Genetic analysis of vitellogenesis in Drosophila melanogaster: the identification of a temperature-sensitive mutation affecting one of the yolk proteins

Development ◽  
1978 ◽  
Vol 47 (1) ◽  
pp. 111-120
Author(s):  
M. Bownes ◽  
B. D. Hames
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Analysis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Temperature Sensitive ◽  
Large Reduction ◽  
Yolk Proteins ◽  
Protein Uptake ◽  
Temperature Sensitive Mutation ◽  
Transplant Experiments

A number of female sterile mutations on the first and third chromosomes of Drosophila melanogaster have been screened for defects in the yolk proteins using polyacrylamide gel electrophoresis. Two new mutants were identified. 6m45 accumulates all three yolk proteins (YP1, YP2 and YP3) in the haemolymph but they are all absent from the ovaries suggesting it is a yolk-protein-uptake mutant. In contrast, 1163 is a temperature-sensitive mutation with a large reduction in the quantity of YP1 in the haemolymph and ovaries at 29 °C. Both mutants are autonomous in ovary transplant experiments.

scholarly journals Variation of egg proteins between bird varieties by using SDS-PAGE

2019 ◽  
Vol 12 (1) ◽  
pp. 68-73
Author(s):  
Questan Amin ◽  
Hemn Zhahir ◽  
Ahmed Shaker
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Egg Yolk ◽  
Egg White ◽  
Yolk Proteins ◽  
Egg White Proteins ◽  
Sds Page

Proteins are essential constituents of all organisms; both egg white proteins and egg yolk are source of protein. The aim of this study was conducted to perform preliminary studies to analyses and compare egg white proteins and yolk proteins from different avian species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) via or with SDS-PAGE (Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis ). 18 Fresh eggs of different poultry species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) were collected from various farms in the Sulaimani province. Data on egg proteins were analyzed using Statistical Xlstate used for dendrogram construction and PCA. The main egg white proteins were Ovomicin, Ovotransferrin, Ovalbumin, Flavoprotein, α- chymotrypsinogen, and Trypsin inhibitor. The main lipoproteins were Apovitellenin VI, Apovitellenin Vb, Apovitellenin V, Apovitellenin IIIa, Apovitellenin III, Apovitellin 7, B-Livetin, Apovitellenin IIa, Apovitellenin II, and Apovitellenin I. All these lipoproteins were observed in the nine birds species. The egg white proteins and yolk lipoproteins for nine species were examined. It can be concluded the large differences were found in a mount of egg white proteins and yolk lipoproteins of the nine species of birds.

scholarly journals Reversible alteration in the neuromuscular junctions of Drosophila melanogaster bearing a temperature-sensitive mutation, shibire.

1979 ◽  
Vol 81 (3) ◽  
pp. 520-527 ◽  
Author(s):  
C A Poodry ◽  
L Edgar
Keyword(s):  
Drosophila Melanogaster ◽  
Temperature Change ◽  
Synaptic Vesicles ◽  
Neuromuscular Junctions ◽  
Prior Treatment ◽  
Temperature Sensitive ◽  
Large Numbers ◽  
Temperature Sensitive Mutation

In this study we report a relationship between the ultrastruct of the neuromuscular junctions of tibial muscles and the temperature-induced paralysis in shibire flies. There is a decrease in the number of synaptic vesicles of neuromuscular junctions in flies which are held at or above 29 degrees. Shortly after return to 22 degrees C, the synaptic vesicles are again present in large numbers. Prior treatment with tetrodotoxin or barbiturate protects the junctions from the temperature change in morphology.

Yolk proteins in salmon (Salmo salar) oocytes, eyed eggs, and alevins differing in viability

1990 ◽  
Vol 68 (5) ◽  
pp. 895-900 ◽  
Author(s):  
Thomas Olin ◽  
Alexandra von der Decken
Keyword(s):  
Molecular Weight ◽  
Salmo Salar ◽  
Gel Electrophoresis ◽  
Developmental Stages ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Antigen ◽  
Protein Composition ◽  
Polyacrylamide Gel ◽  
Parental Origin ◽  
Yolk Proteins

The developmental stages of oocytes, eyed eggs, and alevins from salmon (Salmo salar) were compared for their yolk protein composition. In oocytes, SDS–polyacrylamide gel electrophoresis showed high amounts of a protein with the molecular weight (Mr) of 94 000. In eyed eggs, the 94 000 protein decreased and was undetectable in the alevins. Furthermore, in eyed eggs the proteins of 67 000, 30 000, and 27 000 increased, while in the alevins the concentration of the 67 000 protein decreased and that of the 39 000 increased. Vitellogenin-specific antigen sites analyzed by immunoblotting were most pronounced with the proteins of 94 000, 67 000, 39 000, 30 000, 23 000, and 19 000. Separation of the yolk proteins by HPLC gave four peaks at 280 nm for all three developmental stages. Each peak consisted of several proteins as analyzed by SDS–polyacrylamide gel electrophoresis. The 7-day-old alevins sampled from groups of different parental origin showed differences in the amount of the 67 000 and 23 000 proteins. Expectancy of survival within the group in connection with a slow disappearance of the 67 000 and 23 000 proteins was statistically significant. A fast disappearance may be used as an indication of, but not as the reason for, a high mortality within one group of alevins.

