DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans
Identifieur interne : 000625 ( Main/Corpus ); précédent : 000624; suivant : 000626DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans
Auteurs : Carsten Elke ; Peter Rauch ; Margarethe Spindler Arth ; Klaus Ieter SpindlerSource :
- Archives of Insect Biochemistry and Physiology [ 0739-4462 ] ; 2001-01.
English descriptors
- KwdEn :
Abstract
DNA‐binding features of EcR and USP were investigated using a 0.4 M NaCl extract of the epithelial cell line of Chironomus tentans by means of electrophoretic mobility shift assays (EMSAs). It is shown that the DNA‐binding is enhanced by hormone administration and that in the hormone dependent shift, both EcR and USP, are present. Furthermore, we demonstrate that under these conditions, EcR/USP form a unique complex on inverted repeat elements (PAL1 and hsp27‐EcRE), while on direct repeat elements (DR1‐5), a second complex with higher mobility is formed. In this second complex, neither EcR nor USP are present. Thus, an additional difference between PAL1 and DR‐elements is the competition of other factors for DR‐elements, modulating its function as an EcRE. A competition EMSA, using PAL1 as radiolabeled probe, reveals the following order of binding strength: PAL1>DR4/5>DR1>DR2/3/hsp27. Surprisingly, using DR1 as radiolabeled probe, shows a different order of binding strength: DR1>DR2>DR3/4/5/PAL1>hsp27. This indicates that the complexes formed on PAL1 are not identical to the ones formed on DR1 and that both are not easily convertible. Furthermore, the affinity of the EcR/USP complex may be altered under various conditions or by interaction with cofactors. Upon hormone administration, DNA binding of the receptor complex is enhanced, but the difference to hormone‐free binding reactions decreases in course of time, indicating an additional hormone independent activation. Arch. Insect Biochem. Physiol. 41:124–133, 1999. © 1999 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/arch.2
Links to Exploration step
ISTEX:79061D53B4953C161E3CF203E8F6359F49C1AE8BLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans</title><author><name sortKey="Elke, Carsten" sort="Elke, Carsten" uniqKey="Elke C" first="Carsten" last="Elke">Carsten Elke</name><affiliation><mods:affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</mods:affiliation></affiliation></author><author><name sortKey="Rauch, Peter" sort="Rauch, Peter" uniqKey="Rauch P" first="Peter" last="Rauch">Peter Rauch</name><affiliation><mods:affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</mods:affiliation></affiliation></author><author><name sortKey="Spindler Arth, Margarethe" sort="Spindler Arth, Margarethe" uniqKey="Spindler Arth M" first="Margarethe" last="Spindler Arth">Margarethe Spindler Arth</name><affiliation><mods:affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</mods:affiliation></affiliation></author><author><name sortKey="Spindler, Klaus Ieter" sort="Spindler, Klaus Ieter" uniqKey="Spindler K" first="Klaus Ieter" last="Spindler">Klaus Ieter Spindler</name><affiliation><mods:affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:79061D53B4953C161E3CF203E8F6359F49C1AE8B</idno><date when="2001" year="2001">2001</date><idno type="doi">10.1002/arch.2</idno><idno type="url">https://api.istex.fr/document/79061D53B4953C161E3CF203E8F6359F49C1AE8B/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000625</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans</title><author><name sortKey="Elke, Carsten" sort="Elke, Carsten" uniqKey="Elke C" first="Carsten" last="Elke">Carsten Elke</name><affiliation><mods:affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</mods:affiliation></affiliation></author><author><name sortKey="Rauch, Peter" sort="Rauch, Peter" uniqKey="Rauch P" first="Peter" last="Rauch">Peter Rauch</name><affiliation><mods:affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</mods:affiliation></affiliation></author><author><name sortKey="Spindler Arth, Margarethe" sort="Spindler Arth, Margarethe" uniqKey="Spindler Arth M" first="Margarethe" last="Spindler Arth">Margarethe Spindler Arth</name><affiliation><mods:affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</mods:affiliation></affiliation></author><author><name sortKey="Spindler, Klaus Ieter" sort="Spindler, Klaus Ieter" uniqKey="Spindler K" first="Klaus Ieter" last="Spindler">Klaus Ieter Spindler</name><affiliation><mods:affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Insect Biochemistry and Physiology</title><title level="j" type="sub">Published in Collaboration with the Entomological Society of America</title><title level="j" type="abbrev">Arch. Insect Biochem. Physiol.