Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity
Identifieur interne : 001855 ( Istex/Corpus ); précédent : 001854; suivant : 001856Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity
Auteurs : Tom K. Kerppola ; Tom CurranSource :
- Cell [ 0092-8674 ] ; 1991.
English descriptors
- Teeft :
- Additional regions, Amino acid residues, Analysis probes, Average mobility, Base pairs, Bends, Binding site, Binding sites, Biol, Circular permutation analysis, Circular permutation function, Circularly permuted probes, Complex mobilities, Conformational change, Cosine function, Crothers, Crystal structure, Curran, Different experiments, Different positions, Dimerization, Dnabinding domains, Electrophoretic, Electrophoretic mobilities, Electrophoretic mobility shift analysis, Flexure, Flexure angles, Fosjun heterodimers, Free probes, Gene regulation, Glucocorticoid receptor, Helix, Helix trajectories, Heterodimer, Heterodimers, Homodimer, Homodimer complexes, Homodimers, Identical lengths, Identical results, Independent experiments, Integration host factor, Intrinsic, Intrinsic bends, Landy, Leucine, Leucine region, Leucine region peptides, Leucine region proteins, Leucine zipper, Major groove, Minor groove, Mobility, Mobility patterns, Mobility variations, Moitoso, Molecular models, Nickel chelate affinity chromatography, Nitrogen fixation operons, Opposite orientations, Other peptides, Peptide, Permutation, Permutation analysis, Plasmid, Polyacrylamide, Probe, Probe mobilities, Prolactin gene, Protein complexes, Regulatory elements, Relative mobilities, Same orientations, Same sequences, Second molecule, Spacer, Spacer length, Spacer lengths, Standard deviation, Standard deviations, Structural distortion, Transcription, Transcription activation, Transcription factor, Transcription factors, Transcription initiation, Transcription regulation, Transcriptional, Transcriptional activator, Transcriptional activity, Unpublished data, Vargas, Xylene cyanol, Zipper.
Abstract
Abstract: Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain. We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.
Url:
DOI: 10.1016/0092-8674(91)90621-5
Links to Exploration step
ISTEX:791C3AF85CE2802AEF10F05C021A294E84D50C8ALe document en format XML
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We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. 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Kerppola</name><affiliations><json:string>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110, USA</json:string></affiliations></json:item><json:item><name>Tom Curran</name><affiliations><json:string>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-9ZFT201L-4</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain. We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.</abstract><qualityIndicators><score>8.8</score><pdfWordCount>6667</pdfWordCount><pdfCharCount>44143</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>612.28 x 806 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>150</abstractWordCount><abstractCharCount>1020</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity</title><pmid><json:string>1906785</json:string></pmid><pii><json:string>0092-8674(91)90621-5</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>87</volume><pages><first>1032</first><last>1036</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1991</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0631-9</json:string></pii><volume>66</volume><issue>2</issue><pages><first>317</first><last>326</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1991</json:string></date><geogName></geogName><orgName><json:string>Helen Hay Whitney Foundation</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Jun Probes</json:string><json:string>Jun Heterodimer</json:string><json:string>Analysis Heterodimers</json:string><json:string>Jun Homodimers</json:string><json:string>Tom K. Kerppola</json:string><json:string>K. Yamamoto</json:string><json:string>Jun Homodimer</json:string><json:string>Jun Dimerization</json:string><json:string>Donald Nuss</json:string><json:string>Jun Homo</json:string><json:string>Cory Abate</json:string><json:string>Jun Heterodimers</json:string><json:string>Craig Rosen</json:string></persName><placeName></placeName><ref_url></ref_url><ref_bibl><json:string>Gustafson et al., 1989</json:string><json:string>Wu and Crothers, 1984</json:string><json:string>reviewed in Kerp pola and Curran, 1991</json:string><json:string>Lerman and Frisch, 1982</json:string><json:string>Abate et al., 1991</json:string><json:string>Rauscher et al., 1988</json:string><json:string>Kerppola and Curran, 1991</json:string><json:string>Diamond et al., 1990</json:string><json:string>Thompson and Landy, 1988</json:string><json:string>Hoover et al., 1990</json:string><json:string>Sonnenberg et al., 1989</json:string><json:string>Gartenberg et al., 1990</json:string><json:string>Weiss et al., 1990</json:string><json:string>Risse et al., 1989</json:string><json:string>Lumpkin et al., 1985</json:string><json:string>Vignais and Sentenac, 1989</json:string><json:string>Gober and Shapiro, 1990</json:string><json:string>Talanian et al., 1990</json:string><json:string>Franza et al., 1988</json:string><json:string>Moitoso de Vargas et al., 1989</json:string><json:string>Abate et al.