Estimation of the Thermal Niche of Drosophila melanogaster Using a Temperature-Sensitive Mutation

1987 ◽  
Vol 130 (1) ◽  
pp. 83-90 ◽  
Author(s):  
J. S. Jones ◽  
Jerry A. Coyne ◽  
Linda Partridge
Keyword(s):  
Drosophila Melanogaster ◽  
Temperature Sensitive ◽  
Thermal Niche ◽  
Temperature Sensitive Mutation

scholarly journals VARIATION AND GENOMIC LOCALIZATION OF GENES ENCODING DROSOPHILA MELANOGASTER MALE ACCESSORY GLAND PROTEINS SEPARATED BY SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS

Genetics ◽  
1986 ◽  
Vol 114 (1) ◽  
pp. 77-92
Author(s):  
Michael Whalen ◽  
Thomas G Wilson
Keyword(s):  
Drosophila Melanogaster ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Accessory Gland ◽  
Polyacrylamide Gel ◽  
Null Alleles ◽  
Accessory Gland Proteins ◽  
Dodecyl Sulfate

ABSTRACT Accessory gland proteins from Drosophila melanogaster males have been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis into nine major bands. When individual males from 175 strains were examined, considerable polymorphism for nearly one-half of the major protein bands was seen, including null alleles for three bands. Variation was observed not only among long-established laboratory strains but also among stocks recently derived from natural populations. There was little difference in the amount of variation between P and M strains, indicating that P element mutagenesis is not a factor producing the variation. Codominant expression of variants for each of five bands was found in heterozygotes, suggesting structural gene variation and not posttranslational modification variation. Stocks carrying electrophoretic variants of four of the major proteins were used to map the presumed structural genes for these proteins; the loci were found to be dispersed on the second chromosome. Since males homozygous for variant proteins were fertile, the polymorphism seems to have little immediate effect on successful sperm transfer. We propose that a high degree of polymorphism can be tolerated because these proteins play a nutritive rather than enzymatic role in Drosophila reproduction.

Sexual development in a homothallic fission yeast: synthesis of readiness proteins resolved by gel electrophoresis

1982 ◽  
Vol 60 (6) ◽  
pp. 693-704 ◽  
Author(s):  
G. B. Calleja ◽  
Byron F. Johnson ◽  
Teena Walker
Keyword(s):  
Sexual Development ◽  
Gel Electrophoresis ◽  
Catabolite Repression ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Temperature Sensitive ◽  
Restrictive Temperature ◽  
Low Concentrations ◽  
Coomassie Brilliant ◽  
Temperature Aging

Sexual development of a homothallic strain of Schizosaccharomyces pombe was monitored by radiolabelling and sodium dodecyl sulfate (SDS) – polyacrylamide gel electrophoresis. Of more than 60 bands detected by Coomassie brilliant blue and by autoradiography, about 30 bands synthesized during development were discrete enough for experimental analysis.About a dozen bands are preferentially vegetative, another dozen preferentially developmental. However, vegetative bands as a group are also synthesized during development. Their synthesis is relatively unaffected by low concentrations of cycloheximide or by chloramphenicol and is not temperature sensitive at 37 °C nor catabolite repressible. Only band 40 (ca. 40 000 daltons) seems to be exclusively vegetative.The synthesis of developmental bands 13, 18, 24, 30, and α, all of which first appear during late-log phase, is catabolite repressible. Developmental band 51 is also synthesized throughout the vegetative phase. The synthesis of bands 24, 30, 51, and α is temperature sensitive at 37 °C during the development, but that of band 18 is not. The synthesis of band 13 during development is not temperature sensitive, but its earlier synthesis during late-log phase is. The synthesis of all these six developmental bands is immediately inhibited by cycloheximide, but not by chloramphenicol. Their appearance as a group of radioactive bands is greatly diminished in cultures grown in cycloheximide, in chloramphenicol, or in ethidium bromide.Developmental bands 13, 18, 24, and 30 may be called readiness proteins. They first appear prior to the earliest morphological signs of sexual activity. Their developmental synthesis is inhibited by conditions mat inhibit sexual development. Such inhibitory conditions include anaerobiosis, restrictive temperature, aging in stationary phase, the presence of inhibitors of cytoplasmic protein synthesis and of mitochondrial function, and catabolite repression. Readiness proteins may be regulating the switch from vegetative metabolism.

scholarly journals GENIC VARIATION IN ABUNDANT SOLUBLE PROTEINS OF DROSOPHILA MELANOGASTER AND DROSOPHILA PSEUDOOBSCURA

Genetics ◽  
1982 ◽  
Vol 102 (3) ◽  
pp. 437-453
Author(s):  
Rama S Singh ◽  
Michael B Coulthart
Keyword(s):  
Drosophila Melanogaster ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Soluble Proteins ◽  
One Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Genic Variation ◽  
Soluble Enzymes ◽  
Coomassie Brilliant ◽  
Dimensional Electrophoresis

ABSTRACT Genic variation was surveyed for 20 proteins of Drosophila melanogaster and 18 proteins of D. pseudoobscura. Analysis was by extraction and one-dimensional polyacrylamide gel electrophoresis under nondenaturing conditions, followed by staining with Coomassie Brilliant Blue to detect soluble proteins present in relatively large amounts ("abundant soluble proteins"). D. melanogaster was polymorphic for 65% of its protein loci and an individual was heterozygous for 10% of its loci. The respective figures for D. pseudoobscura were 61% and 11%. These estimates of genic variation fall between previously published estimates obtained for these species by one-dimensional electrophoresis of soluble enzymes and those obtained by two-dimensional electrophoresis of solubilized abundant proteins. However, variation for both species could be strongly partitioned between loci, on the basis of tissue and stage expression of the proteins. The results are discussed with respect to their bearing on the possibility that abundant proteins constitute a distinct class of proteins less polymorphic than soluble enzymes.

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