Differential nuclear receptor signalling from DR4‐type response elements
Identifieur interne : 000B43 ( Main/Corpus ); précédent : 000B42; suivant : 000B44Differential nuclear receptor signalling from DR4‐type response elements
Auteurs : Marcus Quack ; Christian Frank ; Carsten CarlbergSource :
- Journal of Cellular Biochemistry [ 0730-2312 ] ; 2002.
English descriptors
- KwdEn :
Abstract
Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jcb.10247
Links to Exploration step
ISTEX:01C9C305B207DC8E1C9741284A6DAA2F01DC3A74Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Differential nuclear receptor signalling from DR4‐type response elements</title><author><name sortKey="Quack, Marcus" sort="Quack, Marcus" uniqKey="Quack M" first="Marcus" last="Quack">Marcus Quack</name><affiliation><mods:affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>Current Address: Raytest Isotopenmessgeräte GmbH, Sirrenbergstr. 9, D‐45549 Sprockhövel, Germany.</mods:affiliation></affiliation></author><author><name sortKey="Frank, Christian" sort="Frank, Christian" uniqKey="Frank C" first="Christian" last="Frank">Christian Frank</name><affiliation><mods:affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</mods:affiliation></affiliation></author><author><name sortKey="Carlberg, Carsten" sort="Carlberg, Carsten" uniqKey="Carlberg C" first="Carsten" last="Carlberg">Carsten Carlberg</name><affiliation><mods:affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:01C9C305B207DC8E1C9741284A6DAA2F01DC3A74</idno><date when="2002" year="2002">2002</date><idno type="doi">10.1002/jcb.10247</idno><idno type="url">https://api.istex.fr/document/01C9C305B207DC8E1C9741284A6DAA2F01DC3A74/fulltext/pdf</idno><idno type="wicri:Area/Main/Corpus">000B43</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Differential nuclear receptor signalling from DR4‐type response elements</title><author><name sortKey="Quack, Marcus" sort="Quack, Marcus" uniqKey="Quack M" first="Marcus" last="Quack">Marcus Quack</name><affiliation><mods:affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>Current Address: Raytest Isotopenmessgeräte GmbH, Sirrenbergstr. 9, D‐45549 Sprockhövel, Germany.</mods:affiliation></affiliation></author><author><name sortKey="Frank, Christian" sort="Frank, Christian" uniqKey="Frank C" first="Christian" last="Frank">Christian Frank</name><affiliation><mods:affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</mods:affiliation></affiliation></author><author><name sortKey="Carlberg, Carsten" sort="Carlberg, Carsten" uniqKey="Carlberg C" first="Carsten" last="Carlberg">Carsten Carlberg</name><affiliation><mods:affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Cellular Biochemistry</title><title level="j" type="abbrev">J. Cell. Biochem.</title><idno type="ISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="2002">2002</date><biblScope unit="volume">86</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="601">601</biblScope><biblScope unit="page" to="612">612</biblScope></imprint><idno type="ISSN">0730-2312</idno></series><idno type="istex">01C9C305B207DC8E1C9741284A6DAA2F01DC3A74</idno><idno type="DOI">10.1002/jcb.10247</idno><idno type="ArticleID">JCB10247</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0730-2312</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>complexes</term><term>heterodimeric nuclear receptor</term><term>liver X receptor</term><term>response elements</term><term>retinoid X receptor</term><term>thyroid hormone receptor</term><term>transcriptional regulation</term><term>vitamin D receptor</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Marcus Quack</name><affiliations><json:string>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</json:string><json:string>Current Address: Raytest Isotopenmessgeräte GmbH, Sirrenbergstr. 9, D‐45549 Sprockhövel, Germany.</json:string></affiliations></json:item><json:item><name>Christian Frank</name><affiliations><json:string>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</json:string></affiliations></json:item><json:item><name>Carsten Carlberg</name><affiliations><json:string>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</json:string><json:string>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>transcriptional regulation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>vitamin D receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>thyroid hormone receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>liver X receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>retinoid X receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>heterodimeric nuclear receptor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>complexes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>response elements</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>8</score><pdfVersion>1.3</pdfVersion><pdfPageSize>592 x 789 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>8</keywordCount><abstractCharCount>1706</abstractCharCount><pdfWordCount>5499</pdfWordCount><pdfCharCount>34224</pdfCharCount><pdfPageCount>12</pdfPageCount><abstractWordCount>270</abstractWordCount></qualityIndicators><title>Differential nuclear receptor signalling from DR4‐type response elements</title><genre><json:string>article</json:string></genre><host><volume>86</volume><pages><total>12</total><last>612</last><first>601</first></pages><issn><json:string>0730-2312</json:string></issn><issue>3</issue><subject><json:item><value>Article</value></json:item></subject><genre></genre><language><json:string>unknown</json:string></language><eissn><json:string>1097-4644</json:string></eissn><title>Journal of Cellular Biochemistry</title><doi><json:string>10.1002/(ISSN)1097-4644</json:string></doi></host><publicationDate>2002</publicationDate><copyrightDate>2002</copyrightDate><doi><json:string>10.1002/jcb.10247</json:string></doi><id>01C9C305B207DC8E1C9741284A6DAA2F01DC3A74</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/01C9C305B207DC8E1C9741284A6DAA2F01DC3A74/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/01C9C305B207DC8E1C9741284A6DAA2F01DC3A74/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/01C9C305B207DC8E1C9741284A6DAA2F01DC3A74/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Differential