THE CONTROL OF ALDEHYDE OXIDASE AND XANTHINE DEHYDROGENASE ACTIVITIES AND CRM LEVELS BY THE mal LOCUS IN DROSOPHILA MELANOGASTER

1982 ◽  
Vol 24 (1) ◽  
pp. 11-17 ◽  
Author(s):  
M. M. Bentley ◽  
J. H. Williamson
Keyword(s):  
Drosophila Melanogaster ◽  
Full Advantage ◽  
Aldehyde Oxidase ◽  
Xanthine Dehydrogenase ◽  
Complementation Group ◽  
Activity Levels ◽  
Wild Type ◽  
Eye Color ◽  
Pleiotropic Phenotype

The effects of five new mal alleles on aldehyde oxidase (AO) and xanthine dehydrogenase (XDH) activities and CRM levels in Drosophila melanogaster are described. These alleles were isolated by taking full advantage of the pleiotropic phenotype exhibited by all previously described mal alleles and represent at least three unique examples of mal function. At least one of these alleles is a representative of a new complementation group. Two other alleles exhibit a wild-type eye color in homozygous stock and one of these is "leaky", exhibiting some 50% of the XDH activity normally found in Oregon-R control flies and some 12% of the AO activity. CRM and activity levels have been quantitated for both enzymes in all allelic heterozygotes. XDH-CRM levels vary only slightly around wild-type levels while AO-CRM levels appear much more sensitive to mutational alterations.

THE CONTROL OF ALDEHYDE OXIDASE AND XANTHINE DEHYDROGENASE ACTIVITIES BY THE CINNAMON GENE IN DROSOPHILA MELANOGASTER

1979 ◽  
Vol 21 (4) ◽  
pp. 457-471 ◽  
Author(s):  
Michael M. Bentley ◽  
John H. Williamson
Keyword(s):  
Drosophila Melanogaster ◽  
Aldehyde Oxidase ◽  
Heat Stability ◽  
Xanthine Dehydrogenase ◽  
Wild Type ◽  
Eye Color ◽  
Isolation And Characterization ◽  
Heat Labile ◽  
Complementation Groups

The isolation and characterization of 16 alleles of the cinnamon (cin, 1-0.0) locus in Drosophila melanogaster are described. The effects of cin on viability and the maternal effect of cin+ on eye color have been separated from each other as well as from the deficiency for aldehyde oxidase (AO) and xanthine dehydrogenase (XDH) activities. These 16 alleles have been assigned to four complementation groups based on analysis of AO and XDH activities in all heteroallelic female combinations. Zygotic complementation for lethality and eye color has been characterized and allows the ordering of cin alleles in a consistent pattern for the ability to produce viable zygotes and/or complement for the eye color phene. Several complementing cin combinations were analyzed for heat stability of AO. In all cases, AO from allelic heterozygotes was more heat labile than wild-type AO. One cin allele, cin13, produces heat labile AO in combination with cin+ from Oregon-R, hence exhibiting a "dominant" heat stability phenotype.

THE EFFECTS OF MOLYBATE, TUNGSTATE AND lxd ON ALDEHYDE OXIDASE AND XANTHINE DEHYDROGENASE IN DROSOPHILA MELANOGASTER

1981 ◽  
Vol 23 (4) ◽  
pp. 597-609 ◽  
Author(s):  
M. M. Bentley ◽  
J. H. Williamson ◽  
M. J. Oliver
Keyword(s):  
Drosophila Melanogaster ◽  
Sodium Tungstate ◽  
Enzyme System ◽  
Sodium Molybdate ◽  
Aldehyde Oxidase ◽  
Xanthine Dehydrogenase ◽  
Dietary Sodium ◽  
Screening Procedure ◽  
Eye Color

The effects of dietary sodium molybdate and sodium tungstate on eye color and aldehyde oxidase and xanthine dehydrogenase activities have been determined in Drosophila melanogaster. Dietary sodium tungstate administration has been used as a screening procedure to identify two new lxd alleles. Tungstate administration results in increased frequencies of "brown-eyed" flies in lxd stocks and a coordinate decrease in AO and XDH activities in all genotypes tested. The two new lxd alleles affect AO and XDH in a qualitatively but not quantitatively similar fashion to the original lxd allele. AO and XDH activity and AO-CRM levels appear much more sensitive to mutational perturbations of this gene-enzyme system than do XDH-CRM levels in the genotypes tested.

