scholarly journals An RNAi Screen for Genes Involved in Nanoscale Protrusion Formation on Corneal Lens in Drosophila melanogaster

2016 ◽  
Vol 33 (6) ◽  
pp. 583 ◽  
Author(s):  
Ryunosuke Minami ◽  
Chiaki Sato ◽  
Yumi Yamahama ◽  
Hideo Kubo ◽  
Takahiko Hariyama ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Rnai Screen ◽  
Corneal Lens

scholarly journals Identification of novel modulators of mitochondrial function by a genome-wide RNAi screen in Drosophila melanogaster

2007 ◽  
Vol 18 (1) ◽  
pp. 123-136 ◽  
Author(s):  
J. Chen ◽  
X. Shi ◽  
R. Padmanabhan ◽  
Q. Wang ◽  
Z. Wu ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Mitochondrial Function ◽  
Rnai Screen ◽  
Genome Wide ◽  
A Genome

Establishment of pattern in the developing compound eye of Drosophila

1991 ◽  
Vol 49 ◽  
pp. 318-319
Author(s):  
W. Bentham ◽  
C. Poodry
Keyword(s):  
Drosophila Melanogaster ◽  
Compound Eye ◽  
Stray Light ◽  
Pigment Cells ◽  
Hexagonal Array ◽  
Corneal Lens ◽  
Light Gathering

Each compound eye of the fruitfly, Drosophila melanogaster, is composed of about 800 individual light gathering and sensing units called ommatidia. The structure of the ommatidium is the product of some twenty four cells has a corneal lens to focus light, eight photoreceptors to sense the light, and a collar of pigment cells to absorb stray light. There are also mechanosensory bristles associated with ommatidia over much of the eye. The ommatidia are normally organized in a hexagonal array so perfectly placed that it has been called a neurocrystallin lattice. A number of mutations have been isolated that disturb the order or spacing of the ommatidia thereby resulting in a rough appearing eye. The focus of this study is to understand processes at work in establishing the precise pattern of ommatidial spacing.

Drosocrystallin, a major 52 kDa glycoprotein of the Drosophila melanogaster corneal lens. Purification, biochemical characterization, and subcellular localization

1992 ◽  
Vol 102 (2) ◽  
pp. 191-201 ◽  
Author(s):  
N. Komori ◽  
J. Usukura ◽  
H. Matsumoto
Keyword(s):  
Drosophila Melanogaster ◽  
Compound Eye ◽  
Biochemical Characterization ◽  
Immunogold Labelling ◽  
Dispersion Analysis ◽  
Major Protein ◽  
Dense Layer ◽  
Protein Distribution ◽  
Corneal Lens

We have identified a 52 kDa protein, which is a potent substrate for cholera toxin-dependent ADP-ribosylation, in the compound eye preparation of the fruit fly, Drosophila melanogaster. We find that the 52 kDa protein is a glycoprotein and a Ca2+ binder bearing a high content of leucine, serine and glycine. By microsequencing we determined its 13 N-terminal sequence, AYL*PIDLNQLAK, with the asterisk representing an ambiguous signal. In order to study further the 52 kDa protein we have raised a polyclonal antibody against a synthetic oligopeptide representing the N-terminal 13 residues of the 52 kDa protein. By immunogold labelling with the antibody, the epitopes were localized at the EM level to the laminated corneal lens. The number of the gold particles per microns2 in the electron-dense layer of the corneal lens was 2.5 times higher than that of the electron-lucent layer. The pattern of the 52 kDa protein distribution in the corneal lens suggests that the 52 kDa protein is the major protein component that participates in the pattern formation of the alternate refractive indices of the D. melanogaster corneal lens. An X-ray dispersion analysis in situ revealed that the laminated corneal lens contained a higher concentration of Ca2+, supporting the hypothesis that the 52 kDa protein binds Ca2+ in vivo. To the best of our knowledge, this is the first report that identifies the protein entity of an arthropod corneal lens. We propose to designate this 52 kDa protein drosocrystallin.

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

Live Confocal Analysis of Fertilization and Early Development

2001 ◽  
Vol 7 (S2) ◽  
pp. 1012-1013
Author(s):  
Uyen Tram ◽  
William Sullivan
Keyword(s):  
Drosophila Melanogaster ◽  
Embryonic Development ◽  
Real Time ◽  
Early Development ◽  
Fluorescent Probes ◽  
Primary Defect ◽  
Fluorescent Analysis ◽  
Dynamic Event ◽  
Enormous Amount ◽  
Fluorescent Studies

Embryonic development is a dynamic event and is best studied in live animals in real time. Much of our knowledge of the early events of embryogenesis, however, comes from immunofluourescent analysis of fixed embryos. While these studies provide an enormous amount of information about the organization of different structures during development, they can give only a static glimpse of a very dynamic event. More recently real-time fluorescent studies of living embryos have become much more routine and have given new insights to how different structures and organelles (chromosomes, centrosomes, cytoskeleton, etc.) are coordinately regulated. This is in large part due to the development of commercially available fluorescent probes, GFP technology, and newly developed sensitive fluorescent microscopes. For example, live confocal fluorescent analysis proved essential in determining the primary defect in mutations that disrupt early nuclear divisions in Drosophila melanogaster. For organisms in which GPF transgenics is not available, fluorescent probes that label DNA, microtubules, and actin are available for microinjection.

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