Isolation and characterization of flightless mutants in Drosophila melanogaster

Development ◽  
1978 ◽  
Vol 45 (1) ◽  
pp. 123-143
Author(s):  
Takao Koana ◽  
Yoshiki Hotta
Keyword(s):  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Chromosomal Mapping ◽  
Indirect Flight Muscle ◽  
Mapping Technique ◽  
Isolation And Characterization ◽  
Genetic Mosaic ◽  
Column Type ◽  
Muscle Genes ◽  
Development And Differentiation

Since animal behaviour is executed through neuronal circuits including sensory receptors and muscle, genes vital for their development and differentiation must be found among mutants having behavioural anomaly. After mutagenesis with ethyl methanesulphonate (EMS), we screened for X-linked flightless mutants of Drosophila melanogaster by using a column-type flight tester. Approximately 104 individuals were screened and 21 mutant genes were isolated. Chromosomal mapping and complementation experiments revealed that they belong to 15 cistrons randomly located on X chromosome, three cistrons having more than two alleles. Two of the isolated mutants (AtO2 and AtH, which are recessive both behaviourally and morphologically) were analysed with the mosaic fate mapping technique, and both were found to have their primary foci in mesodermal region of blastoderm, suggesting that the genes exert their primary effect in indirect flight muscle. Electronmicroscopic studies on the muscles from four alleles of the AtO2 cistron revealed an abnormality in myofibrillar arrangement. A possible deficit within Z-band components is discussed in relation to wings-up B mutants. The indirect flight muscle of AltH was also examined, and it was found that sarcomere length and diameter of myofibrils were abnormal. It was postulated that a possible factor which controls size of myofibrils is defective in this mutant. These examples indicate the advantage of combining ultrastructural examination with genetic mosaic mapping technique.

Functional and ultrastructural effects of a missense mutation in the indirect flight muscle-specific actin gene of Drosophila melanogaster

1991 ◽  
Vol 222 (4) ◽  
pp. 963-982 ◽  
Author(s):  
John Sparrow ◽  
Mary Reedy ◽  
Elizabeth Ball ◽  
Vassilis Kyrtatas ◽  
Justin Molloy ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Missense Mutation ◽  
Flight Muscle ◽  
Indirect Flight Muscle ◽  
Actin Gene

scholarly journals Pseudo-acetylation of K326 and K328 of actin disrupts Drosophila melanogaster indirect flight muscle structure and performance

2015 ◽  
Vol 6 ◽  
Author(s):  
Meera C. Viswanathan ◽  
Anna C. Blice-Baum ◽  
William Schmidt ◽  
D. Brian Foster ◽  
Anthony Cammarato
Keyword(s):  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Indirect Flight Muscle ◽  
Muscle Structure ◽  
And Performance

scholarly journals Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster

2005 ◽  
Vol 102 (30) ◽  
pp. 10522-10527 ◽  
Author(s):  
H. Liu ◽  
M. S. Miller ◽  
D. M. Swank ◽  
W. A. Kronert ◽  
D. W. Maughan ◽  
...  
Keyword(s):  
Power Generation ◽  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Phosphorylation Site ◽  
Muscle Stiffness ◽  
Indirect Flight Muscle

scholarly journals OVERLAP OF THE BIREFRINGENT COMPONENT OF ADJACENT A REGIONS DURING THE INDUCED SHORTENING OF FIBRILS TEASED FROM DROSOPHILA MUSCLE

1963 ◽  
Vol 19 (1) ◽  
pp. 107-114 ◽  
Author(s):  
John Aronson
Keyword(s):  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Indirect Flight Muscle ◽  
Initial Length

Fibrils from the indirect flight muscle of Drosophila melanogaster which have been teased into a solution containing 0.1 M KCl, 2 mM EDTA, 4 mM MgCl2, and 2.5 mM ATP at pH 7.0 can be made to shorten to 10 per cent of their initial length by reducing the level of ATP at a pH of about 8 or by briefly treating the fibrils with trypsin before lowering the level of ATP. Fibrils shortened in either of these ways, when dehydrated and immersed in nitrobenzene, display a strong positively birefringent band at the level of the Z band. In the trypsin-treated fibrils the width of this Z band increases as the fibril shortens. The data obtained are in agreement with the view that the positively birefringent Z band results from the interdigitation of A filaments in adjacent sarcomeres. With shortening to about 35 per cent of the initial length, the cytological pattern suggests that the A filaments of alternate as well as of adjacent A regions interdigitate.

scholarly journals Transgenic expression and purification of myosin isoforms using the Drosophila melanogaster indirect flight muscle system

