Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity
Identifieur interne : 001D71 ( Istex/Corpus ); précédent : 001D70; suivant : 001D72Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity
Auteurs : Nadia A. Higgy ; Heide A. Tarnasky ; Isabelle Valarché ; Alain Nepveu ; Frans A. Van Der HoornSource :
- BBA - Gene Structure and Expression [ 0167-4781 ] ; 1997.
English descriptors
- Teeft :
- Acta, Amino acids, Assay, Bacterial extracts, Binding site, Biochimica, Biol, Biophysica, Biophysica acta, Cdna, Cdp2, Cell cycle, Cuxrcdp, Cuxrcdp proteins, Cuxrcdp repression, Deletion, Deletion mutants, Dnase, Ectopic expression, Emsa, Emsa supershift assays, Enhancer, Enhancer activity, Enhancer site, Fibroblast, Footprint, Fusion protein, Hcut, Higgy, Homeodomain, Homeodomain protein, Hoorn, Internal control, Monoclonal, Monoclonal antibodies, Mouse fibroblasts, Mouse lung, Mouse testis, Murine, Murine cuxrcdp, Murine lung, Mutant, Mutant site, Nepveu, Nuclear extracts, Nuclear factor, Nuclear protein, Nucleic acids, Oligo, Oocyte, Pblcat2, Phage, Plasmid, Prcrcmvcuxfl, Promoter, Reporter plasmid, Repressor, Somatic cells, Testis, Transfection, Transfections, Unrelated control, Vande woude.
Abstract
Abstract: The c-mos gene is transcribed in male and female germ cells, in differentiating myoblasts and in 3T3 cells from cell-specific promoters. We characterized the rat testis promoter, which contains a TATA-box and one binding site for a testis-specific transcription factor TTF-D, as well as a region which can act as enhancer, which is located approx. 2 kb upstream of the c-mos AUG start codon. It binds three factors at sites I, II and III as determined in DNAse I footprint assays. We demonstrated that a member of the NF-1/CTF family of transcription factors binds site II. Here we report the cloning of the protein that binds to enhancer site III. This protein is the rat homolog of human hCut/CDP, mouse Cux/CDP and canine Clox. hCut/Cux/CDP/Clox (hereafter called Cux/CDP), a 160 kDa protein containing multiple repeats and a homeodomain, negatively regulates the mammalian c-myc, gp91-phox and N-Cam genes. Using bacterially produced murine GST-Cux fusion proteins and GST-Cux deletion mutants, we find that Cux repeat CR3 and the homeodomain are both required for efficient binding to enhancer site III. Mouse lung and testis nuclear Cux/CDP bind to site III as determined in electrophoretic gel mobility supershift assays using two different anti-hCut specific monoclonal antibodies. Transfections of CAT constructs containing the enhancer fragment linked to a minimal promoter demonstrated that Cux/CDP represses c-mos enhancer activity.
Url:
DOI: 10.1016/S0167-4781(96)00221-7
Links to Exploration step
ISTEX:88A9C5DE24BAA56AA38A5FA7A9BD3A5624679A22Le document en format XML
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Tarnasky</name><affiliation><mods:affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</mods:affiliation></affiliation></author><author><name sortKey="Valarche, Isabelle" sort="Valarche, Isabelle" uniqKey="Valarche I" first="Isabelle" last="Valarché">Isabelle Valarché</name><affiliation><mods:affiliation>Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Nepveu, Alain" sort="Nepveu, Alain" uniqKey="Nepveu A" first="Alain" last="Nepveu">Alain Nepveu</name><affiliation><mods:affiliation>Molecular Oncology Group Departments of Medicine and Oncology McGill University, Royal Victoria Hospital Montreal, Quebec, Canada H3A 1A1</mods:affiliation></affiliation></author><author><name sortKey="Van Der Hoorn, Frans A" sort="Van Der Hoorn, Frans A" uniqKey="Van Der Hoorn F" first="Frans A" last="Van Der Hoorn">Frans A. Van Der Hoorn</name><affiliation><mods:affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:88A9C5DE24BAA56AA38A5FA7A9BD3A5624679A22</idno><date when="1997" year="1997">1997</date><idno type="doi">10.1016/S0167-4781(96)00221-7</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-34LPBCB5-D/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001D71</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001D71</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity</title><author><name sortKey="Higgy, Nadia A" sort="Higgy, Nadia A" uniqKey="Higgy N" first="Nadia A" last="Higgy">Nadia A. Higgy</name><affiliation><mods:affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</mods:affiliation></affiliation></author><author><name sortKey="Tarnasky, Heide A" sort="Tarnasky, Heide A" uniqKey="Tarnasky H" first="Heide A" last="Tarnasky">Heide A. Tarnasky</name><affiliation><mods:affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</mods:affiliation></affiliation></author><author><name sortKey="Valarche, Isabelle" sort="Valarche, Isabelle" uniqKey="Valarche I" first="Isabelle" last="Valarché">Isabelle Valarché</name><affiliation><mods:affiliation>Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</mods:affiliation></affiliation></author><author><name