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.

Purine transport by Malpighian tubules of pteridine-deficient eye color mutants of Drosophila melanogaster

1979 ◽  
Vol 17 (5-6) ◽  
pp. 565-573 ◽  
Author(s):  
David T. Sullivan ◽  
L. Anne Bell ◽  
Duncan R. Paton ◽  
Marie C. Sullivan
Keyword(s):  
Drosophila Melanogaster ◽  
Malpighian Tubules ◽  
Eye Color ◽  
Eye Color Mutants

scholarly journals DEVELOPMENTAL AND GENETIC STUDIES ON KYNURENINE HYDROXYLASE FROM DROSOPHILA MELANOGASTER

Genetics ◽  
1973 ◽  
Vol 75 (4) ◽  
pp. 651-661
Author(s):  
David T Sullivan ◽  
Robert J Kitos ◽  
Marie C Sullivan
Keyword(s):  
Drosophila Melanogaster ◽  
Bimodal Distribution ◽  
Maximum Activity ◽  
Wild Type ◽  
Genetic Studies ◽  
Eye Color ◽  
Eye Color Mutants ◽  
Puparium Formation ◽  
Kynurenine Hydroxylase ◽  
Short Time

ABSTRACT The level of kynurenine hydroxylase was measured throughout the development of wild type and the eye color mutants v, cn, st, ltd, cd, kar, w, ca, bri and pP of Drosophila melanogaster. In all cases except cn a bimodal distribution of enzyme activity during development was observed. Activity is initially detectable in second instar. A maximum is reached in early third instar. Activity declines prior to puparium formation. Shortly after pupation, activity rises dramatically to reach a maximum about five times the peak larval level. Maximum activity persists for a short time, and then falls sharply prior to emergence. No activity is detectable in cn, cn3, or cn35K. In pupae which have zero, one, two or three doses of the cn  + allele, activity is proportional to the number of the + alleles. This provides further evidence that the cn locus contains the structural gene for kynurenine hydroxylase. Kynurenine hydroxylase is a useful gene product for studying the events of imaginal disc differentiation.

scholarly journals deep-orange and carnation define distinct stages in late endosomal biogenesis in Drosophila melanogaster

2003 ◽  
Vol 161 (3) ◽  
pp. 593-607 ◽  
Author(s):  
V. Sriram ◽  
K.S. Krishnan ◽  
Satyajit Mayor
Keyword(s):  
Drosophila Melanogaster ◽  
High Resolution ◽  
Immunofluorescence Microscopy ◽  
High Resolution Imaging ◽  
Wild Type ◽  
Eye Color ◽  
Late Endosomes ◽  
Eye Color Mutants ◽  
Resolution Imaging ◽  
Endocytic Compartments

Endosomal degradation is severely impaired in primary hemocytes from larvae of eye color mutants of Drosophila. Using high resolution imaging and immunofluorescence microscopy in these cells, products of eye color genes, deep-orange (dor) and carnation (car), are localized to large multivesicular Rab7-positive late endosomes containing Golgi-derived enzymes. These structures mature into small sized Dor-negative, Car-positive structures, which subsequently fuse to form tubular lysosomes. Defective endosomal degradation in mutant alleles of dor results from a failure of Golgi-derived vesicles to fuse with morphologically arrested Rab7-positive large sized endosomes, which are, however, normally acidified and mature with wild-type kinetics. This locates the site of Dor function to fusion of Golgi-derived vesicles with the large Rab7-positive endocytic compartments. In contrast, endosomal degradation is not considerably affected in car1 mutant; fusion of Golgi-derived vesicles and maturation of large sized endosomes is normal. However, removal of Dor from small sized Car-positive endosomes is slowed, and subsequent fusion with tubular lysosomes is abolished. Overexpression of Dor in car1 mutant aggravates this defect, implicating Car in the removal of Dor from endosomes. This suggests that, in addition to an independent role in fusion with tubular lysosomes, the Sec1p homologue, Car, regulates Dor function.

