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

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

Content Provider	Scilit
Author	Schwyter, D. H. Kron, Stephen Toyoshima, Y. Y. Spudich, J. A. Reisler, E.
Copyright Year	1990
Description	Journal: Journal of Cell Biology 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.
Related Links	http://jcb.rupress.org/content/jcb/111/2/465.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116201/pdf http://jcb.rupress.org/content/111/2/465.full.pdf
ISSN	00221295
DOI	10.1083/jcb.111.2.465
Journal	Journal of Cell Biology
Issue Number	2
Volume Number	111
Language	English
Publisher	Rockefeller University Press
Publisher Date	1990-08-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Cell Biology Biochemistry and Molecular Biology Actin Filaments Atpase Activity Intact Actin Cleaved Actin
Content Type	Text
Resource Type	Article
Subject	Physiology

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