scholarly journals Mutations of Drosophila melanogaster that affect muscles

Development ◽  
1977 ◽  
Vol 40 (1) ◽  
pp. 35-63
Author(s):  
I. I. Deak
Keyword(s):  
Drosophila Melanogaster ◽  
Flight Muscle ◽  
Fat Body ◽  
Muscle Fibres ◽  
Muscle Structure ◽  
Site Of Action ◽  
Chromosome Mutations ◽  
Complementation Groups ◽  
Flight Muscles ◽  
Genetic Techniques

Eight X-chromosome mutations (falling into five complementation groups) that affect the development and morphology of the indirect flight muscles of Drosophila melanogaster were investigated using histological, behavioural and genetic techniques. All of these mutations result in Sightlessness, in a marked reduction in the ability of the flies to jump, and in the wings being held in abnormal positions. Mutations in each of the complementation groups have different effects on the morphology of the muscles. Two (flapwing, vertical wing) result in absence of most of the indirect flight muscle fibres, a third (upheld) is required for the gross organization of muscle structure, another (heldup) is involved in the maintenance of muscle structure once formed, and the fifth seems to be necessary for the detailed architecture of the muscle fibre (indented thorax). The analysis of flies genetically mosaic with respect to each mutation by the technique of fate-mapping suggests that three (heldup, upheld and indented thorax) of the genes concerned have their primary site of action in the musculature itself, while the other two(flapwing and vertical wing) may function primarily in the fat-body and tracheae respectively.

scholarly journals Characterization of components of Z-bands in the fibrillar flight muscle of Drosophila melanogaster.

1989 ◽  
Vol 109 (5) ◽  
pp. 2157-2167 ◽  
Author(s):  
J D Saide ◽  
S Chin-Bow ◽  
J Hogan-Sheldon ◽  
L Busquets-Turner ◽  
J O Vigoreaux ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Flight Muscle ◽  
Cross Reactivity ◽  
Antigenic Determinants ◽  
Immunogold Staining ◽  
Thick Filaments ◽  
The Matrix ◽  
Flight Muscles

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.

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

Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins

1987 ◽  
Vol 7 (9) ◽  
pp. 3084-3091
Author(s):  
C C Karlik ◽  
D L Saville ◽  
E A Fyrberg
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Flight Muscle ◽  
Structure And Function ◽  
Actin Gene ◽  
Wild Type ◽  
Diploid Complement ◽  
Flight Muscles ◽  
Shock Proteins ◽  
And Function

We have characterized two extant mutations of the flight muscle-specific act88F actin gene of Drosophila melanogaster. Both defective alleles were recovered from flightless mutants isolated previously (K. Mogami and Y. Hotta, Mol. Gen. Genet. 183:409-417, 1981). By directly sequencing the mutant alleles, we demonstrated that in act88FIfm(3)2 a single G-C to A-T transition converted arginine-28 to cysteine and that in act88FIfm(3)4 a single A-T to T-A transversion changed isoleucine-76 to phenylalanine. We showed that the actins encoded by either allele were strongly antimorphic. Mutant alleles effectively disrupted myofibril structure and function in the flight muscles of strains having the diploid complement of wild-type act88F genes. However, unlike antimorphic actins encoded by three previously characterized act88F alleles, neither that encoded by act88FIfm(3)2 nor that encoded by act88FIfm(3)4 was a strong inducer of heat shock protein synthesis.

Interspike interval relationship among flight muscle fibres in Drosophila

1980 ◽  
Vol 87 (1) ◽  
pp. 137-147 ◽  
Author(s):  
J. H. Koenig ◽  
K. Ikeda
Keyword(s):  
Interspike Interval ◽  
Flight Muscle ◽  
Motor Units ◽  
Muscle Fibres ◽  
Interspike Intervals ◽  
Neural Input ◽  
Flight Muscles ◽  
Bilateral Pair ◽  
Left And Right ◽  
Driving Source

Simultaneous intracellular recordings were made from the 10 motor units (12 fibres) comprising the bilateral pair of dorsal longitudinal flight muscles in Drosophila melanogaster while in stationary flight. The neural input which commonly drives these units was characterized by observing the influence which this input has on the interspike intervals of the various units. It was observed that the intervals of these units (both ipsilateral and contralateral), when considered collectively (that is, as a series of successively occurring intervals without regard for which unit represents which interval), fluctuate in a serially correlated manner. These interval fluctuations collectively define a fluctuation of complex waveform. The characteristics of this waveform suggest that two (or more) oscillating inputs are involved in commonly driving these units. In addition, a coupling in frequency and timing was observed between certain pairs of ipsilateral units, as well as between the units of one side relative to those of the other side. This coupling suggests that the neural pathway leading from the oscillating driving source might diverge, first to left and right sides, and then at a more peripheral level into three separate pathways, one leading to units 1 and 2, another to units 3 and 4, and a third to unit 5/6.

