Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
Identifieur interne : 002593 ( Istex/Corpus ); précédent : 002592; suivant : 002594Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
Auteurs : Antonis S. Zervos ; Jeno Gyuris ; Roger BrentSource :
- Cell [ 0092-8674 ] ; 1993.
English descriptors
- Teeft :
- Acidic, Activation domain, Activation domains, Activation function, Amino, Amino acids, Amino terminus, Assay, Ayer, Bait, Basic region, Binding assays, Biol, Blackwood, Brent, Cdna, Dang, Donald kufe, Eisenman, Experimental procedures, Family proteins, Form heterodimers, Golemis, Gyuris, Halazonetis, Hela, Helical wheel, Helix, Heterodimers, Human protein, Immunoprecipitation experiments, Interaction trap, Kandil, Kato, Leucine, Leucine zipper, Leucine zippers, Lexa, Lexaopleu2 reporter, Mrna, Mrna levels, Mxil, Mxil interacted, Mxil mrna, Mxil residues, Oligonucleotide, Other members, Other proteins, Plasmid, Reading frame, Retinoic, Retinoic acid, Russ finley, Similarity region, Terminus, Transcription, Unpublished data, Yeast, Zipper.
Abstract
Abstract: We used the interaction trap to isolate a novel human protein that specifically interacts with Max. This protein, Mxi1 (for Max interactor 1), contains a bHLH-Zip motif that is simillar to that found in Myc family proteins. Mxi1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. When bound to DNA by a LexA moiety in yeast, Mxi1 does not stimulate transcription. mxi1 mRNA is expressed in many tissues, and its expression is elevated in U-937 myeloid leukemia cells that have been stimulated to differentiate. These facts are consistent with a model in which Mxi1-Max heterodimers indirectly inhibit Myc function in two ways: first, by sequestering Max, thus preventing the formation of Myc-Max heterodimers, and second, by competing with Myc-Max heterodimers for binding to target sites.
Url:
DOI: 10.1016/0092-8674(93)90662-A
Links to Exploration step
ISTEX:463777C5B3F7B5E959E87A70AFA4BC8F349DE019Le document en format XML
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Zervos</name><affiliation><mods:affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</mods:affiliation></affiliation></author><author><name sortKey="Gyuris, Jeno" sort="Gyuris, Jeno" uniqKey="Gyuris J" first="Jeno" last="Gyuris">Jeno Gyuris</name><affiliation><mods:affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</mods:affiliation></affiliation></author><author><name sortKey="Brent, Roger" sort="Brent, Roger" uniqKey="Brent R" first="Roger" last="Brent">Roger Brent</name><affiliation><mods:affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">72</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="223">223</biblScope><biblScope unit="page" to="232">232</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acidic</term><term>Activation domain</term><term>Activation domains</term><term>Activation function</term><term>Amino</term><term>Amino acids</term><term>Amino terminus</term><term>Assay</term><term>Ayer</term><term>Bait</term><term>Basic region</term><term>Binding assays</term><term>Biol</term><term>Blackwood</term><term>Brent</term><term>Cdna</term><term>Dang</term><term>Donald kufe</term><term>Eisenman</term><term>Experimental procedures</term><term>Family proteins</term><term>Form heterodimers</term><term>Golemis</term><term>Gyuris</term><term>Halazonetis</term><term>Hela</term><term>Helical wheel</term><term>Helix</term><term>Heterodimers</term><term>Human protein</term><term>Immunoprecipitation experiments</term><term>Interaction trap</term><term>Kandil</term><term>Kato</term><term>Leucine</term><term>Leucine zipper</term><term>Leucine zippers</term><term>Lexa</term><term>Lexaopleu2 reporter</term><term>Mrna</term><term>Mrna levels</term><term>Mxil</term><term>Mxil interacted</term><term>Mxil mrna</term><term>Mxil residues</term><term>Oligonucleotide</term><term>Other members</term><term>Other proteins</term><term>Plasmid</term><term>Reading frame</term><term>Retinoic</term><term>Retinoic acid</term><term>Russ finley</term><term>Similarity region</term><term>Terminus</term><term>Transcription</term><term>Unpublished data</term><term>Yeast</term><term>Zipper</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We used the interaction trap to isolate a novel human protein that specifically interacts with Max. This protein, Mxi1 (for Max interactor 1), contains a bHLH-Zip motif that is simillar to that found in Myc family proteins. Mxi1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. When bound to DNA by a LexA moiety in yeast, Mxi1 does not stimulate transcription. mxi1 mRNA is expressed in many tissues, and its expression is elevated in U-937 myeloid leukemia cells that have been stimulated to differentiate. These facts are consistent with a model in which Mxi1-Max heterodimers indirectly inhibit Myc function in two ways: first, by sequestering Max, thus preventing the formation of Myc-Max heterodimers, and second, by competing with Myc-Max heterodimers for binding to target sites.