Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence
A DNA binding and dimerization motif, with apparent amphipathic helices (the HLH motif), has recently been identified in various proteins, including two that bind to immunoglobulin enhancers (E12 and E47). We show here that various HLH proteins can bind as apparent heterodimers to a single DNA motif...
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| Veröffentlicht in: | Cell 1989-08, Vol.58 (3), p.537-544 |
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| creator | Murre, Cornelis McCaw, Patrick Schonleber Vaessin, H. Caudy, M. Jan, L.Y. Jan, Y.N. Cabrera, Carlos V. Buskin, Jean N. Hauschka, Stephen D. Lassar, Andrew B. Weintraub, Harold Baltimore, David |
| description | A DNA binding and dimerization motif, with apparent amphipathic helices (the HLH motif), has recently been identified in various proteins, including two that bind to immunoglobulin enhancers (E12 and E47). We show here that various HLH proteins can bind as apparent heterodimers to a single DNA motif and also, albeit usually more weakly, as apparent homodimers. The HLH domain can mediate heterodimer formation between either
daughterless, E12, or E47 (Class A) and
achaete-scute T3 or
MyoD (Class B) to form proteins with high affinity for the κE2 site in the immunoglobulin kappa chain enhancer. The
achaete-scute T3 and
MyoD proteins do not form κE2-binding heterodimers together, and no active complex with N-
myc was evident. The formation of a heterodimer between the
daughterless and
achaete-scute T3 products may explain the similar phenotypes of mutants at these two loci and the genetic interactions between them. A role of E12 and E47 in mammalian development, analogous to that of
daughterless in Drosophila, is likely. |
| doi_str_mv | 10.1016/0092-8674(89)90434-0 |
| format | Article |
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daughterless, E12, or E47 (Class A) and
achaete-scute T3 or
MyoD (Class B) to form proteins with high affinity for the κE2 site in the immunoglobulin kappa chain enhancer. The
achaete-scute T3 and
MyoD proteins do not form κE2-binding heterodimers together, and no active complex with N-
myc was evident. The formation of a heterodimer between the
daughterless and
achaete-scute T3 products may explain the similar phenotypes of mutants at these two loci and the genetic interactions between them. A role of E12 and E47 in mammalian development, analogous to that of
daughterless in Drosophila, is likely.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(89)90434-0</identifier><identifier>PMID: 2503252</identifier><identifier>CODEN: CELLB5</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject>Animals ; Binding Sites ; Biological and medical sciences ; Creatine Kinase - genetics ; DNA - metabolism ; DNA-Binding Proteins - classification ; DNA-Binding Proteins - metabolism ; DNA-Binding Proteins - ultrastructure ; Drosophila melanogaster - genetics ; Enhancer Elements, Genetic ; Fundamental and applied biological sciences. Psychology ; Genes, Immunoglobulin ; Interactions. Associations ; Intermolecular phenomena ; Macromolecular Substances ; Molecular biophysics ; Protein Binding ; Protein Biosynthesis ; Protein Conformation ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Transcription Factors - classification ; Transcription Factors - metabolism ; Transcription Factors - ultrastructure</subject><ispartof>Cell, 1989-08, Vol.58 (3), p.537-544</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-2f7c33524ec8e1952fceb5d98ad44d01fc7a3164a637d732c4dd7681e1abee053</citedby><cites>FETCH-LOGICAL-c417t-2f7c33524ec8e1952fceb5d98ad44d01fc7a3164a637d732c4dd7681e1abee053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0092867489904340$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6851965$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2503252$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murre, Cornelis</creatorcontrib><creatorcontrib>McCaw, Patrick Schonleber</creatorcontrib><creatorcontrib>Vaessin, H.</creatorcontrib><creatorcontrib>Caudy, M.