sortKey="Nepveu, Alain" sort="Nepveu, Alain" uniqKey="Nepveu A" first="Alain" last="Nepveu">Alain Nepveu</name><affiliation><mods:affiliation>Molecular Oncology Group Departments of Medicine and Oncology McGill University, Royal Victoria Hospital Montreal, Quebec, Canada H3A 1A1</mods:affiliation></affiliation></author><author><name sortKey="Van Der Hoorn, Frans A" sort="Van Der Hoorn, Frans A" uniqKey="Van Der Hoorn F" first="Frans A" last="Van Der Hoorn">Frans A. Van Der Hoorn</name><affiliation><mods:affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">BBA - Gene Structure and Expression</title><title level="j" type="abbrev">BBAEXP</title><idno type="ISSN">0167-4781</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">1351</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="313">313</biblScope><biblScope unit="page" to="324">324</biblScope></imprint><idno type="ISSN">0167-4781</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-4781</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acta</term><term>Amino acids</term><term>Assay</term><term>Bacterial extracts</term><term>Binding site</term><term>Biochimica</term><term>Biol</term><term>Biophysica</term><term>Biophysica acta</term><term>Cdna</term><term>Cdp2</term><term>Cell cycle</term><term>Cuxrcdp</term><term>Cuxrcdp proteins</term><term>Cuxrcdp repression</term><term>Deletion</term><term>Deletion mutants</term><term>Dnase</term><term>Ectopic expression</term><term>Emsa</term><term>Emsa supershift assays</term><term>Enhancer</term><term>Enhancer activity</term><term>Enhancer site</term><term>Fibroblast</term><term>Footprint</term><term>Fusion protein</term><term>Hcut</term><term>Higgy</term><term>Homeodomain</term><term>Homeodomain protein</term><term>Hoorn</term><term>Internal control</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Mouse fibroblasts</term><term>Mouse lung</term><term>Mouse testis</term><term>Murine</term><term>Murine cuxrcdp</term><term>Murine lung</term><term>Mutant</term><term>Mutant site</term><term>Nepveu</term><term>Nuclear extracts</term><term>Nuclear factor</term><term>Nuclear protein</term><term>Nucleic acids</term><term>Oligo</term><term>Oocyte</term><term>Pblcat2</term><term>Phage</term><term>Plasmid</term><term>Prcrcmvcuxfl</term><term>Promoter</term><term>Reporter plasmid</term><term>Repressor</term><term>Somatic cells</term><term>Testis</term><term>Transfection</term><term>Transfections</term><term>Unrelated control</term><term>Vande woude</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The c-mos gene is transcribed in male and female germ cells, in differentiating myoblasts and in 3T3 cells from cell-specific promoters. We characterized the rat testis promoter, which contains a TATA-box and one binding site for a testis-specific transcription factor TTF-D, as well as a region which can act as enhancer, which is located approx. 2 kb upstream of the c-mos AUG start codon. It binds three factors at sites I, II and III as determined in DNAse I footprint assays. We demonstrated that a member of the NF-1/CTF family of transcription factors binds site II. Here we report the cloning of the protein that binds to enhancer site III. This protein is the rat homolog of human hCut/CDP, mouse Cux/CDP and canine Clox. hCut/Cux/CDP/Clox (hereafter called Cux/CDP), a 160 kDa protein containing multiple repeats and a homeodomain, negatively regulates the mammalian c-myc, gp91-phox and N-Cam genes. Using bacterially produced murine GST-Cux fusion proteins and GST-Cux deletion mutants, we find that Cux repeat CR3 and the homeodomain are both required for efficient binding to enhancer site III. Mouse lung and testis nuclear Cux/CDP bind to site III as determined in electrophoretic gel mobility supershift assays using two different anti-hCut specific monoclonal antibodies. Transfections of CAT constructs containing the enhancer fragment linked to a minimal promoter demonstrated that Cux/CDP represses c-mos enhancer activity.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>cuxrcdp</json:string><json:string>enhancer</json:string><json:string>testis</json:string><json:string>murine</json:string><json:string>oligo</json:string><json:string>mutant</json:string><json:string>higgy</json:string><json:string>homeodomain</json:string><json:string>biol</json:string><json:string>acta</json:string><json:string>fibroblast</json:string><json:string>mutant site</json:string><json:string>promoter</json:string><json:string>enhancer activity</json:string><json:string>biophysica</json:string><json:string>biochimica</json:string><json:string>enhancer site</json:string><json:string>biophysica