Literature DB >> 2091322

Orientation of the backbone structure of myosin filaments in relaxed and rigor muscles of the housefly: evidence for non-equivalent crossbridge positions at the surface of thick filaments.

G Beinbrech1, F T Ashton, F A Pepe.   

Abstract

The orientation of the backbone structure of myosin filaments of relaxed and rigor fibers of the flight muscles of the housefly, Musca domestica, relative to the actin filaments has been investigated. In relaxed muscles 23% of the myosin filaments have gaps in the wall of their shaft located opposite the surrounding actin filaments, while in 77% the subfilament pairs of the wall are thus located. These are the expected values if the backbone orientation is random. In rigor muscles 40% of the thick filaments have their gaps opposite the actins and 60%, the subfilament pairs are opposite the actins. This increase in the percentage of filaments with gaps opposite the actins therefore results from binding of the crossbridges in rigor with change in rotational orientation of the backbone. The findings are related to a model of Beinbrech et al. (1988) in which two populations of crossbridges have been postulated: one originating at the surface of the thick filaments, the other coming from within the gap between the subfilament pairs.

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Year:  1990        PMID: 2091322     DOI: 10.1016/0040-8166(90)90045-b

Source DB:  PubMed          Journal:  Tissue Cell        ISSN: 0040-8166            Impact factor:   2.466


  3 in total

Review 1.  Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.

Authors:  Scott L Hooper; Kevin H Hobbs; Jeffrey B Thuma
Journal:  Prog Neurobiol       Date:  2008-06-20       Impact factor: 11.685

2.  Oblique section 3-D reconstruction of relaxed insect flight muscle reveals the cross-bridge lattice in helical registration.

Authors:  H Schmitz; C Lucaveche; M K Reedy; K A Taylor
Journal:  Biophys J       Date:  1994-10       Impact factor: 4.033

3.  Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles.

Authors:  M C Reedy; B Bullard; J O Vigoreaux
Journal:  J Cell Biol       Date:  2000-12-25       Impact factor: 10.539

  3 in total

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