nuclear receptor signalling from DR4‐type response elements</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><availability><p>WILEY</p></availability><date>2002</date></publicationStmt><notesStmt><note>Academy of Finland - No. 50319; No. 50331;</note><note>Medical Faculty of the Heinrich‐Heine‐University Düsseldorf</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Differential nuclear receptor signalling from DR4‐type response elements</title><author><persName><forename type="first">Marcus</forename><surname>Quack</surname></persName><affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</affiliation><affiliation>Current Address: Raytest Isotopenmessgeräte GmbH, Sirrenbergstr. 9, D‐45549 Sprockhövel, Germany.</affiliation></author><author><persName><forename type="first">Christian</forename><surname>Frank</surname></persName><affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</affiliation></author><author><persName><forename type="first">Carsten</forename><surname>Carlberg</surname></persName><note type="correspondence"><p>Correspondence: Department of Biochemistry, University of Kuopio, P.O. box 1627, FIN‐70211 Kuopio, Finland.</p></note><affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</affiliation><affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</affiliation></author></analytic><monogr><title level="j">Journal of Cellular Biochemistry</title><title level="j" type="abbrev">J. Cell. Biochem.</title><idno type="pISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><idno type="DOI">10.1002/(ISSN)1097-4644</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="2002"></date><biblScope unit="volume">86</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="601">601</biblScope><biblScope unit="page" to="612">612</biblScope></imprint></monogr><idno type="istex">01C9C305B207DC8E1C9741284A6DAA2F01DC3A74</idno><idno type="DOI">10.1002/jcb.10247</idno><idno type="ArticleID">JCB10247</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2002</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>transcriptional regulation</term></item><item><term>vitamin D receptor</term></item><item><term>thyroid hormone receptor</term></item><item><term>liver X receptor</term></item><item><term>retinoid X receptor</term></item><item><term>heterodimeric nuclear receptor</term></item><item><term>complexes</term></item><item><term>response elements</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article category</head><item><term>Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2002-04-04">Received</change><change when="2002-05-13">Registration</change><change when="2002">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/01C9C305B207DC8E1C9741284A6DAA2F01DC3A74/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>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>New York</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4644</doi><issn type="print">0730-2312</issn><issn type="electronic">1097-4644</issn><idGroup><id type="product" value="JCB"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF CELLULAR BIOCHEMISTRY">Journal of Cellular Biochemistry</title><title type="short">J. Cell. Biochem.</title></titleGroup></publicationMeta><publicationMeta level="part" position="30"><doi origin="wiley" registered="yes">10.1002/jcb.v86:3</doi><numberingGroup><numbering type="journalVolume" number="86">86</numbering><numbering type="journalIssue">3</numbering></numberingGroup><coverDate startDate="2002">2002</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="20" status="forIssue"><doi origin="wiley" registered="yes">10.1002/jcb.10247</doi><idGroup><id type="unit" value="JCB10247"></id></idGroup><countGroup><count type="pageTotal" number="12"></count></countGroup><titleGroup><title type="articleCategory">Article</title><title type="tocHeading1">Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2002 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2002-04-04"></event><event type="manuscriptAccepted" date="2002-05-13"></event><event type="firstOnline" date="2002-07-01"></event><event type="publishedOnlineFinalForm" date="2002-07-15"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText" date="2010-03-06"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-29"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-23"></event></eventGroup><numberingGroup><numbering type="pageFirst">601</numbering><numbering type="pageLast">612</numbering></numberingGroup><correspondenceTo>Department of Biochemistry, University of Kuopio, P.O. box 1627, FIN‐70211 Kuopio, Finland.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JCB.JCB10247.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="32"></count><count type="wordTotal" number="6047"></count></countGroup><titleGroup><title type="main" xml:lang="en">Differential nuclear receptor signalling from DR4‐type response elements</title><title type="short" xml:lang="en">DR4‐Type Response Elements</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" currentRef="#curr1"><personName><givenNames>Marcus</givenNames><familyName>Quack</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Christian</givenNames><familyName>Frank</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1 #af2" corresponding="yes"><personName><givenNames>Carsten</givenNames><familyName>Carlberg</familyName></personName><contactDetails><email>carlberg@messi.uku.fi</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="DE" type="organization"><unparsedAffiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="FI" type="organization"><unparsedAffiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</unparsedAffiliation></affiliation><affiliation xml:id="curr1" countryCode="DE"><unparsedAffiliation>Raytest Isotopenmessgeräte GmbH, Sirrenbergstr. 9, D‐45549 Sprockhövel, Germany.