acta</json:string><json:string>hcut</json:string><json:string>pblcat2</json:string><json:string>emsa</json:string><json:string>deletion</json:string><json:string>footprint</json:string><json:string>hoorn</json:string><json:string>oocyte</json:string><json:string>plasmid</json:string><json:string>assay</json:string><json:string>transfection</json:string><json:string>transfections</json:string><json:string>dnase</json:string><json:string>cdna</json:string><json:string>cdp2</json:string><json:string>phage</json:string><json:string>monoclonal</json:string><json:string>repressor</json:string><json:string>nepveu</json:string><json:string>monoclonal antibodies</json:string><json:string>prcrcmvcuxfl</json:string><json:string>mouse lung</json:string><json:string>deletion mutants</json:string><json:string>fusion protein</json:string><json:string>somatic cells</json:string><json:string>binding site</json:string><json:string>reporter plasmid</json:string><json:string>vande woude</json:string><json:string>murine cuxrcdp</json:string><json:string>cuxrcdp repression</json:string><json:string>cell cycle</json:string><json:string>nuclear factor</json:string><json:string>mouse testis</json:string><json:string>mouse fibroblasts</json:string><json:string>ectopic expression</json:string><json:string>internal control</json:string><json:string>nuclear extracts</json:string><json:string>amino acids</json:string><json:string>emsa supershift assays</json:string><json:string>murine lung</json:string><json:string>cuxrcdp proteins</json:string><json:string>homeodomain protein</json:string><json:string>unrelated control</json:string><json:string>nuclear protein</json:string><json:string>nucleic acids</json:string><json:string>bacterial extracts</json:string></teeft></keywords><author><json:item><name>Nadia A Higgy</name><affiliations><json:string>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</json:string></affiliations></json:item><json:item><name>Heide A Tarnasky</name><affiliations><json:string>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</json:string></affiliations></json:item><json:item><name>Isabelle Valarché</name><affiliations><json:string>Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</json:string></affiliations></json:item><json:item><name>Alain Nepveu</name><affiliations><json:string>Molecular Oncology Group Departments of Medicine and Oncology McGill University, Royal Victoria Hospital Montreal, Quebec, Canada H3A 1A1</json:string></affiliations></json:item><json:item><name>Frans A van der Hoorn</name><affiliations><json:string>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Testis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>c-mos</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cux homeodomain protein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Homeodomain</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Transcription regulation</value></json:item></subject><arkIstex>ark:/67375/6H6-34LPBCB5-D</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The c-mos gene is transcribed in male and female germ cells, in differentiating myoblasts and in 3T3 cells from cell-specific promoters. We characterized the rat testis promoter, which contains a TATA-box and one binding site for a testis-specific transcription factor TTF-D, as well as a region which can act as enhancer, which is located approx. 2 kb upstream of the c-mos AUG start codon. It binds three factors at sites I, II and III as determined in DNAse I footprint assays. We demonstrated that a member of the NF-1/CTF family of transcription factors binds site II. Here we report the cloning of the protein that binds to enhancer site III. This protein is the rat homolog of human hCut/CDP, mouse Cux/CDP and canine Clox. hCut/Cux/CDP/Clox (hereafter called Cux/CDP), a 160 kDa protein containing multiple repeats and a homeodomain, negatively regulates the mammalian c-myc, gp91-phox and N-Cam genes. Using bacterially produced murine GST-Cux fusion proteins and GST-Cux deletion mutants, we find that Cux repeat CR3 and the homeodomain are both required for efficient binding to enhancer site III. Mouse lung and testis nuclear Cux/CDP bind to site III as determined in electrophoretic gel mobility supershift assays using two different anti-hCut specific monoclonal antibodies. Transfections of CAT constructs containing the enhancer fragment linked to a minimal promoter demonstrated that Cux/CDP represses c-mos enhancer activity.