</title><idno type="ISSN">0739-4462</idno><idno type="eISSN">1520-6327</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-01">2001-01</date><biblScope unit="volume">46</biblScope><biblScope unit="issue">1‐2</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="10">10</biblScope></imprint><idno type="ISSN">0739-4462</idno></series><idno type="istex">79061D53B4953C161E3CF203E8F6359F49C1AE8B</idno><idno type="DOI">10.1002/arch.2</idno><idno type="ArticleID">ARCH2</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0739-4462</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chironomus tentans cell line</term><term>DNA‐binding</term><term>Drosophila Schneider line 2</term><term>ecdysteroid receptor</term><term>ultraspiracle</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">DNA‐binding features of EcR and USP were investigated using a 0.4 M NaCl extract of the epithelial cell line of Chironomus tentans by means of electrophoretic mobility shift assays (EMSAs). It is shown that the DNA‐binding is enhanced by hormone administration and that in the hormone dependent shift, both EcR and USP, are present. Furthermore, we demonstrate that under these conditions, EcR/USP form a unique complex on inverted repeat elements (PAL1 and hsp27‐EcRE), while on direct repeat elements (DR1‐5), a second complex with higher mobility is formed. In this second complex, neither EcR nor USP are present. Thus, an additional difference between PAL1 and DR‐elements is the competition of other factors for DR‐elements, modulating its function as an EcRE. A competition EMSA, using PAL1 as radiolabeled probe, reveals the following order of binding strength: PAL1>DR4/5>DR1>DR2/3/hsp27. Surprisingly, using DR1 as radiolabeled probe, shows a different order of binding strength: DR1>DR2>DR3/4/5/PAL1>hsp27. This indicates that the complexes formed on PAL1 are not identical to the ones formed on DR1 and that both are not easily convertible. Furthermore, the affinity of the EcR/USP complex may be altered under various conditions or by interaction with cofactors. Upon hormone administration, DNA binding of the receptor complex is enhanced, but the difference to hormone‐free binding reactions decreases in course of time, indicating an additional hormone independent activation. Arch. Insect Biochem. Physiol. 41:124–133, 1999. © 1999 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Carsten Elke</name><affiliations><json:string>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</json:string></affiliations></json:item><json:item><name>Peter Rauch</name><affiliations><json:string>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</json:string></affiliations></json:item><json:item><name>Margarethe Spindler‐Barth</name><affiliations><json:string>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</json:string></affiliations></json:item><json:item><name>Klaus‐Dieter Spindler</name><affiliations><json:string>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Chironomus tentans cell line</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Drosophila Schneider line 2</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>ecdysteroid receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>ultraspiracle</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DNA‐binding</value></json:item></subject><language><json:string>eng</json:string></language><abstract>DNA‐binding features of EcR and USP were investigated using a 0.4 M NaCl extract of the epithelial cell line of Chironomus tentans by means of electrophoretic mobility shift assays (EMSAs). It is shown that the DNA‐binding is enhanced by hormone administration and that in the hormone dependent shift, both EcR and USP, are present. Furthermore, we demonstrate that under these conditions, EcR/USP form a unique complex on inverted repeat elements (PAL1 and hsp27‐EcRE), while on direct repeat elements (DR1‐5), a second complex with higher mobility is formed. In this second complex, neither EcR nor USP are present. Thus, an additional difference between PAL1 and DR‐elements is the competition of other factors for DR‐elements, modulating its function as an EcRE. A competition EMSA, using PAL1 as radiolabeled probe, reveals the following order of binding strength: PAL1>DR4/5>DR1>DR2/3/hsp27. Surprisingly, using DR1 as radiolabeled probe, shows a different order of binding strength: DR1>DR2>DR3/4/5/PAL1>hsp27. This indicates that the complexes formed on PAL1 are not identical to the ones formed on DR1 and that both are not easily convertible. Furthermore, the affinity of the EcR/USP complex may be altered under various conditions or by interaction with cofactors. Upon hormone administration, DNA binding of the receptor complex is enhanced, but the difference to hormone‐free binding reactions decreases in course of time, indicating an additional hormone independent activation. Arch. Insect Biochem. Physiol. 41:124–133, 1999. © 1999 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>7.555</score><pdfVersion>1.2</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>5</keywordCount><abstractCharCount>1565</abstractCharCount><pdfWordCount>4795</pdfWordCount><pdfCharCount>30286</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>230</abstractWordCount></qualityIndicators><title>DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans</title><genre><json:string>article</json:string></genre><host><volume>46</volume><pages><total>10</total><last>10</last><first>1</first></pages><issn><json:string>0739-4462</json:string></issn><issue>1‐2</issue><subject><json:item><value>Research Article</value></json:item></subject><genre></genre><language><json:string>unknown</json:string></language><eissn><json:string>1520-6327</json:string></eissn><title>Archives of Insect Biochemistry and