Regulation of amylase activity in Drosophila melanogaster: Variation in the number of enzyme molecules produced by different amylase genotypes

1981 ◽  
Vol 19 (7-8) ◽  
pp. 783-796 ◽  
Author(s):  
D. A. Hickey
Keyword(s):  
Drosophila Melanogaster ◽  
Amylase Activity ◽  
Enzyme Molecules

scholarly journals THE INTERACTION OF GENETIC AND ENVIRONMENTAL FACTORS IN THE CONTROL OF AMYLASE GENE EXPRESSION IN DROSOPHILA MELANOGASTER

Genetics ◽  
1986 ◽  
Vol 114 (3) ◽  
pp. 943-954
Author(s):  
Bernhard F Benkel ◽  
Donal A Hickey
Keyword(s):  
Gene Expression ◽  
Drosophila Melanogaster ◽  
Environmental Factors ◽  
Molecular Basis ◽  
Amylase Activity ◽  
Glucose Repression ◽  
Amylase Gene ◽  
Dietary Effects ◽  
Eukaryotic Gene ◽  
Genetic And Environmental Factors

ABSTRACT A number of previous studies have established that amylase activity can vary between Drosophila strains which are maintained under identical laboratory conditions. In addition, we have recently shown that all strains examined so far are subject to glucose repression of amylase activity. In this study, we show that the degree of glucose repression can vary between strains. Moreover, the glucose repression effect is much more pronounced in larvae than in adult flies. Our results lead to the conclusion that the strain-specific differences in activity and the dietary effects are not independent phenomena. These results have implications for the interpretation of many studies on amylase activity variation, including those experiments which have been designed to link amylase activity variations with fitness differences in nature. A question that naturally arises concerns the molecular basis for these strain-specific variations in the degree of glucose repression of this eukaryotic gene.

scholarly journals Genetic factors on the second and third chromosomes responsible for the variation of amylase activity and inducibility in Drosophila melanogaster

1997 ◽  
Vol 70 (2) ◽  
pp. 97-103 ◽  
Author(s):  
YOSHINORI MATSUO ◽  
TSUNEYUKI YAMAZAKI
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Factors ◽  
Specific Activity ◽  
Amylase Activity ◽  
Chromosome Substitution ◽  
Substitution Lines ◽  
Functional Roles ◽  
Chromosome Substitution Lines ◽  
The Third ◽  
Specific Activities

Using second- or third-chromosome substitution lines of Drosophila melanogaster, the genetic variation of inducibility and amylase specific activities in three media (starch, normal and glucose) were investigated. Genetic factors on both the second and third chromosomes were responsible for the variation in amylase specific activity and inducibility. In glucose medium, the genetic variance of amylase specific activity estimated for the second-chromosome substitution lines was larger than that for the third-chromosome substitution lines; however, for starch medium and inducibility, the variance was larger for the third-chromosome substitution lines. High correlations for the second-chromosome substitution lines and low correlations for the third-chromosome substitution lines were observed for amylase specific activities in different media. These results suggest that the genetic factor(s) responsible for inducibility or amylase activity variation in an induced medium such as starch should be on the third chromosome and those in the non-induced medium such as glucose should be on the second chromosome. The functional roles of the factors on the second and third chromosomes would be the repression and induction of amylase, respectively.

Expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans and some properties of the recombinant enzyme

2002 ◽  
Vol 362 (2) ◽  
pp. 223-229 ◽  
Author(s):  
Benjamin ADAMS ◽  
David J. LOWE ◽  
Andrew T. SMITH ◽  
Claudio SCAZZOCCHIO ◽  
Stephane DEMAIS ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Aspergillus Nidulans ◽  
Specific Activity ◽  
Recombinant Expression ◽  
Expression System ◽  
Complex Mixture ◽  
Xanthine Dehydrogenase ◽  
Cell System ◽  
Post Translational Modification ◽  
Enzyme Molecules

Recent crystal structures of xanthine dehydrogenase, xanthine oxidase and related enzymes have paved the way for a detailed structural and functional analysis of these enzymes. One problem encountered when working with these proteins, especially with recombinant protein, is that the preparations tend to be heterogeneous, with only a fraction of the enzyme molecules being active. This is due to the incompleteness of post-translational modification, which for this protein is a complex, and incompletely understood, process involving incorporation of the Mo and Fe/S centres. The enzyme has been expressed previously in both Drosophila and insect cells using baculovirus. The insect cell system has been exploited by Iwasaki et al. [Iwasaki, Okamoto, Nishino, Mizushima and Hori (2000) J. Biochem (Tokyo) 127, 771–778], but, for the rat enzyme, yields a complex mixture of enzyme forms, containing around 10% of functional enzyme. The expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans is described. The purified protein has been analysed both functionally and spectroscopically. Its specific activity is indistinguishable from that of the enzyme purified from fruit flies [Doyle, Burke, Chovnick, Dutton, Whittle and Bray (1996) Eur. J. Biochem. 239, 782–795], and it appears to be more active than recombinant xanthine dehydrogenase produced with the baculovirus system. EPR spectra of the recombinant Drosophila enzyme are reported, including parameters for the Fe/S centres. Only a very weak ‘Fe/SIII’ signal (g1,2,3, 2.057, 1.930, 1.858) was observed, in contrast to the strong analogous signal reported for the enzyme from baculovirus. Since this signal appears to be associated with incomplete post-translational modification, this is consistent with relatively more complete cofactor incorporation in the Aspergillus-produced enzyme. Thus we have developed a recombinant expression system for D. melanogaster xanthine dehydrogenase, which can be used for the production of site-specific mutations of this enzyme.

scholarly journals GLUCOSE REPRESSION OF AMYLASE GENE EXPRESSION IN DROSOPHILA MELANOGASTER

Genetics ◽  
1986 ◽  
Vol 114 (1) ◽  
pp. 137-144
Author(s):  
Bernhard F Benkel ◽  
Donal A Hickey
Keyword(s):  
Gene Expression ◽  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Cyclic Amp ◽  
Xenopus Oocytes ◽  
Amylase Activity ◽  
Glucose Repression ◽  
Repressive Effect ◽  
Translatable Mrna ◽  
Effect Of Glucose

ABSTRACT We have previously shown that dietary glucose can reduce amylase activity in both adults and larvae of Drosophila; this reduction in enzyme activity reflects a reduction in the quantity of amylase protein, rather than an inhibition of enzyme activity. Here, we report that we have now defined conditions in which the repressive effect of glucose can be greater than 100-fold. Moreover, this repression is partially counteracted by the addition of exogenous cyclic AMP. We also show that there is a direct correlation between changes in amylase activity and changes in the amount of translatable mRNA as assayed in microinjected Xenopus oocytes. This means that the glucose repression is occurring at a pretranslational stage.

Author response for "Location and arrangement of campaniform sensilla in Drosophila melanogaster"

2020 ◽  
Author(s):  
Gesa F. Dinges ◽  
Alexander S. Chockley ◽  
Till Bockemühl ◽  
Kei Ito ◽  
Alexander Blanke ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Author Response ◽  
Campaniform Sensilla
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