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Nucleation of polar actin filament assembly by a positively charged surface

Polylysine-coated polystyrene beads can nucleate polar assembly of monomeric actin into filamentous form. This nucleation has been demonstrated by a combination of biochemical and structural experiments. The polylysine-coated beads accelerate the rate of actin assembly as detected by two different b...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1979
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110329/
https://www.ncbi.nlm.nih.gov/pubmed/572366
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collection PubMed
description Polylysine-coated polystyrene beads can nucleate polar assembly of monomeric actin into filamentous form. This nucleation has been demonstrated by a combination of biochemical and structural experiments. The polylysine-coated beads accelerate the rate of actin assembly as detected by two different biochemical assays. Subsequent examination of the beads by electron microscopy reveals numerous actin filaments of similar length radiating from the beads. ATP promotes this bead-induced acceleration of assembly. Decoration of the filaments with the myosin fragment S1 shows that these filaments all have the same polarity, with the arrowhead pattern pointing toward the bead. The relevance of the system to in vitro mechanisms and its usefulness in other studies are discussed.
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spelling pubmed-21103292008-05-01 Nucleation of polar actin filament assembly by a positively charged surface J Cell Biol Articles Polylysine-coated polystyrene beads can nucleate polar assembly of monomeric actin into filamentous form. This nucleation has been demonstrated by a combination of biochemical and structural experiments. The polylysine-coated beads accelerate the rate of actin assembly as detected by two different biochemical assays. Subsequent examination of the beads by electron microscopy reveals numerous actin filaments of similar length radiating from the beads. ATP promotes this bead-induced acceleration of assembly. Decoration of the filaments with the myosin fragment S1 shows that these filaments all have the same polarity, with the arrowhead pattern pointing toward the bead. The relevance of the system to in vitro mechanisms and its usefulness in other studies are discussed. The Rockefeller University Press 1979-02-01 /pmc/articles/PMC2110329/ /pubmed/572366 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
Nucleation of polar actin filament assembly by a positively charged surface
title Nucleation of polar actin filament assembly by a positively charged surface
title_full Nucleation of polar actin filament assembly by a positively charged surface
title_fullStr Nucleation of polar actin filament assembly by a positively charged surface
title_full_unstemmed Nucleation of polar actin filament assembly by a positively charged surface
title_short Nucleation of polar actin filament assembly by a positively charged surface
title_sort nucleation of polar actin filament assembly by a positively charged surface
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110329/
https://www.ncbi.nlm.nih.gov/pubmed/572366