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Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin

The thick filaments of the nematode Caenorhabditis elegans contain two myosin heavy chain isoforms A and B and paramyosin, the products of the myo-3, unc-54, and unc-15 genes, respectively. Dissociation of paramyosin from native thick filaments at pH 6.36 shows a biphasic function with respect to Na...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1993
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119837/
https://www.ncbi.nlm.nih.gov/pubmed/8408214
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collection PubMed
description The thick filaments of the nematode Caenorhabditis elegans contain two myosin heavy chain isoforms A and B and paramyosin, the products of the myo-3, unc-54, and unc-15 genes, respectively. Dissociation of paramyosin from native thick filaments at pH 6.36 shows a biphasic function with respect to NaCl concentration. Electron microscopy of the remaining structures shows 15-nm core structures that label with monoclonal anti-paramyosin antibody at 72.5-nm intervals. Purified core structures also show 72.5 nm repeats by negative staining. Structural analysis of native thick filaments and dissociated structures suggests that the more dissociable paramyosin is removed radially as well as processively from the filament ends. Minor proteins with masses of 20, 28, and 30 kD cosediment stoichiometrically with paramyosin in purified core structures.
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spelling pubmed-21198372008-05-01 Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin J Cell Biol Articles The thick filaments of the nematode Caenorhabditis elegans contain two myosin heavy chain isoforms A and B and paramyosin, the products of the myo-3, unc-54, and unc-15 genes, respectively. Dissociation of paramyosin from native thick filaments at pH 6.36 shows a biphasic function with respect to NaCl concentration. Electron microscopy of the remaining structures shows 15-nm core structures that label with monoclonal anti-paramyosin antibody at 72.5-nm intervals. Purified core structures also show 72.5 nm repeats by negative staining. Structural analysis of native thick filaments and dissociated structures suggests that the more dissociable paramyosin is removed radially as well as processively from the filament ends. Minor proteins with masses of 20, 28, and 30 kD cosediment stoichiometrically with paramyosin in purified core structures. The Rockefeller University Press 1993-10-02 /pmc/articles/PMC2119837/ /pubmed/8408214 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin
title Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin
title_full Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin
title_fullStr Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin
title_full_unstemmed Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin
title_short Thick filament substructures in Caenorhabditis elegans: evidence for two populations of paramyosin
title_sort thick filament substructures in caenorhabditis elegans: evidence for two populations of paramyosin
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119837/
https://www.ncbi.nlm.nih.gov/pubmed/8408214