.edu), indicating that the Hsc70 family of proteins carries out critical functions at normal temperatures. Furthermore, we found that Hsp70-null females, though fertile, have a significant reduction in fertility, indicating that the heatinducible genes also have some role at normal temperature.…”

Section: Discussionmentioning

confidence: 99%

Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration

Gong

Golic²

2006

Genetics

128

106

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The heat-shock response is a programmed change in gene expression carried out by cells in response to environmental stress, such as heat. This response is universal and is characterized by the synthesis of a small group of conserved protein chaperones. In Drosophila melanogaster the Hsp70 chaperone dominates the profile of protein synthesis during the heat-shock response. We recently generated precise deletion alleles of the Hsp70 genes of D. melanogaster and have used those alleles to characterize the phenotypes of Hsp70-deficient flies. Flies with Hsp70 deletions have reduced thermotolerance. We find that Hsp70 is essential to survive a severe heat shock, but is not required to survive a milder heat shock, indicating that a significant degree of thermotolerance remains in the absence of Hsp70. However, flies without Hsp70 have a lengthened heat-shock response and an extended developmental delay after a non-lethal heat shock, indicating Hsp70 has an important role in recovery from stress, even at lower temperatures. Lack of Hsp70 also confers enhanced sensitivity to a temperature-sensitive lethal mutation and to the neurodegenerative effects produced by expression of a human polyglutamine disease protein.

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Section: Discussionmentioning

confidence: 99%

Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration

Gong

Golic²

2006

Genetics

128

106

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“…Genomic DNA extraction and plasmid rescue from P-elementbearing strains were performed as described previously (Burmester et al, 2000). Electrophoresis and blotting of nucleic acids, RNA purification and polyA + selection, non-radioactive-or radiolabelling, Southern and Northern analyses, PCR amplification of col4a1 exon sequences and DNA sequencing were carried out according to standard methods (Sambrook et al, 1989).…”

Section: Nucleic Acid Analysismentioning

confidence: 99%

Drosophila basement membrane collagen col4a1 mutations cause severe myopathy

et al. 2012

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“…Enzymes of these supplemental pathways are usually absent or localized in nonperoxisomal compartments in most eukaryotes, and their peroxisomal localization is a specialization of relatively few species. Examples of facultative peroxisomal pathways are glycolysis and purine salvage (in the peroxisomes of kinetoplastids, such as Trypanosoma and Leishmania [23]), isoprenoid biosynthesis (in vertebrates [1]), ether phospholipid biosynthesis (in kinetoplastids and animals [15,33]), and the glyoxylate cycle, which channels the products of beta-oxidation into gluconeogenesis in plants, yeasts, and Caenorhabditis elegans (7).Peroxisome-deficient mutants of most organisms are viable (with the possible exception of kinetoplastids), but a lack of functional peroxisomes can lead to severe pathologies in multicellular organisms (3,5,8,16,20,24). In all organisms examined, the most severely affected metabolic pathway is the beta-oxidation of fatty acids, but in human patients bile acid production and cholesterol biosynthesis also seem to be impaired.…”

mentioning

confidence: 99%

“…Peroxisome-deficient mutants of most organisms are viable (with the possible exception of kinetoplastids), but a lack of functional peroxisomes can lead to severe pathologies in multicellular organisms (3,5,8,16,20,24). In all organisms examined, the most severely affected metabolic pathway is the beta-oxidation of fatty acids, but in human patients bile acid production and cholesterol biosynthesis also seem to be impaired.…”

mentioning

confidence: 99%

Loss of Compartmentalization Causes Misregulation of Lysine Biosynthesis in Peroxisome-Deficient Yeast Cells

et al. 2002

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To characterize the metabolic role of peroxisomes in yeast cells under physiological conditions, we performed a comprehensive meta-analysis of published microarray data. Previous studies of yeast peroxisomes have mainly been focused on the function of peroxisomes under extreme conditions, such as growth on oleate or methanol as the sole carbon source, and may therefore not be representative of the normal physiological role of yeast peroxisomes. Surprisingly, our analysis of the microarray data reveals that the only pathway responding to peroxisome deficiency in mid-log phase is lysine biosynthesis, whereas classical peroxisomal pathways such as beta-oxidation are unaffected. We show that the upregulation of lysine biosynthesis genes in peroxisome-deficient yeasts shares many characteristics with the physiological response to lysine starvation. We provide data that suggest that this is the result of a "pathological" stimulation of the Lys14p transcriptional activator by the pathway intermediate aminoadipate semialdehyde. Mistargeting of the peroxisomal lysine pathway to the cytosol increases the active concentration of aminoadipate semialdehyde, which is no longer contained in the peroxisome and can now activate Lys14p at much lower levels than in wild-type yeasts. This is the first well-documented example of pathway misregulation in response to peroxisome deficiency and will be useful in understanding the phenotypic details of human peroxisome-deficient patients (Zellweger syndrome).Peroxisomes are single-membrane-bounded organelles present in most eukaryotic cells, with the exception of Plasmodium, Giardia, Trichomonas, Entamoeba, and related species. Peroxisomes typically contain the enzymes of fatty acid betaoxidation and catalase, which converts the hydrogen peroxide formed by fatty acyl-coenzyme A (CoA) oxidase to water and oxygen. Several other oxidases, e.g., monoamine oxidase, urate oxidase, hydroxyacid oxidase, methanol oxidase, and acetylspermidine oxidase, are also present in peroxisomes of some species and benefit from the same detoxification mechanism. In addition to these oxidative reactions, peroxisomes may contain many other biosynthetic pathways. Enzymes of these supplemental pathways are usually absent or localized in nonperoxisomal compartments in most eukaryotes, and their peroxisomal localization is a specialization of relatively few species. Examples of facultative peroxisomal pathways are glycolysis and purine salvage (in the peroxisomes of kinetoplastids, such as Trypanosoma and Leishmania [23]), isoprenoid biosynthesis (in vertebrates [1]), ether phospholipid biosynthesis (in kinetoplastids and animals [15,33]), and the glyoxylate cycle, which channels the products of beta-oxidation into gluconeogenesis in plants, yeasts, and Caenorhabditis elegans (7).Peroxisome-deficient mutants of most organisms are viable (with the possible exception of kinetoplastids), but a lack of functional peroxisomes can lead to severe pathologies in multicellular organisms (3,5,8,16,20,24). In all organisms ex...

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Genetic and molecular analysis in the 70CD region of the third chromosome of Drosophila melanogaster

Cited by 6 publications

References 26 publications

Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration

Loss of Hsp70 in Drosophila Is Pleiotropic, With Effects on Thermotolerance, Recovery From Heat Shock and Neurodegeneration

Drosophila basement membrane collagen col4a1 mutations cause severe myopathy

Loss of Compartmentalization Causes Misregulation of Lysine Biosynthesis in Peroxisome-Deficient Yeast Cells

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