</creatorcontrib><creatorcontrib>Jan, L.Y.</creatorcontrib><creatorcontrib>Jan, Y.N.</creatorcontrib><creatorcontrib>Cabrera, Carlos V.</creatorcontrib><creatorcontrib>Buskin, Jean N.</creatorcontrib><creatorcontrib>Hauschka, Stephen D.</creatorcontrib><creatorcontrib>Lassar, Andrew B.</creatorcontrib><creatorcontrib>Weintraub, Harold</creatorcontrib><creatorcontrib>Baltimore, David</creatorcontrib><title>Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence</title><title>Cell</title><addtitle>Cell</addtitle><description>A DNA binding and dimerization motif, with apparent amphipathic helices (the HLH motif), has recently been identified in various proteins, including two that bind to immunoglobulin enhancers (E12 and E47). We show here that various HLH proteins can bind as apparent heterodimers to a single DNA motif and also, albeit usually more weakly, as apparent homodimers. The HLH domain can mediate heterodimer formation between either
daughterless, E12, or E47 (Class A) and
achaete-scute T3 or
MyoD (Class B) to form proteins with high affinity for the κE2 site in the immunoglobulin kappa chain enhancer. The
achaete-scute T3 and
MyoD proteins do not form κE2-binding heterodimers together, and no active complex with N-
myc was evident. The formation of a heterodimer between the
daughterless and
achaete-scute T3 products may explain the similar phenotypes of mutants at these two loci and the genetic interactions between them. A role of E12 and E47 in mammalian development, analogous to that of
daughterless in Drosophila, is likely.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Creatine Kinase - genetics</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - classification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>DNA-Binding Proteins - ultrastructure</subject><subject>Drosophila melanogaster - genetics</subject><subject>Enhancer Elements, Genetic</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Immunoglobulin</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Macromolecular Substances</subject><subject>Molecular biophysics</subject><subject>Protein Binding</subject><subject>Protein Biosynthesis</subject><subject>Protein Conformation</subject><subject>Regulatory Sequences, Nucleic Acid</subject><subject>Structure-Activity Relationship</subject><subject>Transcription Factors - classification</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription Factors - ultrastructure</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctu1DAUhi1EVYbCG4DkBUKwCPga25tKVbm0UgUbWFuOfdIaJXGIPdBu-uw4ndEsy8qX853L_x-EXlHygRLafiTEsEa3SrzT5r0hgouGPEEbSoxqBFXsKdockGfoec6_CCFaSnmMjpkknEm2QfeXU4HF-RLTlHEH5S_AhG-gfqYhXadtro8h3jZDSnPzcMXzkgrEil_DVHMLYJ_GeYBbyLjcuIK7OAWcZ_Cxj94Nwx0uCbuVGtOEP307wxl-b2Hy8AId9W7I8HJ_nqCfXz7_OL9orr5_vTw_u2p8VVIa1ivPuWQCvAZqJOs9dDIY7YIQgdDeK8dpK1zLVVCceRGCajUF6joAIvkJerurW2evnXOxY8wehsFNUDVaZSjjTJv_glRKLblRFRQ70C8p5wV6Oy9xdMudpcSu-7Gr-XY132pjH_ZjSU17va-_7UYIh6T9Qmr8zT7ucrWuX9zkYz5grZbUtKue0x0G1bQ_ERabfVwNDXEBX2xI8fE5_gG76a5s</recordid><startdate>19890811</startdate><enddate>19890811</enddate><creator>Murre, Cornelis</creator><creator>McCaw, Patrick Schonleber</creator><creator>Vaessin, H.</creator><creator>Caudy, M.</creator><creator>Jan, L.Y.</creator><creator>Jan, Y.N.</creator><creator>Cabrera, Carlos V.</creator><creator>Buskin, Jean N.</creator><creator>Hauschka, Stephen D.</creator><creator>Lassar, Andrew B.</creator><creator>Weintraub, Harold</creator><creator>Baltimore, David</creator><general>Elsevier Inc</general><general>Cell Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19890811</creationdate><title>Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence</title><author>Murre, Cornelis ; McCaw, Patrick Schonleber ; Vaessin, H. ; Caudy, M. ; Jan, L.Y. ; Jan, Y.N. ; Cabrera, Carlos V. ; Buskin, Jean N. ; Hauschka, Stephen D. ; Lassar, Andrew B. ; Weintraub, Harold ; Baltimore, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-2f7c33524ec8e1952fceb5d98ad44d01fc7a3164a637d732c4dd7681e1abee053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Creatine Kinase - genetics</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - classification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>DNA-Binding Proteins - ultrastructure</topic><topic>Drosophila melanogaster - genetics</topic><topic>Enhancer Elements, Genetic</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Immunoglobulin</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Macromolecular Substances</topic><topic>Molecular biophysics</topic><topic>Protein Binding</topic><topic>Protein Biosynthesis</topic><topic>Protein Conformation</topic><topic>Regulatory Sequences, Nucleic Acid</topic><topic>Structure-Activity Relationship</topic><topic>Transcription Factors - classification</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription Factors - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murre, Cornelis</creatorcontrib><creatorcontrib>McCaw, Patrick Schonleber</creatorcontrib><creatorcontrib>Vaessin, H.</creatorcontrib><creatorcontrib>Caudy, M.</creatorcontrib><creatorcontrib>Jan, L.Y.</creatorcontrib><creatorcontrib>Jan, Y.N.</creatorcontrib><creatorcontrib>Cabrera, Carlos V.</creatorcontrib><creatorcontrib>Buskin, Jean N.</creatorcontrib><creatorcontrib>Hauschka, Stephen D.</creatorcontrib><creatorcontrib>Lassar, Andrew B.</creatorcontrib><creatorcontrib>Weintraub, Harold</creatorcontrib><creatorcontrib>Baltimore, David</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murre, Cornelis</au><au>McCaw, Patrick Schonleber</au><au>Vaessin, H.</au><au>Caudy, M.</au><au>Jan, L.Y.</au><au>Jan, Y.N.</au><au>Cabrera, Carlos V.</au><au>Buskin, Jean N.</au><au>Hauschka, Stephen D.</au><au>Lassar, Andrew B.</au><au>Weintraub, Harold</au><au>Baltimore, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1989-08-11</date><risdate>1989</risdate><volume>58</volume><issue>3</issue><spage>537</spage><epage>544</epage><pages>537-544</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>A DNA binding and dimerization motif, with apparent amphipathic helices (the HLH motif), has recently been identified in various proteins, including two that bind to immunoglobulin enhancers (E12 and E47). We show here that various HLH proteins can bind as apparent heterodimers to a single DNA motif and also, albeit usually more weakly, as apparent homodimers. The HLH domain can mediate heterodimer formation between either
daughterless, E12, or E47 (Class A) and
achaete-scute T3 or
MyoD (Class B) to form proteins with high affinity for the κE2 site in the immunoglobulin kappa chain enhancer. The
achaete-scute T3 and
MyoD proteins do not form κE2-binding heterodimers together, and no active complex with N-
myc was evident. The formation of a heterodimer between the
daughterless and
achaete-scute T3 products may explain the similar phenotypes of mutants at these two loci and the genetic interactions between them. A role of E12 and E47 in mammalian development, analogous to that of
daughterless in Drosophila, is likely.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>2503252</pmid><doi>10.1016/0092-8674(89)90434-0</doi><tpages>8</tpages></addata></record> |
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| ispartof | Cell, 1989-08, Vol.58 (3), p.537-544 |
| issn | 0092-8674 1097-4172 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79123289 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Binding Sites Biological and medical sciences Creatine Kinase - genetics DNA - metabolism DNA-Binding Proteins - classification DNA-Binding Proteins - metabolism DNA-Binding Proteins - ultrastructure Drosophila melanogaster - genetics Enhancer Elements, Genetic Fundamental and applied biological sciences. Psychology Genes, Immunoglobulin Interactions. Associations Intermolecular phenomena Macromolecular Substances Molecular biophysics Protein Binding Protein Biosynthesis Protein Conformation Regulatory Sequences, Nucleic Acid Structure-Activity Relationship Transcription Factors - classification Transcription Factors - metabolism Transcription Factors - ultrastructure |
| title | Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence |
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