Physiology</title><doi><json:string>10.1002/(ISSN)1520-6327</json:string></doi></host><publicationDate>2001</publicationDate><copyrightDate>2001</copyrightDate><doi><json:string>10.1002/arch.2</json:string></doi><id>79061D53B4953C161E3CF203E8F6359F49C1AE8B</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/79061D53B4953C161E3CF203E8F6359F49C1AE8B/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/79061D53B4953C161E3CF203E8F6359F49C1AE8B/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/79061D53B4953C161E3CF203E8F6359F49C1AE8B/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><availability><p>WILEY</p></availability><date>2001</date></publicationStmt><notesStmt><note type="content">*This article originally published in Volume 41, Archives of Insect Biochemistry and Physiology 41:124–133 (1999)</note><note>University of Ulm</note><note>Deutsche Forschungsgemeinschaft - No. SFB351; No. Projekt A5;</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans</title><author><persName><forename type="first">Carsten</forename><surname>Elke</surname></persName><note type="correspondence"><p>Correspondence: Abteilung Allgemeine Zoologie und Endokrinologie (Biologie I), Albert‐Einstein‐Allee 11, D‐89081 Ulm, Germany</p></note><affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</affiliation></author><author><persName><forename type="first">Peter</forename><surname>Rauch</surname></persName><affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</affiliation></author><author><persName><forename type="first">Margarethe</forename><surname>Spindler‐Barth</surname></persName><affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</affiliation></author><author><persName><forename type="first">Klaus‐Dieter</forename><surname>Spindler</surname></persName><affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</affiliation></author></analytic><monogr><title level="j">Archives of Insect Biochemistry and Physiology</title><title level="j" type="sub">Published in Collaboration with the Entomological Society of America</title><title level="j" type="abbrev">Arch. Insect Biochem. Physiol.</title><idno type="pISSN">0739-4462</idno><idno type="eISSN">1520-6327</idno><idno type="DOI">10.1002/(ISSN)1520-6327</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="2001-01"></date><biblScope unit="volume">46</biblScope><biblScope unit="issue">1‐2</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="10">10</biblScope></imprint></monogr><idno type="istex">79061D53B4953C161E3CF203E8F6359F49C1AE8B</idno><idno type="DOI">10.1002/arch.2</idno><idno type="ArticleID">ARCH2</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2001</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>DNA‐binding features of EcR and USP were investigated using a 0.4 M NaCl extract of the epithelial cell line of Chironomus tentans by means of electrophoretic mobility shift assays (EMSAs). It is shown that the DNA‐binding is enhanced by hormone administration and that in the hormone dependent shift, both EcR and USP, are present. Furthermore, we demonstrate that under these conditions, EcR/USP form a unique complex on inverted repeat elements (PAL1 and hsp27‐EcRE), while on direct repeat elements (DR1‐5), a second complex with higher mobility is formed. In this second complex, neither EcR nor USP are present. Thus, an additional difference between PAL1 and DR‐elements is the competition of other factors for DR‐elements, modulating its function as an EcRE. A competition EMSA, using PAL1 as radiolabeled probe, reveals the following order of binding strength: PAL1>DR4/5>DR1>DR2/3/hsp27. Surprisingly, using DR1 as radiolabeled probe, shows a different order of binding strength: DR1>DR2>DR3/4/5/PAL1>hsp27. This indicates that the complexes formed on PAL1 are not identical to the ones formed on DR1 and that both are not easily convertible. Furthermore, the affinity of the EcR/USP complex may be altered under various conditions or by interaction with cofactors. Upon hormone administration, DNA binding of the receptor complex is enhanced, but the difference to hormone‐free binding reactions decreases in course of time, indicating an additional hormone independent activation. Arch. Insect Biochem. Physiol. 41:124–133, 1999. © 1999 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Chironomus tentans cell line</term></item><item><term>Drosophila Schneider line 2</term></item><item><term>ecdysteroid receptor</term></item><item><term>ultraspiracle</term></item><item><term>DNA‐binding</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Research Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1998-07-30">Received</change><change when="1999-01-27">Registration</change><change when="2001-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/79061D53B4953C161E3CF203E8F6359F49C1AE8B/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Inc.</publisherName><publisherLoc>New York</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1520-6327</doi><issn type="print">0739-4462</issn><issn type="electronic">1520-6327</issn><idGroup><id type="product" value="ARCH"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY">Archives of Insect Biochemistry and Physiology</title><title type="subtitle">Published in Collaboration with the Entomological Society of America</title><title type="short">Arch. Insect Biochem. Physiol.