</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">transcriptional regulation</keyword><keyword xml:id="kwd2">vitamin D receptor</keyword><keyword xml:id="kwd3">thyroid hormone receptor</keyword><keyword xml:id="kwd4">liver X receptor</keyword><keyword xml:id="kwd5">retinoid X receptor</keyword><keyword xml:id="kwd6">heterodimeric nuclear receptor</keyword><keyword xml:id="kwd7">complexes</keyword><keyword xml:id="kwd8">response elements</keyword></keywordGroup><fundingInfo><fundingAgency>Academy of Finland</fundingAgency><fundingNumber>50319</fundingNumber><fundingNumber>50331</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Medical Faculty of the Heinrich‐Heine‐University Düsseldorf</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D<sub>3</sub> receptor (VDR), the thyroid hormone receptor (T<sub>3</sub>R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat <i>pit‐1</i> gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T<sub>3</sub>R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Differential nuclear receptor signalling from DR4‐type response elements</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>DR4‐Type Response Elements</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Differential nuclear receptor signalling from DR4‐type response elements</title></titleInfo><name type="personal"><namePart type="given">Marcus</namePart><namePart type="family">Quack</namePart><affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</affiliation><affiliation>Current Address: Raytest Isotopenmessgeräte GmbH, Sirrenbergstr. 9, D‐45549 Sprockhövel, Germany.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christian</namePart><namePart type="family">Frank</namePart><affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Carsten</namePart><namePart type="family">Carlberg</namePart><affiliation>Institute for Physiological Chemistry I, Heinrich‐Heine‐University, D‐40001 Düsseldorf, Germany</affiliation><affiliation>Department of Biochemistry, University of Kuopio, FIN‐70211 Kuopio, Finland</affiliation><description>Correspondence: Department of Biochemistry, University of Kuopio, P.O. box 1627, FIN‐70211 Kuopio, Finland.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2002</dateIssued><dateCaptured encoding="w3cdtf">2002-04-04</dateCaptured><dateValid encoding="w3cdtf">2002-05-13</dateValid><copyrightDate encoding="w3cdtf">2002</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">32</extent><extent unit="words">6047</extent></physicalDescription><abstract lang="en">Nuclear receptors form a large family of highly related transcription factors that transform an incoming signal in the form of a lipophilic hormone into an activation of the basal transcriptional machinery. The specific recognition of nuclear receptor DNA binding sites, referred to as response elements (REs), determines the genes that can be regulated by nuclear hormones. In this study, it was shown that the complexes of the retinoid X receptor (RXR) with either the vitamin D3 receptor (VDR), the thyroid hormone receptor (T3R) or the liver X receptor (LXR) have comparable functionality on a RE of the rat pit‐1 gene that is formed by a direct repeat of two hexameric binding motifs spaced by 4 nucleotides (DR4). The sequence of two nucleotides 5′‐flanking the downstream binding motif of this DR4‐type RE and, interestingly, also those flanking the upstream motif were shown to have in part rather drastic and receptor‐specific effects on heterodimer complex formation on DNA. In particular, a downstream substitution into GA reduced the complex formation for LXR specifically, while upstream substitutions into AA or TA increase complex formation for LXR and, to a lesser extent, T3R. The preference of this in vitro complex formation was shown to correlate well with the functional activity of the nuclear receptors in living cells. The results of this study allow (i) a more detailed understanding of known REs, (ii) a more straightforward search for putative REs in newly identified promoter sequences, for example, of the whole human genome, and (iii) a more precise prediction of the hormone responsiveness of the respective genes. J. Cell. Biochem. 86: 601–612, 2002. © 2002 Wiley‐Liss, Inc.</abstract><note type="funding">Academy of Finland - No. 50319; No. 50331; </note><note type="funding">Medical Faculty of the Heinrich‐Heine‐University Düsseldorf</note><subject lang="en"><genre>Keywords</genre><topic>transcriptional regulation</topic><topic>vitamin D receptor</topic><topic>thyroid hormone receptor</topic><topic>liver X receptor</topic><topic>retinoid X receptor</topic><topic>heterodimeric nuclear receptor</topic><topic>complexes</topic><topic>response elements</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Cellular Biochemistry</title></titleInfo><titleInfo type="abbreviated"><title>J. Cell. Biochem.</title></titleInfo><genre type="Journal">journal</genre><subject><genre>article category</genre><topic>Article</topic></subject><identifier type="ISSN">0730-2312</identifier><identifier type="eISSN">1097-4644</identifier><identifier type="DOI">10.1002/(ISSN)1097-4644</identifier><identifier type="PublisherID">JCB</identifier><part><date>2002</date><detail type="volume"><caption>vol.</caption><number>86</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>601</start><end>612</end><total>12</total></extent></part></relatedItem><identifier type="istex">01C9C305B207DC8E1C9741284A6DAA2F01DC3A74</identifier><identifier type="DOI">10.1002/jcb.10247</identifier><identifier type="ArticleID">JCB10247</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2002 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Wiley Subscription Services, Inc., A Wiley Company</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 000B43 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 000B43 | 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:01C9C305B207DC8E1C9741284A6DAA2F01DC3A74
|texte= Differential nuclear receptor signalling from DR4‐type response elements
}}
| This area was generated with Dilib version V0.6.38. |  |