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>mxil</json:string><json:string>mrna</json:string><json:string>eisenman</json:string><json:string>golemis</json:string><json:string>leucine</json:string><json:string>cdna</json:string><json:string>blackwood</json:string><json:string>biol</json:string><json:string>gyuris</json:string><json:string>brent</json:string><json:string>acidic</json:string><json:string>amino acids</json:string><json:string>amino</json:string><json:string>plasmid</json:string><json:string>halazonetis</json:string><json:string>heterodimers</json:string><json:string>lexa</json:string><json:string>helix</json:string><json:string>mxil mrna</json:string><json:string>unpublished data</json:string><json:string>zipper</json:string><json:string>kato</json:string><json:string>hela</json:string><json:string>kandil</json:string><json:string>leucine zipper</json:string><json:string>interaction trap</json:string><json:string>oligonucleotide</json:string><json:string>retinoic</json:string><json:string>ayer</json:string><json:string>family proteins</json:string><json:string>assay</json:string><json:string>experimental procedures</json:string><json:string>amino terminus</json:string><json:string>retinoic acid</json:string><json:string>basic region</json:string><json:string>similarity region</json:string><json:string>yeast</json:string><json:string>transcription</json:string><json:string>bait</json:string><json:string>leucine zippers</json:string><json:string>other proteins</json:string><json:string>mxil residues</json:string><json:string>dang</json:string><json:string>activation domains</json:string><json:string>binding assays</json:string><json:string>lexaopleu2 reporter</json:string><json:string>activation domain</json:string><json:string>helical wheel</json:string><json:string>mxil interacted</json:string><json:string>donald kufe</json:string><json:string>russ finley</json:string><json:string>form heterodimers</json:string><json:string>immunoprecipitation experiments</json:string><json:string>other members</json:string><json:string>human protein</json:string><json:string>reading frame</json:string><json:string>activation function</json:string><json:string>mrna levels</json:string><json:string>terminus</json:string><json:string>protein</json:string><json:string>activation</json:string><json:string>higher cells</json:string><json:string>different sensitivities</json:string><json:string>different baits</json:string><json:string>mrna expression</json:string><json:string>monocytic markers</json:string><json:string>cell cycle</json:string><json:string>localization signal</json:string><json:string>acidic stretch</json:string><json:string>mammalian cells</json:string><json:string>unknown function</json:string><json:string>acidic residues</json:string><json:string>carboxyl terminus</json:string><json:string>nuclear localization sequence</json:string><json:string>amino acid protein</json:string><json:string>cacgtg consensus site</json:string><json:string>binding reactions</json:string><json:string>adult brain</json:string><json:string>myeloid leukemia cells</json:string><json:string>restriction mapping</json:string><json:string>northern blot</json:string><json:string>murine homolog</json:string><json:string>model systems</json:string><json:string>noncoding region</json:string><json:string>block differentiation</json:string><json:string>open reading frame</json:string><json:string>apparent mobility</json:string><json:string>time point</json:string><json:string>retinoic acid induction</json:string><json:string>retardation assays</json:string><json:string>fusion proteins</json:string><json:string>human brain</json:string><json:string>ophelia papoulas</json:string><json:string>thanos halazonetis</json:string><json:string>binding reaction</json:string><json:string>ralf hass</json:string><json:string>coding sequence</json:string><json:string>avian myelocytomatosis virus</json:string><json:string>current protocols</json:string><json:string>molecular biology</json:string><json:string>personal communication</json:string></teeft></keywords><author><json:item><name>Antonis S. Zervos</name><affiliations><json:string>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</json:string><json:string>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</json:string></affiliations></json:item><json:item><name>Jenő