THE EFFECTS OF LAO ON ALDEHYDE OXIDASE ACTIVITY AND CROSS-REACTING-MATERIAL IN DROSOPHILA MELANOGASTER

1978 ◽  
Vol 20 (4) ◽  
pp. 545-553 ◽  
Author(s):  
John H. Williamson ◽  
Michael M. Bentley ◽  
Melvin J. Oliver ◽  
Billy W. Geer
Keyword(s):  
Drosophila Melanogaster ◽  
Oxidase Activity ◽  
Mutant Allele ◽  
Aldehyde Oxidase ◽  
Wild Type ◽  
Heat Labile ◽  
Major Form ◽  
Normal Enzyme ◽  
Mutant Stock

In Drosophila melanogaster aldehyde oxidase occurs in at least two forms that can be separated electrophoretically. The mutant allele lao (low aldehyde oxidase activity) causes a deficiency of the major form of this enzyme. Immunoelectrophoretic analyses suggest that lao homozygotes produce aldehyde oxidase cross-reacting-material in nearly wild-type levels. Although aldehyde oxidase from the mutant stock is heat labile, properties such as Km and pH optima are not different from the normal enzyme.

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.

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.

Purification and characterization of an extracellular phenol oxidase from culture filtrates of Pyricularia oryzae

1996 ◽  
Vol 42 (5) ◽  
pp. 437-445 ◽  
Author(s):  
Aisha Alsubaey ◽  
Hugh D. Sisler ◽  
Benjamin F. Matthews
Keyword(s):  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Oxidase Activity ◽  
Phenol Oxidase ◽  
Pyricularia Oryzae ◽  
Wild Type ◽  
Phenol Oxidase Activity ◽  
Culture Filtrates ◽  
Major Form ◽  
Albino Mutant

Extracellular phenol oxidase activity was characterized and compared in Pyricularia oryzae wild-type and albino cell types to determine if this phenol oxidase was responsible for lack of melanization in the albino culture. Filtrates of the albino mutant Alb-5 showed activity similar to those of the wild type, while those of a buff mutant (Cp62) showed weak phenol oxidase activity. This indicated that the lack of melanization in the albino mutant was not due to an absence of phenol oxidase activity. The phenol oxidase isoform patterns from the wild type and two mutants were similar when analyzed by polyacrylamide gel electrophoresis. The slowest migrating isoform of phenol oxidase from wild-type Pyricularia oryzae was the major form and had a molecular mass of 380 kDa. The molecular masses of two of the minor forms were 220 and 130 kDa. The isoforms oxidized 1,8-dihydroxynaphthalene, the terminal metabolite in the polyketide pathway to melanin. The major phenol oxidase isoform was also present in extracts from albino mutants and the buff mutant. The major form was enriched by a combination of ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and elution from preparative polyacrylamide gels. The enriched isoform of phenol oxidase separated into two forms after a second electrophoresis, indicating that these two isoforms interconvert. Analysis of both forms by sodium dodecyl sulfate – polacrylamide gel electrophoresis indicated that both were composed of a single subunit with a molecular mass of 70 kDa. The enriched isoform preferred phloroglucinol as a substrate and had a Michaelis constant (Km) of 19.3 mM for phloroglucinol and a pH optimum between 6 and 7.5.Key words: phenol oxidase, laccase, Pyricularia oryzae, rice blast, melanin.

scholarly journals THE REGULATION OF WHITE LOCUS EXPRESSION: A DOMINANT MUTANT ALLELE AT THE WHITE LOCUS OF DROSOPHILA MELANOGASTER

Genetics ◽  
1980 ◽  
Vol 95 (2) ◽  
pp. 341-353
Author(s):  
Paul M Bingham
Keyword(s):  
Drosophila Melanogaster ◽  
Mutant Allele ◽  
Chromosomal Rearrangements ◽  
Wild Type Allele ◽  
Wild Type ◽  
Type Allele ◽  
Dominant Mutant ◽  
White Locus ◽  
Somatic Pairing

ABSTRACT A new mutant allele (wDZL)at the white locus of Drosophila melanogaster is dominant to the wild-type allele, but apparently only when the two alleles are synapsed. When chromosomal rearrangements prevent somatic pairing between the two white alleles, wDZL is rendered recessive to wild type. This observation suggests that the dominance of wDZL is sensitive to a synapsis (transvection) effect. On the basis of this and other properties, it is proposed that wDZL causes the repression of transcription of a synapsed w+ allele, but not of a w+ allele elsewhere in the same nucleus. One model to account for this supposes that wDzL produces a repressor of white-locus transcription. This repressor is presumed to be so unstable that other white genes, removed from wDZL but in the same nucleus, are not detectably repressed. These properties may be simply understood if it is assumed that the repressor produced by the wDZL allele is an RNA molecule.

