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Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures
Proteins produced in cultured Drosophila cells during the heat-shock response (HSPs) were recently shown by autoradiography to be confined in large measure to the cell nucleus. We report here that nuclear HSPs are not associated with nucleosomes solubilizes by treatment with staphylococcal nuclease...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1981
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111893/ https://www.ncbi.nlm.nih.gov/pubmed/6793602 |
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collection | PubMed |
description | Proteins produced in cultured Drosophila cells during the heat-shock response (HSPs) were recently shown by autoradiography to be confined in large measure to the cell nucleus. We report here that nuclear HSPs are not associated with nucleosomes solubilizes by treatment with staphylococcal nuclease at low ionic strength nor are HSPs released by extraction with high salt, which solubilized most of the remaining histones and DNA. Possible functions of nuclear HSPs are discussed. |
format | Text |
id | pubmed-2111893 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1981 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21118932008-05-01 Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures J Cell Biol Articles Proteins produced in cultured Drosophila cells during the heat-shock response (HSPs) were recently shown by autoradiography to be confined in large measure to the cell nucleus. We report here that nuclear HSPs are not associated with nucleosomes solubilizes by treatment with staphylococcal nuclease at low ionic strength nor are HSPs released by extraction with high salt, which solubilized most of the remaining histones and DNA. Possible functions of nuclear HSPs are discussed. The Rockefeller University Press 1981-09-01 /pmc/articles/PMC2111893/ /pubmed/6793602 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 Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
title | Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
title_full | Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
title_fullStr | Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
title_full_unstemmed | Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
title_short | Heat-shock proteins of Drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
title_sort | heat-shock proteins of drosophila are associated with nuclease- resistant, high-salt-resistant nuclear structures |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111893/ https://www.ncbi.nlm.nih.gov/pubmed/6793602 |