Binding preferences of the POU domain protein Brain-4: implications for autoregulation
The POU domain-containing transcription factor Brain-4 (Brn-4, RHS-2) was examined for its sites of expression and DNA binding preferences. In the rat, Brn-4 is expressed in 76 and 65% of vasopressin neurons in the paraventricular and supraoptic nuclei, respectively; but in only 10% of corticotropin...
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| Veröffentlicht in: | Brain research. Molecular brain research. 1996-06, Vol.38 (2), p.209-221 |
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| creator | Malik, Karl F. Kim, Jin Hartman, Adam L. Kim, Paul Scott Young, W. |
| description | The POU domain-containing transcription factor Brain-4 (Brn-4, RHS-2) was examined for its sites of expression and DNA binding preferences. In the rat, Brn-4 is expressed in 76 and 65% of vasopressin neurons in the paraventricular and supraoptic nuclei, respectively; but in only 10% of corticotropin-releasing factor neurons in the paraventricular nucleus of the hypothalamus. From these data we speculate that genes expressed within vasopressingergic neurons are more likely to be regulated by Brn-4 than those in corticotropin-releasing factor neurons. Random oligonucleotide site selection indicates Brn-4 prefers binding the DNA element CAATATGCTAAT and is inflexible in its spacing requirement between putative CAATAT and TAAT half sites, preferring 2 nucleotides between these elements. Electrophoretic mobility shift and DNase I footprinting analyses show five regions between nucleotides −457 and +22 of the Brn-4 promoter that are bound by Brn-4. Furthermore, Brn-4 can transactivate from this region of the Brn-4 promoter, suggesting that Brn-4 expression may be autoregulated. |
| doi_str_mv | 10.1016/0169-328X(95)00308-F |
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In the rat, Brn-4 is expressed in 76 and 65% of vasopressin neurons in the paraventricular and supraoptic nuclei, respectively; but in only 10% of corticotropin-releasing factor neurons in the paraventricular nucleus of the hypothalamus. From these data we speculate that genes expressed within vasopressingergic neurons are more likely to be regulated by Brn-4 than those in corticotropin-releasing factor neurons. Random oligonucleotide site selection indicates Brn-4 prefers binding the DNA element CAATATGCTAAT and is inflexible in its spacing requirement between putative CAATAT and TAAT half sites, preferring 2 nucleotides between these elements. Electrophoretic mobility shift and DNase I footprinting analyses show five regions between nucleotides −457 and +22 of the Brn-4 promoter that are bound by Brn-4. Furthermore, Brn-4 can transactivate from this region of the Brn-4 promoter, suggesting that Brn-4 expression may be autoregulated.</description><identifier>ISSN: 0169-328X</identifier><identifier>EISSN: 1872-6941</identifier><identifier>DOI: 10.1016/0169-328X(95)00308-F</identifier><identifier>PMID: 8793109</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adenine - chemistry ; Animals ; Autoregulation ; Biochemistry and metabolism ; Biological and medical sciences ; Central nervous system ; DNA Footprinting ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation - physiology ; Gene regulation ; Histocytochemistry ; Homeostasis ; Hypothalamus ; In Situ Hybridization ; Male ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Neuropeptide ; POU ; POU Domain Factors ; Promoter Regions, Genetic ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Rats, Sprague-Dawley ; Thymine - chemistry ; Transcription factor ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; Vertebrates: nervous system and sense organs</subject><ispartof>Brain research. Molecular brain research., 1996-06, Vol.38 (2), p.209-221</ispartof><rights>1996</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-9041015a9e9e2bbdde159ea7bae32efa62ba1a5c28e2a96a092491a1bb2325023</citedby><cites>FETCH-LOGICAL-c437t-9041015a9e9e2bbdde159ea7bae32efa62ba1a5c28e2a96a092491a1bb2325023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3127009$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8793109$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malik, Karl F.</creatorcontrib><creatorcontrib>Kim, Jin</creatorcontrib><creatorcontrib>Hartman, Adam L.</creatorcontrib><creatorcontrib>Kim, Paul</creatorcontrib><creatorcontrib>Scott Young, W.</creatorcontrib><title>Binding preferences of the POU domain protein Brain-4: implications for autoregulation</title><title>Brain research. Molecular brain research.</title><addtitle>Brain Res Mol Brain Res</addtitle><description>The POU domain-containing transcription factor Brain-4 (Brn-4, RHS-2) was examined for its sites of expression and DNA binding preferences. In the rat, Brn-4 is expressed in 76 and 65% of vasopressin neurons in the paraventricular and supraoptic nuclei, respectively; but in only 10% of corticotropin-releasing factor neurons in the paraventricular nucleus of the hypothalamus. From these data we speculate that genes expressed within vasopressingergic neurons are more likely to be regulated by Brn-4 than those in corticotropin-releasing factor neurons. Random oligonucleotide site selection indicates Brn-4 prefers binding the DNA element CAATATGCTAAT and is inflexible in its spacing requirement between putative CAATAT and TAAT half sites, preferring 2 nucleotides between these elements. Electrophoretic mobility shift and DNase I footprinting analyses show five regions between nucleotides −457 and +22 of the Brn-4 promoter that are bound by Brn-4. Furthermore, Brn-4 can transactivate from this region of the Brn-4 promoter, suggesting that Brn-4 expression may be autoregulated.