Methods ◽  
2012 ◽  
Vol 56 (1) ◽  
pp. 25-32 ◽  
Author(s):  
James T. Caldwell ◽  
Girish C. Melkani ◽  
Tom Huxford ◽  
Sanford I. Bernstein
Keyword(s):  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Indirect Flight Muscle ◽  
Myosin Isoforms ◽  
Expression And Purification ◽  
Muscle System ◽  
Transgenic Expression

Screen for new mutations on the 2nd chromosome involved in indirect flight muscle development in Drosophila melanogaster

Genome ◽  
2007 ◽  
Vol 50 (4) ◽  
pp. 343-350 ◽  
Author(s):  
Sajesh Babu ◽  
Nallur B. Ramachandra
Keyword(s):  
Drosophila Melanogaster ◽  
Muscle Development ◽  
Flight Muscle ◽  
Polarized Light ◽  
Indirect Flight Muscle ◽  
Recessive Mutations ◽  
Complete Penetrance ◽  
Recessive Genes ◽  
Complementation Groups ◽  
Mutant Lines

An extensive ethylmethanesulfonate mutagenesis of Drosophila melanogaster was undertaken to isolate the stronger alleles of 3 indirect flight-muscle mutations. We isolated 17 strong mutant lines, with nearly complete penetrance and expressivity, using direct screening under polarized light, from more than 1700 mutagenized chromosomes. On complementation, we found 11 of these 17 mutant lines to be alleles of 3 indirect flight-muscle mutations (Ifm(2)RU1, 3 noncomplementing lines; ifm(2)RU2, 6 alleles; ifm(2)RU3, 2 alleles) of the previously isolated 8 complementation groups (Ifm(2)RU1to ifm(2)RU8). In addition, we found 6 new complementation groups with strong defects in adult-muscle morphology; we named these ifm(2)RS1 to ifm(2)RS6. All mutant lines were mapped by meiotic recombination, and 5 of the 6 new complementation lines were mapped using chromosome deficiencies. ifm(2)RS1 maps to a region that harbors ifm(2)RU4 (a mutation that was isolated previously); however, theses are not alleles because each complements the other mutation, and the mutant-muscle phenotype is very different. We used direct screening under polarized light to find recessive mutations; although this method was labor intensive, it can be used to identify recessive genes involved in myogenesis, unlike screens for flightlessness or wing-position defects. This screen identifies regions on the second chromosome that harbor probable genes that are likely expressed in the mesoderm and are thought to be involved in myogenesis. This screen has generated valuable resources that will help us to understand the role of many molecular players involved in myogenesis.

scholarly journals The genetics of catalase in Drosophila melanogaster: isolation and characterization of acatalasemic mutants.

Genetics ◽  
1989 ◽  
Vol 122 (3) ◽  
pp. 643-652 ◽  
Author(s):  
W J Mackay ◽  
G C Bewley
Keyword(s):  
Drosophila Melanogaster ◽  
Free Radical ◽  
Catalase Activity ◽  
Oxygen Toxicity ◽  
Threshold Effect ◽  
Culture Conditions ◽  
Free Radical Damage ◽  
Isolation And Characterization ◽  
Standard Culture ◽  
Hypomorphic Alleles

Abstract Activated oxygen species have been demonstrated to be the important agents in oxygen toxicity by disrupting the structural and functional integrity of cells through lipid peroxidation events, DNA damage and protein inactivation. The biological consequences of free radical damage have long been hypothesized to be a causal agent in many aging-related diseases. Catalase (H2O2:H2O2 oxidoreductase; EC 1.15.1.1) is one of several enzymes involved in the scavenging of oxygen free radicals and free radical derivatives. The structural gene for catalase in Drosophila melanogaster has been localized to region 75D1-76A on chromosome 3L by dosage responses to segmental aneuploidy. This study reports the isolation of a stable deficiency, Df(3L)CatDH104(75C1-2;75F1), that uncovers the catalase locus and the subsequent isolation of six acatalasemic mutants. All catalase mutants are viable under standard culture conditions and recessive lethal mutations within the 75Cl-F1 interval have been shown not to affect catalase activity. Two catalase mutations are amorphic while four are hypomorphic alleles of the Cat+ locus. The lack of intergenic complementation between the six catalase mutations strongly suggests that there is only one functional gene in Drosophila. One acatalesemic mutation was mapped to position 3-47.0 which resides within the catalase dosage sensitive region. While complete loss of catalase activity confers a severe viability effect, residual levels are sufficient to restore viability to wild type levels. These results suggest a threshold effect for viability and offer an explanation for the general lack of phenotypic effects associated with the known mammalian acatalasemics.

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