The Fibrillar Flight Muscles of Giant Water-Bugs: An Electron-Microscope Study

1967 ◽  
Vol 2 (3) ◽  
pp. 435-444
Author(s):  
DOREEN E. ASHHURST
Keyword(s):  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Flight Muscle ◽  
Muscle Fibres ◽  
Transverse Tubular System ◽  
Tropical Water ◽  
Tubular System ◽  
Flight Muscles ◽  
And Function ◽  
Water Bugs

The fibrillar flight muscles of several species of tropical water-bugs of the family Belostomatidae have been examined in the electron microscope. The myofibrils are very similar to those of the other fibrillar flight muscles which have been studied. The membrane systems, however, display features which appear to be peculiar to this family. The sarcoplasmic reticulum can be divided into three parts: a series of interconnecting vesicles surrounding the Z-lines, randomly scattered small vesicles around the myofibrils, and flattened cisternae which lie along the transverse tubular system, and form the dyads. These three components of the sarcoplasmic reticulum do not appear to be interconnected. The cisternae of the dyads contain an electrondense substance. The narrow tubules of the transverse tubular system or T-system penetrate deep into the fibre from the cell membrane. They follow a course roughly perpendicular to the myofibrils at the level of the M-lines. The dyads are scattered along their length, and may not be near a myofibril. Another system of very large vesicles is found in the muscle fibres, interspersed among the mitochondria. These vesicles usually appear to be empty; their nature and function are not at present known. Numerous mitochondria are present among the myofibrils. The peculiarities of the water-bug fibrillar flight muscle are discussed in relation to the flight muscles of other insects and the physiological properties of fibrillar flight muscle.

scholarly journals Recovery of dominant, autosomal flightless mutants of Drosophila melanogaster and identification of a new gene required for normal muscle structure and function.

Genetics ◽  
1994 ◽  
Vol 137 (1) ◽  
pp. 151-164 ◽  
Author(s):  
R M Cripps ◽  
E Ball ◽  
M Stark ◽  
A Lawn ◽  
J C Sparrow
Keyword(s):  
Drosophila Melanogaster ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Chain Gene ◽  
Normal Muscle ◽  
Muscle Structure ◽  
New Gene ◽  
Flight Muscles ◽  
And Function ◽  
Muscle Myosin

Abstract To identify further mutations affecting muscle function and development in Drosophila melanogaster we recovered 22 autosomal dominant flightless mutations. From these we have isolated eight viable and lethal alleles of the muscle myosin heavy chain gene, and seven viable alleles of the indirect flight muscle (IFM)-specific Act88F actin gene. The Mhc mutations display a variety of phenotypic effects, ranging from reductions in myosin heavy chain content in the indirect flight muscles only, to reductions in the levels of this protein in other muscles. The Act88F mutations range from those which produce no stable actin and have severely abnormal myofibrillar structure, to those which accumulate apparently normal levels of actin in the flight muscles but which still have abnormal myofibrils and fly very poorly. We also recovered two recessive flightless mutants on the third chromosome. The remaining five dominant flightless mutations are all lethal alleles of a gene named lethal(3)Laker. The Laker alleles have been characterized and the gene located in polytene bands 62A10,B1-62B2,4. Laker is a previously unidentified locus which is haplo-insufficient for flight. In addition, adult wild-type heterozygotes and the lethal larval trans-heterozygotes show abnormalities of muscle structure indicating that the Laker gene product is an important component of muscle.

scholarly journals CryoEM Structure of Drosophila Flight Muscle Thick Filaments at 7Å Resolution

2020 ◽  
Author(s):  
Nadia Daneshparvar ◽  
Dianne W. Taylor ◽  
Thomas S. O’Leary ◽  
Hamidreza Rahmani ◽  
Fatemeh Abbasi Yeganeh ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Striated Muscle ◽  
Flight Muscle ◽  
Coiled Coil ◽  
Thick Filament ◽  
Fruit Fly ◽  
Actin Binding ◽  
Thick Filaments ◽  
Flight Muscles ◽  
Lethocerus Indicus