</abstract><qualityIndicators><score>9.676</score><pdfWordCount>6451</pdfWordCount><pdfCharCount>38338</pdfCharCount><pdfVersion>1.1</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>595 x 763 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>223</abstractWordCount><abstractCharCount>1454</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity</title><pmid><json:string>9130595</json:string></pmid><pii><json:string>S0167-4781(96)00221-7</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>BBA - Gene Structure and Expression</title><language><json:string>unknown</json:string></language><publicationDate>1997</publicationDate><issn><json:string>0167-4781</json:string></issn><pii><json:string>S0167-4781(00)X0033-4</json:string></pii><volume>1351</volume><issue>3</issue><pages><first>313</first><last>324</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1997</json:string></date><geogName><json:string>region of Cux</json:string></geogName><orgName><json:string>Royal Victoria Hospital Montreal, Quebec, Canada H</json:string><json:string>Biotech</json:string><json:string>Hubrecht Laboratory, Netherlands Institute</json:string><json:string>Netherlands Molecular Oncology Group Departments of Medicine and Oncology</json:string><json:string>National Cancer Institute of Canada</json:string><json:string>Edith Weiss Memorial Endowment</json:string><json:string>Hugo</json:string><json:string>Medical Research Council of Canada</json:string></orgName><orgName_funder><json:string>National Cancer Institute of Canada</json:string><json:string>Edith Weiss Memorial Endowment</json:string><json:string>Hugo</json:string><json:string>Medical Research Council of Canada</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>R. Gupta</json:string><json:string>Transfections</json:string><json:string>Higgy</json:string><json:string>B. Kuhnel</json:string></persName><placeName><json:string>Utrecht</json:string><json:string>Calgary</json:string><json:string>Philadelphia</json:string><json:string>PA</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>N.A. Higgy et al.</json:string><json:string>Fox Chase Cancer Center, 7701</json:string><json:string>Sambrook et al.</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-34LPBCB5-D</json:string></ark><categories><wos></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular 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 - Genetics</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biophysics</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Structural 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><json:string>4 - biologie moleculaire et cellulaire</json:string></inist></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1016/S0167-4781(96)00221-7</json:string></doi><id>88A9C5DE24BAA56AA38A5FA7A9BD3A5624679A22</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-34LPBCB5-D/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-34LPBCB5-D/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-34LPBCB5-D/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>©1997 Elsevier Science B.V.</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</p></availability><date>1997</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">Fig. 1: Binding of testis nuclear proteins to the c-mos enhancer. (A) Schematic representation of the c-mos locus. Indicated are mos elements derived from rat and mouse: the c-mos coding region (orf), the c-mos enhancer, the myoblast enhancer, the rat inhibitory sequences RIS, the mouse inhibitory sequence UMS and the repressor element, as well as the four identified promoters. We previously determined that the mos enhancer binds murine fibroblast nuclear proteins on sites I, II and III (the sequence of DNAse I footprint region III is indicated). The indicated base changes were introduced to generate a mutant site III. (B) The rat mos enhancer was end-labeled on the coding strand and analyzed in DNAse I footprint assays using no protein, or 10 μg and 50 μg of rat testis nuclear proteins. Indicated are footprint regions II and III and three DNAse I hypersensitive sites (arrowheads).</note><note type="content">Fig. 2: The nuclear protein binding to site III is a Cut homolog. The inserts from phages that express a site-III-binding protein were sequenced, which indicated that they were identical to the published partial rat CDP2 cDNA [31]. Mammalian Cux/CDP homologs are schematically represented and compared to Drosophila Cut: indicated are conserved putative coiled-coil structures (CC), conserved Cut repeats CR1-CR3 and the homeodomain (HD). Also indicated is the extent of the inserts of phages that react with site III oligo, and the regions that were deleted from the murine Cux/CDP protein to generate two Cux/CDP deletion mutants used in DNA binding studies.</note><note type="content">Fig. 3: Bacterially produced Cux/CDP binds site III oligo. EMSA was used to analyze the interaction of bacterially produced GST-Cux fusion protein with the site III oligo. Reactions were done with radiolabeled site III oligo and either no protein (lane 1), or bacterial extracts containing GST-Cux (lanes 2–8), GST (lane 9), GST-ΔCR3Cux, which lacks the Cut repeat 3 and homeodomain (lane 10) and GST-ΔHDCux, which lacks the homeodomain (lane 11). Binding reactions shown in lanes 3–5 contained 100, 300 and 500 mM NaCl, respectively. Reactions in lanes 6–8 contained a 100-fold molar excess of unlabelled ds site III oligo, mutant site III oligo or of an unrelated oligo, respectively. The site III-Cux DNA-protein complex is indicated by the arrow, while a non-specific complex due to an uncharacterized bacterial protein is indicated by the star.