Complementation at the Maroon-like Eye-Color Locus of Drosophila melanogaster

Science ◽  
1960 ◽  
Vol 131 (3416) ◽  
pp. 1810-1811 ◽  
Author(s):  
Edward Glassman ◽  
William Pinkerton
Keyword(s):  
Drosophila Melanogaster ◽  
Xanthine Dehydrogenase ◽  
Wild Type ◽  
Eye Color ◽  
Enzyme Substrates

Two "allelic" Drosophila melanogaster mutants which are deficient in xanthine dehydrogenase can complement one another in heterozygotes. This complementation is due to the production of small amounts of xanthine dehydrogenase, enough of which is present to restore the normal eye color. However, not enough of the enzyme is present to produce normal amounts of the enzyme products, or to reduce the accumulation of the enzyme substrates to levels found in wild-type flies.

scholarly journals INTRACISTRONIC MAPPING OF ELECTROPHORETIC SITES IN DROSOPHILA MELANOGASTER: FIDELITY OF INFORMATION TRANSFER BY GENE CONVERSION

Genetics ◽  
1974 ◽  
Vol 76 (2) ◽  
pp. 289-299
Author(s):  
Margaret McCarron ◽  
William Gelbart ◽  
Arthur Chovnick
Keyword(s):  
Drosophila Melanogaster ◽  
Information Transfer ◽  
Large Scale ◽  
Genetic Basis ◽  
Xanthine Dehydrogenase ◽  
Specific Protein ◽  
Wild Type ◽  
Electrophoretic Variation ◽  
The Stability ◽  
Recombination Experiments

ABSTRACT A convenient method is described for the intracistronic mapping of genetic sites responsible for electrophoretic variation of a specific protein in Drosophila melanogaster. A number of wild-type isoalleles of the rosy locus have been isolated which are associated with the production of electrophoretically distinguishable xanthine dehydrogenases. Large-scale recombination experiments were carried out involving null enzyme mutants induced on electrophoretically distinct wild-type isoalleles, the genetic basis for which is followed as a nonselective marker in the cross. Additionally, a large-scale recombination experiment was carried out involving null enzyme rosy mutants induced on the same wild-type isoallele. Examination of the electrophoretic character of crossover and convertant products recovered from the latter experiment revealed that all exhibited the same parental electrophoretic character. In addition to documenting the stability of the xanthine dehydrogenase electrophoretic character, this observation argues against a special mutagenesis hypothesis to explain conversions resulting from allele recombination studies.

Die fluoreszierenden Stoffe aus den Malpighischen-Gefäßen der Wildform und verschiedener Augenfarbenmutanten von Drosophila melanogaster

1968 ◽  
Vol 23 (3) ◽  
pp. 376-386 ◽  
Author(s):  
Armin Wessing ◽  
Dieter Eichelberg
Keyword(s):  
Drosophila Melanogaster ◽  
Malpighian Tubules ◽  
Wild Type ◽  
Eye Color ◽  
Eye Color Mutants

The Malpighian tubules of Drosophila melanogaster accumulate a great number of substances, many of which fluoresce. This paper is concerned with the identification of these substances by chromatography and their location by fluorescentmicroscopy (fig. 4, 5). It appears that they mainly belong to the following three groups: Pteridines, tryptophane and some of its metabolites, and riboflavine (tab. 1).The pattern of fluorescent substances of the eye color mutants cn, v, se, st, bw, ry, and w vary significantly. The patterns of these mutants are compared and discussed with that of the wild-type.

scholarly journals EVIDENCE FOR REGULATORY VARIANTS OF THE DOPA DECARBOXYLASE AND ALPHA-METHYLDOPA HYPERSENSITIVE LOCI IN DROSOPHILA