</json:string><json:string>Goodman and Nash, 1989</json:string><json:string>Cohen and Curran, 1990</json:string><json:string>Bohmann et al., 1987</json:string><json:string>reviewed in Curran and Vogt, 1991</json:string><json:string>Levene et al., 1986</json:string><json:string>McAllister and Achberger, 1989</json:string><json:string>Schreck et al., 1990</json:string><json:string>Wang and Giaever, 1988</json:string><json:string>Peck and Wang, 1981</json:string><json:string>Moitoso de Vargas and Landy, 1991</json:string><json:string>Brennan et al., 1990</json:string><json:string>Kim et al., 1990</json:string><json:string>Salvo and Grindley, 1988</json:string><json:string>Zinkel and Crothers, 1987</json:string><json:string>Baur and Knippers, 1988</json:string><json:string>Hai and Curran, 1991</json:string><json:string>Distel et al., 1988</json:string><json:string>Rojo et al., 1990</json:string><json:string>Kim et al., 1989</json:string><json:string>Bracco et al., 1989</json:string><json:string>Neil et al., 1990</json:string><json:string>Vinson et al., 1989</json:string><json:string>Ryseck and Bravo, 1991</json:string><json:string>Salvo and Grindley, 1987</json:string><json:string>Snyder et al., 1989</json:string><json:string>Abate et al., 1990b</json:string><json:string>Levene and Zimm, 1989</json:string><json:string>Rhodes and Klug, 1981</json:string><json:string>Htun and Dahlberg, 1988</json:string><json:string>Zahn and Blattner, 1987</json:string><json:string>Koo et al., 1990</json:string><json:string>Williams et al., 1988</json:string><json:string>reviewed in Kerppola and Curran, 1991</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-9ZFT201L-4</json:string></ark><categories><wos><json:string>1 - 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We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.</p></abstract></profileDesc><revisionDesc><change when="1991-05-30">Modified</change><change when="1991">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9ZFT201L-4/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>91906215</aid><ce:pii>0092-8674(91)90621-5</ce:pii><ce:doi>10.1016/0092-8674(91)90621-5</ce:doi><ce:copyright type="unknown" year="1991"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity</ce:title><ce:author-group><ce:author><ce:given-name>Tom K.</ce:given-name><ce:surname>Kerppola</ce:surname></ce:author><ce:author><ce:given-name>Tom</ce:given-name><ce:surname>Curran</ce:surname></ce:author><ce:affiliation><ce:textfn>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="21" month="3" year="1991"></ce:date-received><ce:date-revised day="30" month="5" year="1991"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain. We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Fos-Jun heterodimers and jun homodimers bend DNA in opposite orientations: Implications for transcription factor cooperativity</title></titleInfo><name type="personal"><namePart type="given">Tom K.</namePart><namePart type="family">Kerppola</namePart><affiliation>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Tom</namePart><namePart type="family">Curran</namePart><affiliation>Department of Molecular Oncology and Virology Roche Institute of Molecular Biology Nutley, New Jersey 07110, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued><dateModified encoding="w3cdtf">1991-05-30</dateModified><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain. We show that Fos and Jun induce a corresponding alteration in the conformation of the DNA helix. Circular permutation analysis indicated that both Fos-Jun heterodimers and Jun homodimers induce flexure at the AP-1 site. Phasing analysis demonstrated that Fos-Jun heterodimers and Jun homodimers induce DNA bends that are directed in opposite orientations. Fos-Jun heterodimers bend DNA toward the major groove, whereas Jun homodimers bend DNA toward the minor groove. Fos and Jun peptides encompassing the dimerization and DNA-binding domains bend DNA in the same orientations as the full-length proteins. However, additional regions of both proteins influence the magnitude of the DNA bend angle. Thus, despite the amino acid sequence similarity in the basic region Fos-Jun heterodimers and Jun homodimers form topologically distinct DNA-protein complexes.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0631-9</identifier><part><date>1991</date><detail type="volume"><number>66</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>185</start><end>413</end></extent><extent unit="pages"><start>317</start><end>326</end></extent></part></relatedItem><identifier type="istex">791C3AF85CE2802AEF10F05C021A294E84D50C8A</identifier><identifier type="ark">ark:/67375/6H6-9ZFT201L-4</identifier><identifier type="DOI">10.1016/0092-8674(91)90621-5</identifier><identifier type="PII">0092-8674(91)90621-5</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-9ZFT201L-4/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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