scholarly journals LACK OF DOSAGE COMPENSATION FOR AN AUTOSOMAL GENE RELOCATED TO THE X CHROMOSOME IN DROSOPHILA MELANOGASTER

Genetics ◽  
1977 ◽  
Vol 85 (3) ◽  
pp. 489-496
Author(s):  
Richard L Roehrdanz ◽  
James M Kitchens ◽  
John C Lucchesi
Keyword(s):  
Drosophila Melanogaster ◽  
Experimental Evidence ◽  
Structural Gene ◽  
X Chromosome ◽  
Dosage Compensation ◽  
Oxidase Activity ◽  
Aldehyde Oxidase ◽  
Autosomal Gene

ABSTRACT Aldehyde oxidase activity has been measured in flies with the structural gene for this enzyme translocated to the X chromosome. These measurements are presented as experimental evidence that, in Drosophila melanogaster, an autosomal gene relocated to the X chromosome is not dosage compensated.

scholarly journals The lifespan of starving flies of different Drosophila melanogaster stocks: effects of caffeine and He-Ne laser light

2018 ◽  
Vol 22 ◽  
pp. 80-85
Author(s):  
O. V. Gorenskaya ◽  
N. S. Filiponenko ◽  
Yu. G. Shckorbatov
Keyword(s):  
Drosophila Melanogaster ◽  
Laser Light ◽  
External Factors ◽  
Lifespan Extension ◽  
Starvation Resistance ◽  
Wild Type ◽  
Aim Analysis ◽  
Chronic Effects ◽  
Cultural Medium ◽  
Mutant Stock

Aim. Analysis of the chronic effects of caffeine and laser radiation on starvation resistance in Drosophila melanogaster, in depends on the genotype. Methods. The experiments were carried out in wild type stocks of Drosophila melanogaster: Canton-S and Oregon; mutant stock ebony and stocks with mutation ebony saturated by stocks Canton-S and Oregon – ebonyC-S and ebonyOr. Caffeine was applied in concentration of 0.5 mg/ml in the cultural medium. Flies were exposed to He-Ne laser light of wavelength 632.8 nm and surface power density 0.03 mW/cm2 for 5 minutes. Control flies were grown under standard living conditions. Results. The lifespan during starvation dependence on a genotype (17.62 % and 19.51 %), external factors (h = 17.02 % and 19.64 %) and on the combined factors – h = 4.37 % and 2.42 % (for males and males, respectively) was shown. Conclusions. Almost in all experimental variants caffeine and laser light induced the extension lifespan during starvation. The simultaneous applying of both factors (caffeine+laser light) induced the maximal lifespan extension in Drosophila stocks C-S, ebony, and ebonyOr. Such additive effect was not observed in ebonyC-S flies. We connect the observed effects of caffeine and laser light with hormesis effect.Keywords: drosophila, genotype, lifespan during starvation, mutation, stress tolerance.

GENETIC CONTROL OF ALDEHYDE OXIDASE ACTIVITY AND CROSS-REACTING-MATERIAL IN DROSOPHILA MELANOGASTER

1978 ◽  
Vol 20 (4) ◽  
pp. 489-497 ◽  
Author(s):  
Eva M. Meidinger ◽  
John H. Williamson
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Control ◽  
Structural Gene ◽  
Oxidase Activity ◽  
Aldehyde Oxidase ◽  
Xanthine Dehydrogenase ◽  
The Other ◽  
Pyridoxal Oxidase

Four different genes are known to affect aldehyde oxidase activity (AO) in Drosophila melanogaster. Mutants at each of these loci eliminate AO activity and simultaneously eliminate detectable AO-crossing reacting material (AO-CRM) even though only one is the structural gene for AO (Aldoxn). The other three genes (cin1, lxd and mal) coordinately "control" the levels of activity of AO and two related enzymes, xanthine dehydrogenase (XDH) and pyridoxal oxidase (PO). Contrary to their effects on AO-CRM, neither of these three mutants eliminate XDH-CRM. A model of interaction of these enzymes and genes controlling their activities is discussed.

Sign in / Sign up

Export Citation Format

Share Document