</title></titleGroup></publicationMeta><publicationMeta level="part" position="10"><doi origin="wiley" registered="yes">10.1002/arch.v46:1/2</doi><titleGroup><title type="specialIssueTitle">Advances in Cell Culture Research</title></titleGroup><numberingGroup><numbering type="journalVolume" number="46">46</numbering><numbering type="includedIssue">1</numbering><numbering type="includedIssue">2</numbering><numbering type="journalIssue">1‐2</numbering></numberingGroup><coverDate startDate="2001-01">January ‐ February 2001</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="2" status="forIssue"><doi origin="wiley" registered="yes">10.1002/arch.2</doi><idGroup><id type="unit" value="ARCH2"></id></idGroup><countGroup><count type="pageTotal" number="10"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title><title type="tocHeading1">Research Article</title></titleGroup><copyright ownership="publisher">Copyright © 2001 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="1998-07-30"></event><event type="manuscriptAccepted" date="1999-01-27"></event><event type="firstOnline" date="2001-04-03"></event><event type="publishedOnlineFinalForm" date="2001-04-03"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-09"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-06"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-15"></event></eventGroup><numberingGroup><numbering type="pageFirst">1</numbering><numbering type="pageLast">10</numbering></numberingGroup><correspondenceTo>Abteilung Allgemeine Zoologie und Endokrinologie (Biologie I), Albert‐Einstein‐Allee 11, D‐89081 Ulm, Germany</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:ARCH.ARCH2.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="49"></count><count type="wordTotal" number="5334"></count></countGroup><titleGroup><title type="main" xml:lang="en">DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from <i>Chironomus tentans</i> <link href="#fn1"></link></title><title type="short" xml:lang="en">DNA‐Binding Properties of EcR/USP</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Carsten</givenNames><familyName>Elke</familyName></personName><contactDetails><email normalForm="carsten.elke@biologie.uni-ulm.de">carsten.elke@biologie.uni‐ulm.de</email></contactDetails></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Peter</givenNames><familyName>Rauch</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Margarethe</givenNames><familyName>Spindler‐Barth</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Klaus‐Dieter</givenNames><familyName>Spindler</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="DE" type="organization"><unparsedAffiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="DE" type="organization"><unparsedAffiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1"><i>Chironomus tentans</i> cell line</keyword><keyword xml:id="kwd2"><i>Drosophila</i> Schneider line 2</keyword><keyword xml:id="kwd3">ecdysteroid receptor</keyword><keyword xml:id="kwd4">ultraspiracle</keyword><keyword xml:id="kwd5">DNA‐binding</keyword></keywordGroup><fundingInfo><fundingAgency>University of Ulm</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Deutsche Forschungsgemeinschaft</fundingAgency><fundingNumber>SFB351</fundingNumber><fundingNumber>Projekt A5</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>DNA‐binding features of EcR and USP were investigated using a 0.4 M NaCl extract of the epithelial cell line of <i>Chironomus tentans</i> by means of electrophoretic mobility shift assays (EMSAs). It is shown that the DNA‐binding is enhanced by hormone administration and that in the hormone dependent shift, both EcR and USP, are present. Furthermore, we demonstrate that under these conditions, EcR/USP form a unique complex on inverted repeat elements (PAL1 and hsp27‐EcRE), while on direct repeat elements (DR1‐5), a second complex with higher mobility is formed. In this second complex, neither EcR nor USP are present. Thus, an additional difference between PAL1 and DR‐elements is the competition of other factors for DR‐elements, modulating its function as an EcRE. A competition EMSA, using PAL1 as radiolabeled probe, reveals the following order of binding strength: PAL1>DR4/5>DR1>DR2/3/hsp27. Surprisingly, using DR1 as radiolabeled probe, shows a different order of binding strength: DR1>DR2>DR3/4/5/PAL1>hsp27. This indicates that the complexes formed on PAL1 are not identical to the ones formed on DR1 and that both are not easily convertible. Furthermore, the affinity of the EcR/USP complex may be altered under various conditions or by interaction with cofactors.</p><p>Upon hormone administration, DNA binding of the receptor complex is enhanced, but the difference to hormone‐free binding reactions decreases in course of time, indicating an additional hormone independent activation. Arch. Insect Biochem. Physiol. 