</description><subject>Adenine - chemistry</subject><subject>Animals</subject><subject>Autoregulation</subject><subject>Biochemistry and metabolism</subject><subject>Biological and medical sciences</subject><subject>Central nervous system</subject><subject>DNA Footprinting</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation - physiology</subject><subject>Gene regulation</subject><subject>Histocytochemistry</subject><subject>Homeostasis</subject><subject>Hypothalamus</subject><subject>In Situ Hybridization</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred Strains</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neuropeptide</subject><subject>POU</subject><subject>POU Domain Factors</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Thymine - chemistry</subject><subject>Transcription factor</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0169-328X</issn><issn>1872-6941</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFLwzAUxoMoc07_A4UeRPRQTdJ2bTwIbjgVBvPgxFt4TV810jYzaQX_e9Nt7OghPPK-7z3e9yPklNFrRtn4xj8RRjx7vxTJFaURzcLZHhmyLOXhWMRsnwx3lkNy5NwXpZRljA3IIEtFxKgYkreJbgrdfAQriyVabBS6wJRB-4nBy2IZFKYG3XjVtOjrxPpfGN8Gul5VWkGrTeOC0tgAutZY_Oiqde-YHJRQOTzZ1hFZzh5ep0_hfPH4PL2fhyqO0jYUNPZREhAokOd5USBLBEKaA0YcSxjzHBgkimfIQYyBCh4LBizPecQTyqMRudjs9Qd-d-haWWunsKqgQdM5mWY-JhXCG-ONUVnjnM8qV1bXYH8lo7LHKXtWsmclRSLXOOXMj51t93d5jcVuaMvP6-dbHZyCqrTQKO12tojxlK5tdxsbehY_Gq10SvesC21RtbIw-v87_gCZZZF7</recordid><startdate>19960601</startdate><enddate>19960601</enddate><creator>Malik, Karl F.</creator><creator>Kim, Jin</creator><creator>Hartman, Adam L.</creator><creator>Kim, Paul</creator><creator>Scott Young, W.</creator><general>Elsevier B.V</general><general>Elsevier</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>7X8</scope></search><sort><creationdate>19960601</creationdate><title>Binding preferences of the POU domain protein Brain-4: implications for autoregulation</title><author>Malik, Karl F. ; Kim, Jin ; Hartman, Adam L. ; Kim, Paul ; Scott Young, W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-9041015a9e9e2bbdde159ea7bae32efa62ba1a5c28e2a96a092491a1bb2325023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenine - chemistry</topic><topic>Animals</topic><topic>Autoregulation</topic><topic>Biochemistry and metabolism</topic><topic>Biological and medical sciences</topic><topic>Central nervous system</topic><topic>DNA Footprinting</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation - physiology</topic><topic>Gene regulation</topic><topic>Histocytochemistry</topic><topic>Homeostasis</topic><topic>Hypothalamus</topic><topic>In Situ Hybridization</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred Strains</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neuropeptide</topic><topic>POU</topic><topic>POU Domain Factors</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Thymine - chemistry</topic><topic>Transcription factor</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Malik, Karl F.</creatorcontrib><creatorcontrib>Kim, Jin</creatorcontrib><creatorcontrib>Hartman, Adam L.</creatorcontrib><creatorcontrib>Kim, Paul</creatorcontrib><creatorcontrib>Scott Young, W.</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>MEDLINE - Academic</collection><jtitle>Brain research. Molecular brain research.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Malik, Karl F.</au><au>Kim, Jin</au><au>Hartman, Adam L.</au><au>Kim, Paul</au><au>Scott Young, W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding preferences of the POU domain protein Brain-4: implications for autoregulation</atitle><jtitle>Brain research. Molecular brain research.</jtitle><addtitle>Brain Res Mol Brain Res</addtitle><date>1996-06-01</date><risdate>1996</risdate><volume>38</volume><issue>2</issue><spage>209</spage><epage>221</epage><pages>209-221</pages><issn>0169-328X</issn><eissn>1872-6941</eissn><abstract>The POU domain-containing transcription factor Brain-4 (Brn-4, RHS-2) was examined for its sites of expression and DNA binding preferences. In the rat, Brn-4 is expressed in 76 and 65% of vasopressin neurons in the paraventricular and supraoptic nuclei, respectively; but in only 10% of corticotropin-releasing factor neurons in the paraventricular nucleus of the hypothalamus. From these data we speculate that genes expressed within vasopressingergic neurons are more likely to be regulated by Brn-4 than those in corticotropin-releasing factor neurons. Random oligonucleotide site selection indicates Brn-4 prefers binding the DNA element CAATATGCTAAT and is inflexible in its spacing requirement between putative CAATAT and TAAT half sites, preferring 2 nucleotides between these elements. Electrophoretic mobility shift and DNase I footprinting analyses show five regions between nucleotides −457 and +22 of the Brn-4 promoter that are bound by Brn-4. Furthermore, Brn-4 can transactivate from this region of the Brn-4 promoter, suggesting that Brn-4 expression may be autoregulated.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>8793109</pmid><doi>10.1016/0169-328X(95)00308-F</doi><tpages>13</tpages></addata></record> |
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| ispartof | Brain research. Molecular brain research., 1996-06, Vol.38 (2), p.209-221 |
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| subjects | Adenine - chemistry Animals Autoregulation Biochemistry and metabolism Biological and medical sciences Central nervous system DNA Footprinting DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Regulation - physiology Gene regulation Histocytochemistry Homeostasis Hypothalamus In Situ Hybridization Male Mice Mice, Inbred Strains Molecular Sequence Data Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Neuropeptide POU POU Domain Factors Promoter Regions, Genetic Protein Binding Protein Structure, Tertiary Rats Rats, Sprague-Dawley Thymine - chemistry Transcription factor Transcription Factors - chemistry Transcription Factors - metabolism Vertebrates: nervous system and sense organs |
| title | Binding preferences of the POU domain protein Brain-4: implications for autoregulation |
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