Folding of influenza hemagglutinin in the endoplasmic reticulum
Identifieur interne : 000998 ( Pmc/Corpus ); précédent : 000997; suivant : 000999Folding of influenza hemagglutinin in the endoplasmic reticulum
Auteurs :Source :
- The Journal of Cell Biology [ 0021-9525 ] ; 1991.
Abstract
The folding of influenza hemagglutinin (HA0) in the ER was analyzed in tissue culture cells by following the formation of intrachain disulfides after short (1 min) radioactive pulses. While some disulfide bonds were already formed on the nascent chains, the subunits acquired their final disulfide composition and antigenic epitopes posttranslationally. Two posttranslational folding intermediates were identified. In CHO cells constitutively expressing HA0, mature HA0 subunits were formed with a half time of 3 min and their folding reached completion at 22 min. The rate of folding was highly dependent on cell type and expression system, and thus regulated by factors other than the sequence of the protein alone. Exposure of cells to stress conditions increased the level of glucose regulated proteins, including BiP, and decreased the folding rate. The efficiency of folding and subsequent trimerization was not dependent on the rate of translation, nor on temperature between 37 and 15 degrees C; however, the rates of folding and trimerization decreased with decreasing temperature. Whereas the rate of folding was independent of expression level, trimerization was accelerated at higher levels of expression.
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PubMed: 1650370
PubMed Central: 2289100
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PMC:2289100Le document en format XML
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<series><title level="j">The Journal of Cell Biology</title>
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<front><div type="abstract" xml:lang="en"><p>The folding of influenza hemagglutinin (HA0) in the ER was analyzed in tissue culture cells by following the formation of intrachain disulfides after short (1 min) radioactive pulses. While some disulfide bonds were already formed on the nascent chains, the subunits acquired their final disulfide composition and antigenic epitopes posttranslationally. Two posttranslational folding intermediates were identified. In CHO cells constitutively expressing HA0, mature HA0 subunits were formed with a half time of 3 min and their folding reached completion at 22 min. The rate of folding was highly dependent on cell type and expression system, and thus regulated by factors other than the sequence of the protein alone. Exposure of cells to stress conditions increased the level of glucose regulated proteins, including BiP, and decreased the folding rate. The efficiency of folding and subsequent trimerization was not dependent on the rate of translation, nor on temperature between 37 and 15 degrees C; however, the rates of folding and trimerization decreased with decreasing temperature. Whereas the rate of folding was independent of expression level, trimerization was accelerated at higher levels of expression.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">J Cell Biol</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Cell Biol</journal-id>
<journal-id journal-id-type="publisher-id">J. Cell Biol.</journal-id>
<journal-title-group><journal-title>The Journal of Cell Biology</journal-title>
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<issn pub-type="ppub">0021-9525</issn>
<issn pub-type="epub">1540-8140</issn>
<publisher><publisher-name>The Rockefeller University Press</publisher-name>
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<article-meta><article-id pub-id-type="pmid">1650370</article-id>
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<article-id pub-id-type="publisher-id">91317859</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Articles</subject>
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<title-group><article-title>Folding of influenza hemagglutinin in the endoplasmic reticulum</article-title>
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<pub-date pub-type="ppub"><day>1</day>
<month>8</month>
<year>1991</year>
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<volume>114</volume>
<issue>3</issue>
<fpage>401</fpage>
<lpage>411</lpage>
<permissions><license license-type="openaccess"><license-p>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 <ext-link ext-link-type="uri" xlink:href="http://www.rupress.org/terms">http://www.rupress.org/terms</ext-link>
). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc-sa/4.0/">http://creativecommons.org/licenses/by-nc-sa/4.0/</ext-link>
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<abstract><p>The folding of influenza hemagglutinin (HA0) in the ER was analyzed in tissue culture cells by following the formation of intrachain disulfides after short (1 min) radioactive pulses. While some disulfide bonds were already formed on the nascent chains, the subunits acquired their final disulfide composition and antigenic epitopes posttranslationally. Two posttranslational folding intermediates were identified. In CHO cells constitutively expressing HA0, mature HA0 subunits were formed with a half time of 3 min and their folding reached completion at 22 min. The rate of folding was highly dependent on cell type and expression system, and thus regulated by factors other than the sequence of the protein alone. Exposure of cells to stress conditions increased the level of glucose regulated proteins, including BiP, and decreased the folding rate. The efficiency of folding and subsequent trimerization was not dependent on the rate of translation, nor on temperature between 37 and 15 degrees C; however, the rates of folding and trimerization decreased with decreasing temperature. Whereas the rate of folding was independent of expression level, trimerization was accelerated at higher levels of expression.</p>
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