</note><note type="content">Fig. 4: Recognition of Cux/CDP and hCut by MAb A and W3. Human HL60 cells (untreated or treated with retinoic acid (RA)) and 293 cells (plus a transformed subclone 293-T), mouse MEL cells, mouse NIH3T3 fibroblasts and rat FR3T3 fibroblasts were metabolically labelled with [35S]methionine, cells were lysed and Cux/CDP proteins were immunoprecipitated using the A (lanes 1–4) and W3 (lanes 5–7) monoclonal antibodies. Molecular weight markers are indicated.</note><note type="content">Fig. 5: Binding of mouse lung and testis Cux/CDP to site III. To further analyze the binding of Cux/CDP present in nuclear extracts isolated from mouse lung (lanes 2–8) and mouse testis (lanes 10–16), we carried out EMSA-supershift assays, using radiolabeled site III oligo as probe and the following monoclonal antibodies: an unrelated control monoclonal antibody AB2 (lanes 3, 4, 11 and 12), Cux/CDP-specific monoclonal antibody A (lanes 5, 6, 13 and 14) and the second Cux/CDP-specific monoclonal antibody W3 (lanes 7, 8, 15 and 16). Control reactions contained no nuclear protein (lanes 1 and 9) or mouse nuclear lung and testis extracts and antibody buffer (lanes 2 and 10, respectively). Monoclonal antibodies were used in two amounts: 1.5 μl (lanes 3, 5, 7, 11, 13 and 15) and 5.5 μl (lanes 4, 6, 8, 12, 14 and 16). Reactions were separated on 5% native polyacrylamide gels.</note><note type="content">Fig. 6: Repression of enhancer activity by Cux/CDP. Transient transfections were carried out to analyze the effect of Cux/CDP on enhancer activity. The reporter plasmid was pWT1-CAT containing the enhancer linked to a minimal tk promoter and the CAT gene (lanes 2–4, 6, 7), pRSV-CAT containing the RSV LTR linked to CAT (lane 5) and pBLCAT2 containing a minimal tk promoter linked to the CAT gene without any enhancer (lane 1). Increasing amounts of pRc/CṀVCuxFL containing the CMV promoter linked to murine Cux/CDP were co-transfected in experiments shown in lanes 3 and 4 as indicated. Transfections shown in lanes 6 and 7 repeated the condition shown in lane 4 and contained in addition a 10-fold molar excess of site III (in pBS-wt) and of mutant site III (in pBS-mut) as competitors.</note><note type="content">Table 1: Repression of enhancer activity by Cux/CDP</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity</title><author xml:id="author-0000"><persName><forename type="first">Nadia A</forename><surname>Higgy</surname></persName><note type="biography">Present address: Fox Chase Cancer Center, 7701 Burholme Ave, Philadelphia, PA 19111, USA.</note><affiliation>Present address: Fox Chase Cancer Center, 7701 Burholme Ave, Philadelphia, PA 19111, USA.</affiliation><affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Heide A</forename><surname>Tarnasky</surname></persName><affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Isabelle</forename><surname>Valarché</surname></persName><affiliation>Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Alain</forename><surname>Nepveu</surname></persName><affiliation>Molecular Oncology Group Departments of Medicine and Oncology McGill University, Royal Victoria Hospital Montreal, Quebec, Canada H3A 1A1</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Frans A</forename><surname>van der Hoorn</surname></persName><affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</affiliation></author><idno type="istex">88A9C5DE24BAA56AA38A5FA7A9BD3A5624679A22</idno><idno type="ark">ark:/67375/6H6-34LPBCB5-D</idno><idno type="DOI">10.1016/S0167-4781(96)00221-7</idno><idno type="PII">S0167-4781(96)00221-7</idno></analytic><monogr><title level="j">BBA - Gene Structure and Expression</title><title level="j" type="abbrev">BBAEXP</title><idno type="pISSN">0167-4781</idno><idno type="PII">S0167-4781(00)X0033-4</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">1351</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="313">313</biblScope><biblScope unit="page" to="324">324</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The c-mos gene is transcribed in male and female germ cells, in differentiating myoblasts and in 3T3 cells from cell-specific promoters. We characterized the rat testis promoter, which contains a TATA-box and one binding site for a testis-specific transcription factor TTF-D, as well as a region which can act as enhancer, which is located approx. 