Genetic and molecular analyses of Drosophila contractile protein genes

Fyrberg, Eric

doi:10.1002/bies.950020604

Cited by 4 publications

(3 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Exons 5, 6 and 7 have internal splice sites and isoforms contain long or short versions of these exons. The Drosophila myofilin gene maps to chromosome position 3R 88E2, which is close to several genes expressed specifically in IFM (Karlik et al, 1984;Fyrberg, 1985;Bernstein et al, 1993). This suggests that there may be some coordination in the regulation of the expression of these genes (Spellman and Rubin, 2002).…”

Section: Sequence Of Lethocerus and Drosophila Myofilinmentioning

confidence: 97%

Myofilin, a protein in the thick filaments of insect muscle

Qiu

Brendel

Cunha

et al. 2005

Journal of Cell Science

View full text Add to dashboard Cite

Thick filaments in striated muscle are myosin polymers with a length and diameter that depend on the fibre type. In invertebrates, the length of the thick filaments varies widely in different muscles and additional proteins control filament assembly. Thick filaments in asynchronous insect flight muscle have an extremely regular structure, which is likely to be essential for the oscillatory contraction of these muscles. The factors controlling the assembly of thick filaments in insect flight muscle are not known. We previously identified a thick filament core protein, zeelin 1, in Lethocerus flight and non-flight muscles. This has been sequenced, and the corresponding proteins in Drosophila and Anopheles have been identified. The protein has been re-named myofilin. Zeelin 2, which is on the outside of Lethocerus flight muscle thick filaments, has been sequenced and because of the similarity to Drosophila flightin, is re-named flightin. In Drosophila flight muscle, myofilin has a molecular weight of 20 kDa and is one of five isoforms produced from a single gene. In situ hybridisation of Drosophila embryos showed that myofilin RNA is first expressed late in embryogenesis at stage 15, a little later than myosin. Antibody to myofilin labelled the entire A-band, except for the H-zone, in cryosections of flight and non-flight muscle. The periodicity of myofilin in Drosophila flight muscle thick filaments was found to be 30 nm by measuring the spacing of gold particles in labelled cryosections; this is about twice the 14.5 nm spacing of myosin molecules. The molar ratio of myofilin to myosin in indirect flight muscle is 1:2, which is the same as that of flightin. We propose a model for the association of these proteins in thick filaments, which is consistent with the periodicity and stoichiometry. Myofilin is probably needed for filament assembly in all muscles, and flightin for stability of flight muscle thick filaments in adult flies.

show abstract

Section: Sequence Of Lethocerus and Drosophila Myofilinmentioning

confidence: 97%

Myofilin, a protein in the thick filaments of insect muscle

Qiu

Brendel

Cunha

et al. 2005

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…For a variety of reasons discussed in previous reports, Drosophila indirect flight muscles lend themselves especially well to this endeavor (5,14). Furthermore, a suitable tropomyosin null allele has already been demonstrated in the flightless Drosophila Ifm(3)3 mutant (10).…”

Section: Ltr Ecori Hindmmentioning

confidence: 89%

Genetic rescue of muscle defects associated with a mutant Drosophila melanogaster tropomyosin allele.

Fyrberg¹,

Karlik²

1987

Mol. Cell. Biol.

View full text Add to dashboard Cite

We describe a genetic transformation system which should prove useful for investigating tropomyosin assembly and function. Muscle abnormalities associated with a defective tropomyosin allele were corrected by integrating the wild-type gene into germ line chromosomes. The transformation protocol permits application of directed mutagenesis techniques in investigations of contractile regulatory mechanisms.

show abstract

“…One calcium-binding troponin complex LTR EcoRI HindM Sal I Hind m I recipients having null mutations in their "resident" tropomyosin gene copies. For a variety of reasons discussed in previous reports, Drosophila indirect flight muscles lend themselves especially well to this endeavor (5,14). Furthermore, a suitable tropomyosin null allele has already been demonstrated in the flightless Drosophila Ifm(3)3 mutant (10).…”

mentioning

confidence: 89%