scholarly journals Fine structure of flight muscles in different Notch mutants of Drosophila melanogaster reared at different temperatures

1987 ◽  
Vol 196 (1) ◽  
pp. 12-15 ◽  
Author(s):  
Johanna Vilkki ◽  
Petter Portin
1992 ◽  
Vol 262 ◽  
Author(s):  
Klaus Pressel ◽  
G. Bohnert ◽  
A. Dörnen ◽  
K. Thonke

ABSTRACTThe 0.5 eV (2.5 μm 4000 cm1) emission band in InP has been studied by optical spectroscopy. By the use of Fourier-transform-infrared photoluminescence we have been able to observe at least a three-fold fine structure in the zero-phonon transitions at ∼ 4300 cm−1 which are studied at different temperatures. Based on the fine structure and the long decay time of 1.1 ms we ascribe the 0.5 eV emission to the 4T1 → 6A1 spin-flip transition of Fe3+. The excitation spectrum of this Fe3+-related emission shows a characteristic fine structure at ∼ 1.13 eV which belongs to a charge-transfer process of the type: Fe3+ + hv (1.13 eV) → [Fe2+, bound hole]. We discuss the excitation mechanism of the 0.5 eV emission by charge-transfer states and compare the results with an emission at 3057 cm1 in GaAs, which we attribute to the same Fe3+ transition (decay time: 1.9 ms).


1989 ◽  
Vol 109 (5) ◽  
pp. 2157-2167 ◽  
Author(s):  
J D Saide ◽  
S Chin-Bow ◽  
J Hogan-Sheldon ◽  
L Busquets-Turner ◽  
J O Vigoreaux ◽  
...  

Twelve monoclonal antibodies have been raised against proteins in preparations of Z-disks isolated from Drosophila melanogaster flight muscle. The monoclonal antibodies that recognized Z-band components were identified by immunofluorescence microscopy of flight muscle myofibrils. These antibodies have identified three Z-disk antigens on immunoblots of myofibrillar proteins. Monoclonal antibodies alpha:1-4 recognize a 90-100-kD protein which we identify as alpha-actinin on the basis of cross-reactivity with antibodies raised against honeybee and vertebrate alpha-actinins. Monoclonal antibodies P:1-4 bind to the high molecular mass protein, projectin, a component of connecting filaments that link the ends of thick filaments to the Z-band in insect asynchronous flight muscles. The anti-projectin antibodies also stain synchronous muscle, but, surprisingly, the epitopes here are within the A-bands, not between the A- and Z-bands, as in flight muscle. Monoclonal antibodies Z(210):1-4 recognize a 210-kD protein that has not been previously shown to be a Z-band structural component. A fourth antigen, resolved as a doublet (approximately 400/600 kD) on immunoblots of Drosophila fibrillar proteins, is detected by a cross reacting antibody, Z(400):2, raised against a protein in isolated honeybee Z-disks. On Lowicryl sections of asynchronous flight muscle, indirect immunogold staining has localized alpha-actinin and the 210-kD protein throughout the matrix of the Z-band, projectin between the Z- and A-bands, and the 400/600-kD components at the I-band/Z-band junction. Drosophila alpha-actinin, projectin, and the 400/600-kD components share some antigenic determinants with corresponding honeybee proteins, but no honeybee protein interacts with any of the Z(210) antibodies.


Author(s):  
I. I. Deak ◽  
A. Rähmi ◽  
P. R. Bellamy ◽  
M. Bienz ◽  
A. Blumer ◽  
...  

Genome ◽  
1999 ◽  
Vol 42 (3) ◽  
pp. 403-411 ◽  
Author(s):  
Kelly H Soanes ◽  
John B Bell

In 1931, Theodore Quelprud characterized a novel spontaneous mutation in Drosophila melanogaster, which was named aeroplane (ae) based on its abnormal wing posture. Although the characterization of the original ae locus was minimal, it is very likely that another allele of this extinct mutation has now been identified. aeroplane-like (ae-l) was isolated as a by-product of a transformation experiment. The apparent wing paralysis is not caused by any obvious abnormalities in the thorax, wing, indirect flight muscles or direct flight muscles. Classical genetic complementation analyses of ae-l with other genes in the region suggest that it represents an allele of a novel locus. Unexpectedly, a molecular examination revealed that the physical lesion identified in the ae-l mutant is exceptionally close to the homeotic gene teashirt (tsh) and, indeed, may represent an unusual allele of teashirt.Key words: aeroplane, teashirt, wing posture, Drosophila, flight.


Genetics ◽  
1964 ◽  
Vol 50 (6) ◽  
pp. 1245-1259 ◽  
Author(s):  
Arthur Chovnick ◽  
Abraham Schalet ◽  
R Peter Kernaghan ◽  
Marion Krauss

2020 ◽  
Vol 64 (1-2-3) ◽  
pp. 167-173
Author(s):  
Saroj Jawkar ◽  
Upendra Nongthomba

Myogenesis is a complex multifactorial process leading to the formation of the adult muscle. An amalgamation of autonomous processes including myoblast fusion and myofibrillogenesis, as well as non-autonomous processes, such as innervations from neurons and precise connections with attachment sites, are responsible for successful development and function of muscles. In this review, we describe the development of the indirect flight muscles (IFMs) in Drosophila melanogaster, and highlight the use of the IFMs as a model for studying muscle development and disease, based on recent studies on the development and function of IFMs.


Author(s):  
Shao-Yen Kao ◽  
Elena Nikonova ◽  
Keshika Ravichandran ◽  
Maria L. Spletter

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