2 kb upstream of the c-mos AUG start codon. It binds three factors at sites I, II and III as determined in DNAse I footprint assays. We demonstrated that a member of the NF-1/CTF family of transcription factors binds site II. Here we report the cloning of the protein that binds to enhancer site III. This protein is the rat homolog of human hCut/CDP, mouse Cux/CDP and canine Clox. hCut/Cux/CDP/Clox (hereafter called Cux/CDP), a 160 kDa protein containing multiple repeats and a homeodomain, negatively regulates the mammalian c-myc, gp91-phox and N-Cam genes. Using bacterially produced murine GST-Cux fusion proteins and GST-Cux deletion mutants, we find that Cux repeat CR3 and the homeodomain are both required for efficient binding to enhancer site III. Mouse lung and testis nuclear Cux/CDP bind to site III as determined in electrophoretic gel mobility supershift assays using two different anti-hCut specific monoclonal antibodies. Transfections of CAT constructs containing the enhancer fragment linked to a minimal promoter demonstrated that Cux/CDP represses c-mos enhancer activity.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Testis</term></item><item><term>c-mos</term></item><item><term>Cux homeodomain protein</term></item><item><term>Homeodomain</term></item><item><term>Transcription regulation</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1996-10-30">Modified</change><change when="1997">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-34LPBCB5-D/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: ce:floats; body; 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:entity SYSTEM="gr1" NDATA="IMAGE" name="gr1"></istex:entity><istex:entity SYSTEM="gr2" NDATA="IMAGE" name="gr2"></istex:entity><istex:entity SYSTEM="gr3" NDATA="IMAGE" name="gr3"></istex:entity><istex:entity SYSTEM="gr4" NDATA="IMAGE" name="gr4"></istex:entity><istex:entity SYSTEM="gr5" NDATA="IMAGE" name="gr5"></istex:entity><istex:entity SYSTEM="gr6" NDATA="IMAGE" name="gr6"></istex:entity></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>BBAEXP</jid><aid>92968</aid><ce:pii>S0167-4781(96)00221-7</ce:pii><ce:doi>10.1016/S0167-4781(96)00221-7</ce:doi><ce:copyright year="1997" type="full-transfer">Elsevier Science B.V.</ce:copyright></item-info><head><ce:title><ce:italic>Cux/CDP</ce:italic> homeodomain protein binds to an enhancer in the rat c-<ce:italic>mos</ce:italic> locus and represses its activity</ce:title><ce:author-group><ce:author><ce:given-name>Nadia A</ce:given-name><ce:surname>Higgy</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Heide A</ce:given-name><ce:surname>Tarnasky</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref></ce:author><ce:author><ce:given-name>Isabelle</ce:given-name><ce:surname>Valarché</ce:surname><ce:cross-ref refid="AFF2">b</ce:cross-ref></ce:author><ce:author><ce:given-name>Alain</ce:given-name><ce:surname>Nepveu</ce:surname><ce:cross-ref refid="AFF3">c</ce:cross-ref></ce:author><ce:author><ce:given-name>Frans A</ce:given-name><ce:surname>van der Hoorn</ce:surname><ce:cross-ref refid="AFF1">a</ce:cross-ref><ce:cross-ref refid="CORR1">*</ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Molecular Oncology Group Departments of Medicine and Oncology McGill University, Royal Victoria Hospital Montreal, Quebec, Canada H3A 1A1</ce:textfn></ce:affiliation><ce:correspondence id="CORR1"><ce:label>*</ce:label><ce:text>Corresponding author. Fax: +1 (403) 2838727. E-mail: fvdhoorn@acs.ucalgary.ca</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>1</ce:label><ce:note-para>Present address: Fox Chase Cancer Center, 7701 Burholme Ave, Philadelphia, PA 19111, USA.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="19" month="6" year="1996"></ce:date-received><ce:date-revised day="30" month="10" year="1996"></ce:date-revised><ce:date-accepted day="30" month="10" year="1996"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The c-<ce:italic>mos</ce:italic> gene is transcribed in male and female germ cells, in differentiating myoblasts and in 3T3 cells from cell-specific promoters. We characterized the rat testis promoter, which contains a TATA-box and one binding site for a testis-specific transcription factor TTF-D, as well as a region which can act as enhancer, which is located approx. 2 kb upstream of the c-<ce:italic>mos</ce:italic> AUG start codon. It binds three factors at sites I, II and III as determined in DNAse I footprint assays. We demonstrated that a member of the NF-1/CTF family of transcription factors binds site II. Here we report the cloning of the protein that binds to enhancer site III. This protein is the rat homolog of human hCut/CDP, mouse Cux/CDP and canine Clox. hCut/Cux/CDP/Clox (hereafter called Cux/CDP), a 160 kDa protein containing multiple repeats and a homeodomain, negatively regulates the mammalian c-<ce:italic>myc</ce:italic>, gp91-phox and N-Cam genes. Using bacterially produced murine GST-Cux fusion proteins and GST-Cux deletion mutants, we find that Cux repeat CR3 and the homeodomain are both required for efficient binding to enhancer site III. Mouse lung and testis nuclear Cux/CDP bind to site III as determined in electrophoretic gel mobility supershift assays using two different anti-hCut specific monoclonal antibodies. Transfections of CAT constructs containing the enhancer fragment linked to a minimal promoter demonstrated that Cux/CDP represses c-<ce:italic>mos</ce:italic> enhancer activity.