AbstractStriated muscle thick filaments are composed of myosin II and several non-myosin proteins. Myosin II’s long α-helical coiled-coil tail forms the dense protein backbone of filaments while its N-terminal globular head containing the catalytic and actin binding activities extends outward from the backbone. Here we report the structure of thick filaments of the flight muscle of the fruit fly Drosophila melanogaster at 7 Å resolution. Its myosin tails are arranged in curved molecular crystalline layers identical to flight muscles of the giant waterbug Lethocerus indicus. Four non-myosin densities are observed, three of which correspond to ones found in Lethocerus; one new density, possibly stretchin-Mlck, is found on the backbone outer surface. Surprisingly, the myosin heads are disordered rather than ordered along the filament backbone. Our results show striking myosin tail similarity within flight muscle filaments of two insect orders separated by several hundred million years of evolution.Significance StatementMyosin thick filaments are one of striated muscle’s key structures, but also one of its least understood. A key question is how the myosin a-helical coiled-coil tail is arranged in the backbone. At 7Å resolution, sufficient to resolve individual a-helices, the myosin tail arrangement in thick filaments from the flight muscle of the fruit fly Drosophila melanogaster is strikingly similar to the myosin tail arrangement in flight muscles of the giant waterbug Lethocerus indicus. Nearly every other thick filament feature is different. Drosophila and Lethocerus evolved separately >245 million years ago suggesting myosin tail packing into curved molecular crystalline layers forms a highly conserved thick filament building block and different properties are obtained by alterations in non-myosin proteins.

scholarly journals Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins.

1987 ◽  
Vol 7 (9) ◽  
pp. 3084-3091 ◽  
Author(s):  
C C Karlik ◽  
D L Saville ◽  
E A Fyrberg
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Flight Muscle ◽  
Structure And Function ◽  
Actin Gene ◽  
Wild Type ◽  
Diploid Complement ◽  
Flight Muscles ◽  
Shock Proteins ◽  
And Function

We have characterized two extant mutations of the flight muscle-specific act88F actin gene of Drosophila melanogaster. Both defective alleles were recovered from flightless mutants isolated previously (K. Mogami and Y. Hotta, Mol. Gen. Genet. 183:409-417, 1981). By directly sequencing the mutant alleles, we demonstrated that in act88FIfm(3)2 a single G-C to A-T transition converted arginine-28 to cysteine and that in act88FIfm(3)4 a single A-T to T-A transversion changed isoleucine-76 to phenylalanine. We showed that the actins encoded by either allele were strongly antimorphic. Mutant alleles effectively disrupted myofibril structure and function in the flight muscles of strains having the diploid complement of wild-type act88F genes. However, unlike antimorphic actins encoded by three previously characterized act88F alleles, neither that encoded by act88FIfm(3)2 nor that encoded by act88FIfm(3)4 was a strong inducer of heat shock protein synthesis.

The Physiology of Blood Trehalose and its Function During Flight in the Blowfly

1961 ◽  
Vol 38 (4) ◽  
pp. 771-792 ◽  
Author(s):  
JAMES S. CLEGG ◽  
DAVID R. EVANS
Keyword(s):  
Blood Volume ◽  
Flight Muscle ◽  
Fat Body ◽  
Normal Blood ◽  
Phormia Regina ◽  
Rate Processes ◽  
Flight Muscles ◽  
Trehalose Synthesis ◽  
Lines Of Evidence ◽  
Exogenous Substrates

1. The finding (Evans & Dethier, 1957) that glucose and trehalose are the normal blood sugars of the blowfly Phormia regina has been confirmed. 2. It is estimated that most of the flight energy is derived from the oxidation of trehalose and, to a lesser extent, of other sugars found in the blood. 3. Several lines of evidence indicate that the concentration of blood trehalose normally regulates the rate at which energy is expended by the flight muscles during flight. ‘Exhaustion’ results when trehalose cannot be supplied to the flight muscle at the necessary rate. 4. Fat body is the chief source of blood trehalose; endogenous and exogenous substrates are used for its synthesis. The rate of blood trehalose synthesis can be very rapid, almost compensating for the rate of utilization by the flight muscle during flight. 5. It appears, therefore, that the intensity of flight is determined largely by the interaction of two rate processes: the rate of trehalose utilization (flight muscles) and the rate of trehalose synthesis (fat body). 6. A diagram is presented which accounts for the establishment of glucose and trehalose as the normal blood sugars of this fly and summarizes our findings on the transfer of carbohydrates between various tissues. 7. The blood volume (6-7 µl.) has been estimated from dilution of injected 14C-inulin. This volume is not changed appreciably by flight.

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