Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
Identifieur interne : 004561 ( Main/Exploration ); précédent : 004560; suivant : 004562Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
Auteurs : Antonis S. Zervos [États-Unis] ; Jeno Gyuris [États-Unis] ; Roger Brent [États-Unis]Source :
- 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proteins, Plasmid, Reading frame, Retinoic, Retinoic acid, Russ finley, Similarity region, Terminus, Transcription, Unpublished data, Yeast, Zipper.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
Affiliations:
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Zervos</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Genetics Harvard Medical School Boston</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Molecular Biology Massachusetts General Hospital Boston</wicri:cityArea></affiliation></author><author><name sortKey="Gyuris, Jeno" sort="Gyuris, Jeno" uniqKey="Gyuris J" first="Jeno" last="Gyuris">Jeno Gyuris</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Genetics Harvard Medical School Boston</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Molecular Biology Massachusetts General Hospital Boston</wicri:cityArea></affiliation></author><author><name sortKey="Brent, Roger" sort="Brent, Roger" uniqKey="Brent R" first="Roger" last="Brent">Roger Brent</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Genetics Harvard Medical School Boston</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Department of Molecular Biology Massachusetts General Hospital Boston</wicri:cityArea></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><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li></region></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Zervos, Antonis S" sort="Zervos, Antonis S" uniqKey="Zervos A" first="Antonis S." last="Zervos">Antonis S. Zervos</name></region><name sortKey="Brent, Roger" sort="Brent, Roger" uniqKey="Brent R" first="Roger" last="Brent">Roger Brent</name><name sortKey="Brent, Roger" sort="Brent, Roger" uniqKey="Brent R" first="Roger" last="Brent">Roger Brent</name><name sortKey="Gyuris, Jeno" sort="Gyuris, Jeno" uniqKey="Gyuris J" first="Jeno" last="Gyuris">Jeno Gyuris</name><name sortKey="Gyuris, Jeno" sort="Gyuris, Jeno" uniqKey="Gyuris J" first="Jeno" last="Gyuris">Jeno Gyuris</name><name sortKey="Zervos, Antonis S" sort="Zervos, Antonis S" uniqKey="Zervos A" first="Antonis S." last="Zervos">Antonis S. Zervos</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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