Über das Auftreten von Tetrahydrobiopterin und Riboflavin in den Malpighischen Gefäßen von Drosophila melanogaster und deren Mutante brown

1969 ◽  
Vol 24 (1) ◽  
pp. 123-127
Author(s):  
Dieter Eichelberg
Keyword(s):  
Drosophila Melanogaster ◽  
Uric Acid ◽  
Malpighian Tubules ◽  
Wild Type ◽  
Strong Reduction ◽  
Stages Of Development ◽  
Eye Color ◽  
Color Mutant

This paper is concerned with the different occurrence of tetrahydrobiopterin (THB) and riboflavine in the Malpighian tubules (MT) of the wild-type and of the eye color mutant brown (bw) of Drosophila melanogaster during different stages of development and life. In the MT of the mutant brown there is a strong reduction of THB and riboflavine contents in proportion to the amounts of the MT of the wild-type. Furthermore, in the mutant brown the THB, similar like isoxanthopterin and uric acid, disappears out of the MT soon after hatching. The results are discussed with regard to biogenetic coherences.

INTERACTION BETWEEN PTERIDINE SYNTHESIS AND RIBOFLAVIN ACCUMULATION IN DROSOPHILA MELANOGASTER

1972 ◽  
Vol 14 (1) ◽  
pp. 105-111 ◽  
Author(s):  
Harry Nickla
Keyword(s):  
Drosophila Melanogaster ◽  
Maternal Effect ◽  
Yellow Pigment ◽  
Wild Type ◽  
Cytoplasmic Factor ◽  
Eye Color ◽  
Spectrophotometric Methods ◽  
Eye Color Mutants ◽  
Per Se ◽  
Pigment Accumulation

Using chromatographic and spectrophotometric methods, riboflavin was determined to be the major component of yellow pigment in the Malpighian tubes of wild-type Drosophila melanogaster. While reduced yellow pigment accumulation in larvae of eye color mutants is consistently correlated with a reduction of drosopterin formation in adults, reduction of drosopterin synthesis is not always associated with decreased yellow pigment in Malpighian tubes.In the light mutant, reduced yellow pigment accumulation per se is not responsible for reduced drosopterin synthesis; however, a labile cytoplasmic factor associated with the light maternal effect does influence yellow pigment accumulation in Malpighian tubes.

scholarly journals Identification of cis-regulatory elements required for larval expression of the Drosophila melanogaster alcohol dehydrogenase gene.

Genetics ◽  
1990 ◽  
Vol 124 (3) ◽  
pp. 637-646 ◽  
Author(s):  
V Corbin ◽  
T Maniatis
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Dna Sequences ◽  
Regulatory Elements ◽  
Malpighian Tubules ◽  
Proximal Promoter ◽  
Start Site ◽  
Wild Type ◽  
Tissue Specific ◽  
Adh Gene

Abstract The Alcohol dehydrogenase (Adh) genes of two distantly related species, Drosophila melanogaster and Drosophila mulleri, display similar, but not identical, patterns of tissue-specific expression in larvae and adults. The regulatory DNA sequences necessary for wild-type Adh expression in D. mulleri larvae were previously reported. In this paper we present an analysis of the DNA sequences necessary for wild-type Adh expression in D. melanogaster larvae. We show that transcription from the proximal promoter of the melanogaster Adh gene is regulated by a far upstream enhancer and two or more elements near the transcription start site. The enhancer is tissue specific and stimulates transcription to high levels in fat body and to lower levels in midgut and malpighian tubules whether linked to the proximal promoter or to a heterologous promoter. The enhancer activity localized to at least two discrete regions dispersed over more than 1.7 kb of DNA. Deletion of any one of these subregions reduces Adh transcription in all three larval tissues. Similarly, two regions immediately upstream of the proximal promoter start site are necessary for wild-type transcription levels in all three tissues. Thus, each of the identified regulatory elements is sufficient for low levels of Adh gene expression in all three larval tissues, but maximal levels of expression requires the entire set.

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