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Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein
We identify a novel myosin-binding protein, designated 53K, which appears to mediate the low ionic strength solubility of myosin in extracts of unfertilized sea urchin eggs. The protein possesses a subunit molecular mass on SDS-PAGE of 53 kD, an S value of 7, may be organized into disulfide-linked o...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1987
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114777/ https://www.ncbi.nlm.nih.gov/pubmed/3624311 |
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collection | PubMed |
description | We identify a novel myosin-binding protein, designated 53K, which appears to mediate the low ionic strength solubility of myosin in extracts of unfertilized sea urchin eggs. The protein possesses a subunit molecular mass on SDS-PAGE of 53 kD, an S value of 7, may be organized into disulfide-linked oligomers, and is associated with myosin in egg extracts. Both myosin and 53K co-precipitate from extract upon the addition of nucleoside triphosphates and co-sediment with an S value of 24 by sedimentation velocity centrifugation. Myosin in extracts not associated with 53K has an S value of 10. Further, myosin can be immunoprecipitated from extract with antibody to 53K and the 53K in extracts binds to a myosin affinity column. When extract is depleted of 53K, a majority of the myosin precipitates out of extract in a nucleotide-independent manner. Whereas purified myosin precipitates in the absence of nucleotide when recombined with dialysis buffer or myosin-depleted extract, reconstituting 53K and myosin before addition to buffer or myosin-depleted extract partially restores the low ionic strength solubility demonstrated by myosin in fresh egg extracts. The 53-kD protein may represent a new class of authentic myosin-binding proteins that may regulate the supramolecular organization of myosin in nonmuscle cells. |
format | Text |
id | pubmed-2114777 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1987 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21147772008-05-01 Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein J Cell Biol Articles We identify a novel myosin-binding protein, designated 53K, which appears to mediate the low ionic strength solubility of myosin in extracts of unfertilized sea urchin eggs. The protein possesses a subunit molecular mass on SDS-PAGE of 53 kD, an S value of 7, may be organized into disulfide-linked oligomers, and is associated with myosin in egg extracts. Both myosin and 53K co-precipitate from extract upon the addition of nucleoside triphosphates and co-sediment with an S value of 24 by sedimentation velocity centrifugation. Myosin in extracts not associated with 53K has an S value of 10. Further, myosin can be immunoprecipitated from extract with antibody to 53K and the 53K in extracts binds to a myosin affinity column. When extract is depleted of 53K, a majority of the myosin precipitates out of extract in a nucleotide-independent manner. Whereas purified myosin precipitates in the absence of nucleotide when recombined with dialysis buffer or myosin-depleted extract, reconstituting 53K and myosin before addition to buffer or myosin-depleted extract partially restores the low ionic strength solubility demonstrated by myosin in fresh egg extracts. The 53-kD protein may represent a new class of authentic myosin-binding proteins that may regulate the supramolecular organization of myosin in nonmuscle cells. The Rockefeller University Press 1987-08-01 /pmc/articles/PMC2114777/ /pubmed/3624311 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 Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
title | Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
title_full | Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
title_fullStr | Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
title_full_unstemmed | Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
title_short | Low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
title_sort | low ionic strength solubility of myosin in sea urchin egg extracts is mediated by a myosin-binding protein |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114777/ https://www.ncbi.nlm.nih.gov/pubmed/3624311 |