Gyuris</name><affiliations><json:string>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</json:string><json:string>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</json:string></affiliations></json:item><json:item><name>Roger Brent</name><affiliations><json:string>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</json:string><json:string>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-J2LGTS22-S</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: We used the interaction trap to isolate a novel human protein that specifically interacts with Max. This protein, Mxi1 (for Max interactor 1), contains a bHLH-Zip motif that is simillar to that found in Myc family proteins. Mxi1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. When bound to DNA by a LexA moiety in yeast, Mxi1 does not stimulate transcription. mxi1 mRNA is expressed in many tissues, and its expression is elevated in U-937 myeloid leukemia cells that have been stimulated to differentiate. These facts are consistent with a model in which Mxi1-Max heterodimers indirectly inhibit Myc function in two ways: first, by sequestering Max, thus preventing the formation of Myc-Max heterodimers, and second, by competing with Myc-Max heterodimers for binding to target sites.</abstract><qualityIndicators><score>8.608</score><pdfWordCount>7295</pdfWordCount><pdfCharCount>48176</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>611.84 x 863.768 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>134</abstractWordCount><abstractCharCount>866</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites</title><pmid><json:string>8425219</json:string></pmid><pii><json:string>0092-8674(93)90662-A</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>89</volume><pages><first>599</first><last>602</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1993</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0405-9</json:string></pii><volume>72</volume><issue>2</issue><pages><first>223</first><last>232</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1993</json:string></date><geogName></geogName><orgName><json:string>Stratagene, Inc.</json:string><json:string>US Biochemicals</json:string><json:string>Biochem</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Andrew Mendelsohn</json:string><json:string>E. A. Golemis</json:string><json:string>J. Biol</json:string><json:string>Max Partner</json:string><json:string>John Wiley</json:string><json:string>Steve Hanes</json:string><json:string>Erica Golemis</json:string><json:string>R. Bernard</json:string><json:string>Ralf Hass</json:string><json:string>Zip</json:string><json:string>Tom Kadesh</json:string><json:string>Thanos Halazonetis</json:string><json:string>Russ Finley</json:string><json:string>G. Gill</json:string><json:string>Bob Kingston</json:string><json:string>M. Billard</json:string><json:string>E. Blackwood</json:string><json:string>LexA-Max LexA-Mxil</json:string><json:string>Marc Billard</json:string><json:string>Andrew Lassar</json:string><json:string>R. Tjian</json:string><json:string>David Ish-Horowitz</json:string><json:string>C. Besmond</json:string><json:string>Ralph Hass</json:string><json:string>Steve Sloan</json:string><json:string>LexA-Max LexA</json:string><json:string>Ophelia Papoulas</json:string><json:string>Tod Gulick</json:string><json:string>Rene Bernards</json:string><json:string>Mxil</json:string><json:string>R. Finley</json:string><json:string>Mad</json:string><json:string>Don Ayer</json:string><json:string>J. Gyuris</json:string><json:string>Donald Kufe</json:string><json:string>Bob Eisenman</json:string></persName><placeName></placeName><ref_url></ref_url><ref_bibl><json:string>Smith and Corcoran, 1989</json:string><json:string>Hoffman and Winston (1987)</json:string><json:string>Papoulas et al. (1992)</json:string><json:string>Ebina et al., 1983</json:string><json:string>for reviews see Cole, 1986</json:string><json:string>Watanabe et al., 1965</json:string><json:string>Kamens et al., 1990</json:string><json:string>Ayer et al., 1993</json:string><json:string>Hu et al. (1990)</json:string><json:string>Blackwood and Eisenman, 1991</json:string><json:string>E. A. Golemis et al.</json:string><json:string>Hann and Eisenman, 1984</json:string><json:string>Heaney et al., 1986</json:string><json:string>Halazonetis and Kandil, 1992</json:string><json:string>Blackwood et al., 1992a, 1992b</json:string><json:string>J. Gyuris et al.