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Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin

Subtilisin cleaved actin was shown to retain several properties of intact actin including the binding of heavy meromyosin (HMM), the dissociation from HMM by ATP, and the activation of HMM ATPase activity. Similar Vmax but different Km values were obtained for acto- HMM ATPase with the cleaved and i...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1990
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116201/
https://www.ncbi.nlm.nih.gov/pubmed/2143196
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description Subtilisin cleaved actin was shown to retain several properties of intact actin including the binding of heavy meromyosin (HMM), the dissociation from HMM by ATP, and the activation of HMM ATPase activity. Similar Vmax but different Km values were obtained for acto- HMM ATPase with the cleaved and intact actins. The ATPase activity of HMM stimulated by copolymers of intact and cleaved actin showed a linear dependence on the fraction of intact actin in the copolymer. The most important difference between the intact and cleaved actin was observed in an in vitro motility assay for actin sliding movement over an HMM coated surface. Only 30% of the cleaved actin filaments appeared mobile in this assay and moreover, the velocity of the mobile filaments was approximately 30% that of intact actin filaments. These results suggest that the motility of actin filaments can be uncoupled from the activation of myosin ATPase activity and is dependent on the structural integrity of actin and perhaps, dynamic changes in the actin molecule.
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spelling pubmed-21162012008-05-01 Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin J Cell Biol Articles Subtilisin cleaved actin was shown to retain several properties of intact actin including the binding of heavy meromyosin (HMM), the dissociation from HMM by ATP, and the activation of HMM ATPase activity. Similar Vmax but different Km values were obtained for acto- HMM ATPase with the cleaved and intact actins. The ATPase activity of HMM stimulated by copolymers of intact and cleaved actin showed a linear dependence on the fraction of intact actin in the copolymer. The most important difference between the intact and cleaved actin was observed in an in vitro motility assay for actin sliding movement over an HMM coated surface. Only 30% of the cleaved actin filaments appeared mobile in this assay and moreover, the velocity of the mobile filaments was approximately 30% that of intact actin filaments. These results suggest that the motility of actin filaments can be uncoupled from the activation of myosin ATPase activity and is dependent on the structural integrity of actin and perhaps, dynamic changes in the actin molecule. The Rockefeller University Press 1990-08-01 /pmc/articles/PMC2116201/ /pubmed/2143196 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
Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
title Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
title_full Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
title_fullStr Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
title_full_unstemmed Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
title_short Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
title_sort subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116201/
https://www.ncbi.nlm.nih.gov/pubmed/2143196