Genetics ◽  
1986 ◽  
Vol 112 (2) ◽  
pp. 249-265 ◽  
Author(s):  
J Lawrence Marsh ◽  
T R F Wright
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Linkage ◽  
Dopa Decarboxylase ◽  
Activity Levels ◽  
Genetic Element ◽  
Wild Type ◽  
Molecular Analyses ◽  
Regulatory Variants ◽  
Close Proximity ◽  
Type Strains

ABSTRACT We have analyzed two variants of Drosophila melanogaster(RS and RE) which lead to the dual phenotype of elevated DDC activity and increased resistance to dietary alpha-methyldopa relative to Oregon-R controls. Both phenotypes show tight genetic linkage to the dopa decarboxylase, Ddc, and l(2)amd genes (i.e., < 0.05 cM distant). We find that low (Oregon-R), medium (RS) and high (RE and Canton-S) levels of DDC activity seen at both pupariation and eclosion in these strains are completely accounted for by differences in accumulation of DDC protein as measured by immunoprecipitation. Genetic reconstruction experiments in which Ddc  + and amd  + gene doses are varied show that increasing DDC activity does not lead to a measurable increase in resistance to dietary alphamethyldopa. This suggests that the increased resistance to dietary alpha-methyldopa is not the result of increased DDC activity but, rather, results from increased l(2)amd  + activity. Both cytogenetic and molecular analyses indicate that these overproduction variants are not the result of small duplications of the Ddc and amd genes, nor are they associated with small (?100 bp) insertions or deletions. Measurements of DDC activity in wild-type strains of Drosophila reveal a unimodal distribution of activity levels with the Canton-S and RE strains at the high end of the scale, the Oregon-R control at the low end and RS near the modal value. We conclude that accumulated changes in a genetic element (or elements) in close proximity to the Ddc  + and amd  + genes lead to the coordinated changes in the expression of the Ddc and amd genes in these strains.

scholarly journals Xanthine dehydrogenase is transported to the Drosophila eye.

Genetics ◽  
1989 ◽  
Vol 123 (3) ◽  
pp. 503-509 ◽  
Author(s):  
A G Reaume ◽  
S H Clark ◽  
A Chovnick
Keyword(s):  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Xanthine Dehydrogenase ◽  
Leader Sequence ◽  
Intermediary Metabolism ◽  
Peroxisomal Protein ◽  
Eye Color ◽  
Peroxisomal Targeting ◽  
A Cell ◽  
Color Phenotype

Abstract The rosy (ry) locus in Drosophila melanogaster codes for the enzyme xanthine dehydrogenase. Mutants that have no enzyme activity are characterized by a brownish eye color phenotype reflecting a deficiency in the red eye pigment. This report demonstrates that enzyme which is synthesized in some tissue other than the eye is transported and sequestered at the eye. Previous studies find that no leader sequence is associated with this molecule but a peroxisomal targeting sequence has been noted, and the enzyme has been localized to peroxisomes. This represents a rare example of an enzyme involved in intermediary metabolism being transported from one tissue to another and may also be the first example of a peroxisomal protein being secreted from a cell.

Notizen: A New Mutant Affecting Aldehyde Oxidase in Drosophila melanogaster

1979 ◽  
Vol 34 (3-4) ◽  
pp. 304-305 ◽  
Author(s):  
Michael M. Bentley ◽  
John H. Williamson
Keyword(s):  
Drosophila Melanogaster ◽  
Type Strain ◽  
Wild Type Strain ◽  
Aldehyde Oxidase ◽  
Heat Stability ◽  
Chromosome 2 ◽  
Control Strain ◽  
Wild Type ◽  
Mutant Stock ◽  
Wild Type Control

Abstract A new locus, Aldox-2, which affects the activity and heat stability of aldehyde oxidase in D. melanogaster is described. The Aldox-2 locus is localized to map position 86 on chromosome 2, between c and px. Aldehyde oxidase activity in Aldox-2 homozygotes is approximately 25 - 30% that of the Oregon-R wild-type control strain. The enzyme from the mutant stock is much more heat labile than is the enzyme from the wild-type strain. Both the activity and heat phenotypes are completely recessive.

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