</json:string><json:string>Miller, 1972</json:string><json:string>Adams et al., 1992</json:string><json:string>Beckmann and Kadesch, 1991</json:string><json:string>Kretzner et al., 1992</json:string><json:string>Stone et al., 1987</json:string><json:string>Rao and Johnson, 1970</json:string><json:string>as in Halazonetis and Kandil, 1991</json:string><json:string>reviewed in Harris and Ralph, 1985</json:string><json:string>reviewed in Vinson and Garcia, 1992</json:string><json:string>Gunji et al., 1992</json:string><json:string>Gujii et al., 1992</json:string><json:string>Dang et al., 1992</json:string><json:string>Halazonetis and Kandil, 1991</json:string><json:string>Berberich and Cole, 1992</json:string><json:string>Dang et al., 1969</json:string><json:string>Prendergast et al., 1991</json:string><json:string>Pugh and Tjian, 1990</json:string><json:string>Golemis and Brent, 1992</json:string><json:string>Watanabe et al., 1985</json:string><json:string>reviewed in Liischer and Eisenmann, 1990</json:string><json:string>Kato et al., 1992</json:string><json:string>Shi et al., 1992</json:string><json:string>Benezra et al. (1990)</json:string><json:string>Lech et al., 1988</json:string><json:string>Tokunaga et al., 1967</json:string><json:string>Shea et al. (1989)</json:string><json:string>Miner and Wold, 1991</json:string><json:string>Blackwell et al., 1990</json:string><json:string>Evan et al., 1992</json:string><json:string>Freytag, 1988</json:string><json:string>Guthrie and Fink, 1992</json:string><json:string>Ausubel et al., 1992</json:string><json:string>Fields and Bong (1969)</json:string><json:string>Liischer and Eisbnman, 1988</json:string><json:string>Fields and Song (1989)</json:string><json:string>Kume et al., 1988</json:string><json:string>Hass et al., 1991</json:string><json:string>Dingwafl and Laskey, 1991</json:string><json:string>Blackwood and Eisenmann (1991)</json:string><json:string>Chirgwin et al., 1979</json:string><json:string>Devereux et al., 1984</json:string><json:string>Ayer et al. (1993)</json:string><json:string>Kato et al., 1990</json:string><json:string>Liischer and Eisenman, 1990</json:string><json:string>Ruden et al., 1991</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-J2LGTS22-S</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - cell biology</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - developmental biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - General Biochemistry, Genetics and Molecular Biology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1993</publicationDate><copyrightDate>1993</copyrightDate><doi><json:string>10.1016/0092-8674(93)90662-A</json:string></doi><id>463777C5B3F7B5E959E87A70AFA4BC8F349DE019</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-J2LGTS22-S/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-J2LGTS22-S/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-J2LGTS22-S/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1993</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites</title><author xml:id="author-0000"><persName><forename type="first">Antonis S.</forename><surname>Zervos</surname></persName><affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</affiliation><affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Jenő</forename><surname>Gyuris</surname></persName><affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</affiliation><affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Roger</forename><surname>Brent</surname></persName><affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</affiliation><affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</affiliation></author><idno type="istex">463777C5B3F7B5E959E87A70AFA4BC8F349DE019</idno><idno type="ark">ark:/67375/6H6-J2LGTS22-S</idno><idno type="DOI">10.1016/0092-8674(93)90662-A</idno><idno type="PII">0092-8674(93)90662-A</idno></analytic><monogr><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="pISSN">0092-8674</idno><idno type="PII">S0092-8674(00)X0405-9</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993"></date><biblScope unit="volume">72</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="223">223</biblScope><biblScope unit="page" to="232">232</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1993</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: We used the interaction trap to isolate a novel human protein that specifically interacts with Max. This protein, Mxi1 (for Max interactor 1), contains a bHLH-Zip motif that is simillar to that found in Myc family proteins. Mxi1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. When bound to DNA by a LexA moiety in yeast, Mxi1 does not stimulate transcription. mxi1 mRNA is expressed in many tissues, and its expression is elevated in U-937 myeloid leukemia cells that have been stimulated to differentiate. These facts are consistent with a model in which Mxi1-Max heterodimers indirectly inhibit Myc function in two ways: first, by sequestering Max, thus preventing the formation of Myc-Max heterodimers, and second, by competing with Myc-Max heterodimers for binding to target sites.