41:124–133, 1999. © 1999 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>This article originally published in Volume 41, Archives of Insect Biochemistry and Physiology 41:124–133 (1999)</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>DNA‐Binding Properties of EcR/USP</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from</title></titleInfo><name type="personal"><namePart type="given">Carsten</namePart><namePart type="family">Elke</namePart><affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</affiliation><description>Correspondence: Abteilung Allgemeine Zoologie und Endokrinologie (Biologie I), Albert‐Einstein‐Allee 11, D‐89081 Ulm, Germany</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Peter</namePart><namePart type="family">Rauch</namePart><affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Margarethe</namePart><namePart type="family">Spindler‐Barth</namePart><affiliation>Lehrstuhl für Hormon‐ und Entwicklungsphysiologie, Heinrich‐Heine‐Universität, Düsseldorf, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Klaus‐Dieter</namePart><namePart type="family">Spindler</namePart><affiliation>Abteilung Allgemeine Zoologie und Endokrinologie, Universität Ulm, Ulm, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>John Wiley & Sons, Inc.</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2001-01</dateIssued><dateCaptured encoding="w3cdtf">1998-07-30</dateCaptured><dateValid encoding="w3cdtf">1999-01-27</dateValid><copyrightDate encoding="w3cdtf">2001</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">5</extent><extent unit="references">49</extent><extent unit="words">5334</extent></physicalDescription><abstract lang="en">DNA‐binding features of EcR and USP were investigated using a 0.4 M NaCl extract of the epithelial cell line of Chironomus tentans by means of electrophoretic mobility shift assays (EMSAs). It is shown that the DNA‐binding is enhanced by hormone administration and that in the hormone dependent shift, both EcR and USP, are present. Furthermore, we demonstrate that under these conditions, EcR/USP form a unique complex on inverted repeat elements (PAL1 and hsp27‐EcRE), while on direct repeat elements (DR1‐5), a second complex with higher mobility is formed. In this second complex, neither EcR nor USP are present. Thus, an additional difference between PAL1 and DR‐elements is the competition of other factors for DR‐elements, modulating its function as an EcRE. A competition EMSA, using PAL1 as radiolabeled probe, reveals the following order of binding strength: PAL1>DR4/5>DR1>DR2/3/hsp27. Surprisingly, using DR1 as radiolabeled probe, shows a different order of binding strength: DR1>DR2>DR3/4/5/PAL1>hsp27. This indicates that the complexes formed on PAL1 are not identical to the ones formed on DR1 and that both are not easily convertible. Furthermore, the affinity of the EcR/USP complex may be altered under various conditions or by interaction with cofactors. Upon hormone administration, DNA binding of the receptor complex is enhanced, but the difference to hormone‐free binding reactions decreases in course of time, indicating an additional hormone independent activation. Arch. Insect Biochem. Physiol. 41:124–133, 1999. © 1999 Wiley‐Liss, Inc.</abstract><note type="content">*This article originally published in Volume 41, Archives of Insect Biochemistry and Physiology 41:124–133 (1999)</note><note type="funding">University of Ulm</note><note type="funding">Deutsche Forschungsgemeinschaft - No. SFB351; No. Projekt A5; </note><subject lang="en"><genre>Keywords</genre><topic>Chironomus tentans cell line</topic><topic>Drosophila Schneider line 2</topic><topic>ecdysteroid receptor</topic><topic>ultraspiracle</topic><topic>DNA‐binding</topic></subject><relatedItem type="host"><titleInfo><title>Archives of Insect Biochemistry and Physiology</title><subTitle>Published in Collaboration with the Entomological Society of America</subTitle></titleInfo><titleInfo type="abbreviated"><title>Arch. Insect Biochem. Physiol.</title></titleInfo><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Research Article</topic></subject><identifier type="ISSN">0739-4462</identifier><identifier type="eISSN">1520-6327</identifier><identifier type="DOI">10.1002/(ISSN)1520-6327</identifier><identifier type="PublisherID">ARCH</identifier><part><date>2001</date><detail type="title"><title>Advances in Cell Culture Research</title></detail><detail type="volume"><caption>vol.</caption><number>46</number></detail><detail type="issue"><caption>no.</caption><number>1‐2</number></detail><extent unit="pages"><start>1</start><end>10</end><total>10</total></extent></part></relatedItem><identifier type="istex">79061D53B4953C161E3CF203E8F6359F49C1AE8B</identifier><identifier type="DOI">10.1002/arch.2</identifier><identifier type="ArticleID">ARCH2</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2001 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>John Wiley & Sons, Inc.</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Musique/explor/SchutzV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000625 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000625 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Musique
|area= SchutzV1
|flux= Main
|étape= Corpus
|type= RBID
|clé= ISTEX:79061D53B4953C161E3CF203E8F6359F49C1AE8B
|texte= DNA‐binding properties of the ecdysteroid receptor‐complex (EcR/USP) of the epithelial cell line from Chironomus tentans
}}
| This area was generated with Dilib version V0.6.38. |  |