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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...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1979
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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. |
format | Text |
id | pubmed-2110329 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1979 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |