Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1 (∗)
YY1 is a multifunctional transcription factor capable of either activation or repression of transcription. Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus a...
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| Veröffentlicht in: | The Journal of biological chemistry 1995-12, Vol.270 (50), p.30213-30220 |
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| container_title | The Journal of biological chemistry |
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| creator | Bushmeyer, Sarah Park, Kyoungsook Atchison, Michael L. |
| description | YY1 is a multifunctional transcription factor capable of either activation or repression of transcription. Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus and requires amino acids 16-29 and 80-100 for maximal activity. The region between residues 16 and 29 has the potential to form an acidic amphipathic helix, whereas residues between 80 and 100 are rich in proline and glutamine. The YY1 repression domain lies near the carboxyl terminus and is embedded within the YY1 zinc finger region necessary for binding to DNA. Deletion of YY1 amino acids, which include zinc fingers 3 and 4, abolishes repression. However, site-directed mutagenesis, progressive deletion, and internal deletion mutant analyses indicate that the normal structures of zinc fingers 3 and 4 are not required for repression. |
| doi_str_mv | 10.1074/jbc.270.50.30213 |
| format | Article |
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Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus and requires amino acids 16-29 and 80-100 for maximal activity. The region between residues 16 and 29 has the potential to form an acidic amphipathic helix, whereas residues between 80 and 100 are rich in proline and glutamine. The YY1 repression domain lies near the carboxyl terminus and is embedded within the YY1 zinc finger region necessary for binding to DNA. Deletion of YY1 amino acids, which include zinc fingers 3 and 4, abolishes repression. However, site-directed mutagenesis, progressive deletion, and internal deletion mutant analyses indicate that the normal structures of zinc fingers 3 and 4 are not required for repression.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.270.50.30213</identifier><identifier>PMID: 8530432</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3T3 Cells ; Animals ; Base Sequence ; Binding Sites ; Blotting, Western ; Cell Line ; Chloramphenicol O-Acetyltransferase - analysis ; Chloramphenicol O-Acetyltransferase - biosynthesis ; Cloning, Molecular ; DNA - metabolism ; DNA Primers ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - isolation & purification ; DNA-Binding Proteins - metabolism ; Electrophoresis, Polyacrylamide Gel ; Erythroid-Specific DNA-Binding Factors ; Mice ; Molecular Sequence Data ; Mutagenesis ; Mutagenesis, Site-Directed ; Nuclear Proteins - chemistry ; Nuclear Proteins - metabolism ; Polymerase Chain Reaction ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Restriction Mapping ; Sequence Deletion ; Spodoptera ; Transcription Factors - chemistry ; Transcription Factors - isolation & purification ; Transcription Factors - metabolism ; Transfection ; YY1 Transcription Factor ; Zinc Fingers</subject><ispartof>The Journal of biological chemistry, 1995-12, Vol.270 (50), p.30213-30220</ispartof><rights>1995 © 1995 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c513t-d566fa008b89cb2d579109456cc1ee390c8705064249336b466853d7a2ed2d623</citedby><cites>FETCH-LOGICAL-c513t-d566fa008b89cb2d579109456cc1ee390c8705064249336b466853d7a2ed2d623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8530432$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bushmeyer, Sarah</creatorcontrib><creatorcontrib>Park, Kyoungsook</creatorcontrib><creatorcontrib>Atchison, Michael L.</creatorcontrib><title>Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1 (∗)</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>YY1 is a multifunctional transcription factor capable of either activation or repression of transcription. Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus and requires amino acids 16-29 and 80-100 for maximal activity. The region between residues 16 and 29 has the potential to form an acidic amphipathic helix, whereas residues between 80 and 100 are rich in proline and glutamine. The YY1 repression domain lies near the carboxyl terminus and is embedded within the YY1 zinc finger region necessary for binding to DNA. Deletion of YY1 amino acids, which include zinc fingers 3 and 4, abolishes repression. However, site-directed mutagenesis, progressive deletion, and internal deletion mutant analyses indicate that the normal structures of zinc fingers 3 and 4 are not required for repression.</description><subject>3T3 Cells</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Blotting, Western</subject><subject>Cell Line</subject><subject>Chloramphenicol O-Acetyltransferase - analysis</subject><subject>Chloramphenicol O-Acetyltransferase - biosynthesis</subject><subject>Cloning, Molecular</subject><subject>DNA - metabolism</subject><subject>DNA Primers</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Erythroid-Specific DNA-Binding Factors</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - metabolism</subject><subject>Polymerase Chain Reaction</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Restriction Mapping</subject><subject>Sequence Deletion</subject><subject>Spodoptera</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - isolation & purification</subject><subject>Transcription Factors - metabolism</subject><subject>Transfection</subject><subject>YY1 Transcription Factor</subject><subject>Zinc Fingers</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM1K5TAUx8Mw4lw_9rMZ6GIYFOydk6Tpx-zk6lVBceOArkKank4jbXNNWkWfwDfw_XwSo_figGA2Cef_wcmPkO8UphSy5Pd1qacsg6mAKQdG-RcyoZDzmAt6-ZVMIMzigon8G9nw_hrCSQq6TtZzwSHhbELUrFFO6QGdeVCDsX1k62g-9vr1rdrowHbK9D66M0Nj-mhoMDob28HU_y0XTvVeO7N4i89DmXV70dUVjXaeH592t8harVqP26t7k_ydH17MjuPT86OT2f5prAXlQ1yJNK0VQF7mhS5ZJbKCQpGIVGuKyAvQeQYC0oQlBedpmaRp-ESVKYYVq1LGN8mvZe_C2ZsR_SA74zW2rerRjl7SLNAQiQhGWBq1s947rOXCmU65e0lBvlKVgaoMVKUA-UY1RH6suseyw-o9sMIY9J9LvTH_mjvjUJbG6ga7jzV_ljYMHG4NOum1wV5jFSJ6kJU1n-_wAnM6kjg</recordid><startdate>19951215</startdate><enddate>19951215</enddate><creator>Bushmeyer, Sarah</creator><creator>Park, Kyoungsook</creator><creator>Atchison, Michael L.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>19951215</creationdate><title>Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1 (∗)</title><author>Bushmeyer, Sarah ; Park, Kyoungsook ; Atchison, Michael L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c513t-d566fa008b89cb2d579109456cc1ee390c8705064249336b466853d7a2ed2d623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>3T3 Cells</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Blotting, Western</topic><topic>Cell Line</topic><topic>Chloramphenicol O-Acetyltransferase - analysis</topic><topic>Chloramphenicol O-Acetyltransferase - biosynthesis</topic><topic>Cloning, Molecular</topic><topic>DNA - metabolism</topic><topic>DNA Primers</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Erythroid-Specific DNA-Binding Factors</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - metabolism</topic><topic>Polymerase Chain Reaction</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Restriction Mapping</topic><topic>Sequence Deletion</topic><topic>Spodoptera</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - isolation & purification</topic><topic>Transcription Factors - metabolism</topic><topic>Transfection</topic><topic>YY1 Transcription Factor</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bushmeyer, Sarah</creatorcontrib><creatorcontrib>Park, Kyoungsook</creatorcontrib><creatorcontrib>Atchison, Michael L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bushmeyer, Sarah</au><au>Park, Kyoungsook</au><au>Atchison, Michael L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1 (∗)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1995-12-15</date><risdate>1995</risdate><volume>270</volume><issue>50</issue><spage>30213</spage><epage>30220</epage><pages>30213-30220</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>YY1 is a multifunctional transcription factor capable of either activation or repression of transcription. Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus and requires amino acids 16-29 and 80-100 for maximal activity. The region between residues 16 and 29 has the potential to form an acidic amphipathic helix, whereas residues between 80 and 100 are rich in proline and glutamine. The YY1 repression domain lies near the carboxyl terminus and is embedded within the YY1 zinc finger region necessary for binding to DNA. Deletion of YY1 amino acids, which include zinc fingers 3 and 4, abolishes repression. However, site-directed mutagenesis, progressive deletion, and internal deletion mutant analyses indicate that the normal structures of zinc fingers 3 and 4 are not required for repression.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8530432</pmid><doi>10.1074/jbc.270.50.30213</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1995-12, Vol.270 (50), p.30213-30220 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 3T3 Cells Animals Base Sequence Binding Sites Blotting, Western Cell Line Chloramphenicol O-Acetyltransferase - analysis Chloramphenicol O-Acetyltransferase - biosynthesis Cloning, Molecular DNA - metabolism DNA Primers DNA-Binding Proteins - chemistry DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel Erythroid-Specific DNA-Binding Factors Mice Molecular Sequence Data Mutagenesis Mutagenesis, Site-Directed Nuclear Proteins - chemistry Nuclear Proteins - metabolism Polymerase Chain Reaction Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping Sequence Deletion Spodoptera Transcription Factors - chemistry Transcription Factors - isolation & purification Transcription Factors - metabolism Transfection YY1 Transcription Factor Zinc Fingers |
| title | Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1 (∗) |
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