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Testis</ce:text></ce:keyword><ce:keyword><ce:text>c-<ce:italic>mos</ce:italic></ce:text></ce:keyword><ce:keyword><ce:text>Cux homeodomain protein</ce:text></ce:keyword><ce:keyword><ce:text>Homeodomain</ce:text></ce:keyword><ce:keyword><ce:text>Transcription regulation</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Cux/CDP homeodomain protein binds to an enhancer in the rat c- mos locus and represses its activity</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>homeodomain protein binds to an enhancer in the rat c-</title></titleInfo><name type="personal"><namePart type="given">Nadia A</namePart><namePart type="family">Higgy</namePart><affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</affiliation><description>Present address: Fox Chase Cancer Center, 7701 Burholme Ave, Philadelphia, PA 19111, USA.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Heide A</namePart><namePart type="family">Tarnasky</namePart><affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Isabelle</namePart><namePart type="family">Valarché</namePart><affiliation>Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alain</namePart><namePart type="family">Nepveu</namePart><affiliation>Molecular Oncology Group Departments of Medicine and Oncology McGill University, Royal Victoria Hospital Montreal, Quebec, Canada H3A 1A1</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Frans A</namePart><namePart type="family">van der Hoorn</namePart><affiliation>Department of Medical Biochemistry, University of Calgary, 3330 Hospital Drive, N.W., Calgary, Alberta, Canada T2N 4N1</affiliation><description>Corresponding author. Fax: +1 (403) 2838727. E-mail: fvdhoorn@acs.ucalgary.ca</description><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">1997</dateIssued><dateModified encoding="w3cdtf">1996-10-30</dateModified><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The c-mos gene is transcribed in male and female germ cells, in differentiating myoblasts and in 3T3 cells from cell-specific promoters. We characterized the rat testis promoter, which contains a TATA-box and one binding site for a testis-specific transcription factor TTF-D, as well as a region which can act as enhancer, which is located approx. 2 kb upstream of the c-mos AUG start codon. It binds three factors at sites I, II and III as determined in DNAse I footprint assays. We demonstrated that a member of the NF-1/CTF family of transcription factors binds site II. Here we report the cloning of the protein that binds to enhancer site III. This protein is the rat homolog of human hCut/CDP, mouse Cux/CDP and canine Clox. hCut/Cux/CDP/Clox (hereafter called Cux/CDP), a 160 kDa protein containing multiple repeats and a homeodomain, negatively regulates the mammalian c-myc, gp91-phox and N-Cam genes. Using bacterially produced murine GST-Cux fusion proteins and GST-Cux deletion mutants, we find that Cux repeat CR3 and the homeodomain are both required for efficient binding to enhancer site III. Mouse lung and testis nuclear Cux/CDP bind to site III as determined in electrophoretic gel mobility supershift assays using two different anti-hCut specific monoclonal antibodies. Transfections of CAT constructs containing the enhancer fragment linked to a minimal promoter demonstrated that Cux/CDP represses c-mos enhancer activity.</abstract><note type="content">Fig. 1: Binding of testis nuclear proteins to the c-mos enhancer. (A) Schematic representation of the c-mos locus. Indicated are mos elements derived from rat and mouse: the c-mos coding region (orf), the c-mos enhancer, the myoblast enhancer, the rat inhibitory sequences RIS, the mouse inhibitory sequence UMS and the repressor element, as well as the four identified promoters. We previously determined that the mos enhancer binds murine fibroblast nuclear proteins on sites I, II and III (the sequence of DNAse I footprint region III is indicated). The indicated base changes were introduced to generate a mutant site III. (B) The rat mos enhancer was end-labeled on the coding strand and analyzed in DNAse I footprint assays using no protein, or 10 μg and 50 μg of rat testis nuclear proteins. Indicated are footprint regions II and III and three DNAse I hypersensitive sites (arrowheads).</note><note type="content">Fig. 2: The nuclear protein binding to site III is a Cut homolog. The inserts from phages that express a site-III-binding protein were sequenced, which indicated that they were identical to the published partial rat CDP2 cDNA [31]. Mammalian Cux/CDP homologs are schematically represented and compared to Drosophila Cut: indicated are conserved putative coiled-coil structures (CC), conserved Cut repeats CR1-CR3 and the homeodomain (HD). Also indicated is the extent of the inserts of phages that react with site III oligo, and the regions that were deleted from the murine Cux/CDP protein to generate two Cux/CDP deletion mutants used in DNA binding studies.