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Assemblages of multiple thick filaments in nematode mutants

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Summary

A spectrum of thick filament-related structures exhibiting novel structural features is isolated in addition to the normal thick filaments fromunc-15 andunc-82 mutants ofCaenorhabditis elegans. Many assemblages have multiple myosin-coated filaments extending from both ends of central domains exhibiting paracrystalline paramyosin. The filament ends resemble the polar core structures of native thick filaments. Assemblages with filaments at only one end and short thick filaments that branch are also present. This spectrum of novel structures accumulates at high levels in specific mutants due to alterations in paramyosin or other interacting proteins. The multifilament structures are either alternative assemblages of thick filament proteins and substructures or usually transient nucleation centres active in the assembly of thick filaments which are favoured under mutant conditions.

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Authors and Affiliations

  1. Department of Neurology, Baylor College of Medicine, 77030, Houston, Texas, USA

    Henry F. Epstein, Irving Ortiz & Gary C. Berliner

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  1. Henry F. Epstein
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  2. Irving Ortiz
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  3. Gary C. Berliner
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Epstein, H.F., Ortiz, I. & Berliner, G.C. Assemblages of multiple thick filaments in nematode mutants. J Muscle Res Cell Motil 8, 527–536 (1987). https://doi.org/10.1007/BF01567911

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  • DOI: https://doi.org/10.1007/BF01567911

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