</p></abstract></profileDesc><revisionDesc><change when="1992-11-24">Modified</change><change when="1993">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-J2LGTS22-S/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>9390662A</aid><ce:pii>0092-8674(93)90662-A</ce:pii><ce:doi>10.1016/0092-8674(93)90662-A</ce:doi><ce:copyright type="unknown" year="1993"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites</ce:title><ce:author-group><ce:author><ce:given-name>Antonis S.</ce:given-name><ce:surname>Zervos</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jenő</ce:given-name><ce:surname>Gyuris</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Roger</ce:given-name><ce:surname>Brent</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="25" month="9" year="1992"></ce:date-received><ce:date-revised day="24" month="11" year="1992"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>We used the interaction trap to isolate a novel human protein that specifically interacts with Max. This protein, Mxi1 (for Max interactor 1), contains a bHLH-Zip motif that is simillar to that found in Myc family proteins. Mxi1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. When bound to DNA by a LexA moiety in yeast, Mxi1 does not stimulate transcription. <ce:italic>mxi1</ce:italic> mRNA is expressed in many tissues, and its expression is elevated in U-937 myeloid leukemia cells that have been stimulated to differentiate. These facts are consistent with a model in which Mxi1-Max heterodimers indirectly inhibit Myc function in two ways: first, by sequestering Max, thus preventing the formation of Myc-Max heterodimers, and second, by competing with Myc-Max heterodimers for binding to target sites.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites</title></titleInfo><name type="personal"><namePart type="given">Antonis S.</namePart><namePart type="family">Zervos</namePart><affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</affiliation><affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jenő</namePart><namePart type="family">Gyuris</namePart><affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</affiliation><affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Roger</namePart><namePart type="family">Brent</namePart><affiliation>Department of Genetics Harvard Medical School Boston, Massachusetts 02114 USA</affiliation><affiliation>Department of Molecular Biology Massachusetts General Hospital Boston, Massachusetts 02114 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">1993</dateIssued><dateModified encoding="w3cdtf">1992-11-24</dateModified><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: We used the interaction trap to isolate a novel human protein that specifically interacts with Max. This protein, Mxi1 (for Max interactor 1), contains a bHLH-Zip motif that is simillar to that found in Myc family proteins. Mxi1 interacts specifically with Max to form heterodimers that efficiently bind to the Myc-Max consensus recognition site. When bound to DNA by a LexA moiety in yeast, Mxi1 does not stimulate transcription. mxi1 mRNA is expressed in many tissues, and its expression is elevated in U-937 myeloid leukemia cells that have been stimulated to differentiate. These facts are consistent with a model in which Mxi1-Max heterodimers indirectly inhibit Myc function in two ways: first, by sequestering Max, thus preventing the formation of Myc-Max heterodimers, and second, by competing with Myc-Max heterodimers for binding to target sites.</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">1993</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0405-9</identifier><part><date>1993</date><detail type="volume"><number>72</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>161</start><end>300</end></extent><extent unit="pages"><start>223</start><end>232</end></extent></part></relatedItem><identifier type="istex">463777C5B3F7B5E959E87A70AFA4BC8F349DE019</identifier><identifier type="ark">ark:/67375/6H6-J2LGTS22-S</identifier><identifier type="DOI">10.1016/0092-8674(93)90662-A</identifier><identifier type="PII">0092-8674(93)90662-A</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-J2LGTS22-S/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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