</note><note type="content">Fig. 3: Bacterially produced Cux/CDP binds site III oligo. EMSA was used to analyze the interaction of bacterially produced GST-Cux fusion protein with the site III oligo. Reactions were done with radiolabeled site III oligo and either no protein (lane 1), or bacterial extracts containing GST-Cux (lanes 2–8), GST (lane 9), GST-ΔCR3Cux, which lacks the Cut repeat 3 and homeodomain (lane 10) and GST-ΔHDCux, which lacks the homeodomain (lane 11). Binding reactions shown in lanes 3–5 contained 100, 300 and 500 mM NaCl, respectively. Reactions in lanes 6–8 contained a 100-fold molar excess of unlabelled ds site III oligo, mutant site III oligo or of an unrelated oligo, respectively. The site III-Cux DNA-protein complex is indicated by the arrow, while a non-specific complex due to an uncharacterized bacterial protein is indicated by the star.</note><note type="content">Fig. 4: Recognition of Cux/CDP and hCut by MAb A and W3. Human HL60 cells (untreated or treated with retinoic acid (RA)) and 293 cells (plus a transformed subclone 293-T), mouse MEL cells, mouse NIH3T3 fibroblasts and rat FR3T3 fibroblasts were metabolically labelled with [35S]methionine, cells were lysed and Cux/CDP proteins were immunoprecipitated using the A (lanes 1–4) and W3 (lanes 5–7) monoclonal antibodies. Molecular weight markers are indicated.</note><note type="content">Fig. 5: Binding of mouse lung and testis Cux/CDP to site III. To further analyze the binding of Cux/CDP present in nuclear extracts isolated from mouse lung (lanes 2–8) and mouse testis (lanes 10–16), we carried out EMSA-supershift assays, using radiolabeled site III oligo as probe and the following monoclonal antibodies: an unrelated control monoclonal antibody AB2 (lanes 3, 4, 11 and 12), Cux/CDP-specific monoclonal antibody A (lanes 5, 6, 13 and 14) and the second Cux/CDP-specific monoclonal antibody W3 (lanes 7, 8, 15 and 16). Control reactions contained no nuclear protein (lanes 1 and 9) or mouse nuclear lung and testis extracts and antibody buffer (lanes 2 and 10, respectively). Monoclonal antibodies were used in two amounts: 1.5 μl (lanes 3, 5, 7, 11, 13 and 15) and 5.5 μl (lanes 4, 6, 8, 12, 14 and 16). Reactions were separated on 5% native polyacrylamide gels.</note><note type="content">Fig. 6: Repression of enhancer activity by Cux/CDP. Transient transfections were carried out to analyze the effect of Cux/CDP on enhancer activity. The reporter plasmid was pWT1-CAT containing the enhancer linked to a minimal tk promoter and the CAT gene (lanes 2–4, 6, 7), pRSV-CAT containing the RSV LTR linked to CAT (lane 5) and pBLCAT2 containing a minimal tk promoter linked to the CAT gene without any enhancer (lane 1). Increasing amounts of pRc/CṀVCuxFL containing the CMV promoter linked to murine Cux/CDP were co-transfected in experiments shown in lanes 3 and 4 as indicated. Transfections shown in lanes 6 and 7 repeated the condition shown in lane 4 and contained in addition a 10-fold molar excess of site III (in pBS-wt) and of mutant site III (in pBS-mut) as competitors.</note><note type="content">Table 1: Repression of enhancer activity by Cux/CDP</note><subject><genre>Keywords</genre><topic>Testis</topic><topic>c-mos</topic><topic>Cux homeodomain protein</topic><topic>Homeodomain</topic><topic>Transcription regulation</topic></subject><relatedItem type="host"><titleInfo><title>BBA - Gene Structure and Expression</title></titleInfo><titleInfo type="abbreviated"><title>BBAEXP</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">1997</dateIssued></originInfo><identifier type="ISSN">0167-4781</identifier><identifier type="PII">S0167-4781(00)X0033-4</identifier><part><date>1997</date><detail type="volume"><number>1351</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue-pages"><start>249</start><end>364</end></extent><extent unit="pages"><start>313</start><end>324</end></extent></part></relatedItem><identifier type="istex">88A9C5DE24BAA56AA38A5FA7A9BD3A5624679A22</identifier><identifier type="ark">ark:/67375/6H6-34LPBCB5-D</identifier><identifier type="DOI">10.1016/S0167-4781(96)00221-7</identifier><identifier type="PII">S0167-4781(96)00221-7</identifier><accessCondition type="use and reproduction" contentType="copyright">©1997 Elsevier Science B.V.</accessCondition><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><recordOrigin>Elsevier Science B.V., ©1997</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-34LPBCB5-D/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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