single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding
Specific DNA binding to the core consensus site GAGAGAG has been shown with an 82-residue peptide (residues 310-391) taken from the Drosophila transcription factor GAGA. Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding (residues 310-372) i...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-04, Vol.93 (7), p.2822-2826 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Pedone, P.V Ghirlando, R Clore, G.M Gronenborn, A.M Felsenfeld, G Omichinski, J.G |
| description | Specific DNA binding to the core consensus site GAGAGAG has been shown with an 82-residue peptide (residues 310-391) taken from the Drosophila transcription factor GAGA. Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding (residues 310-372) includes a single zinc finger of the Cys2-His2 family and a stretch of basic amino acids located on the N-terminal end of the zinc finger. In gel retardation assays, the specific binding seen with either the peptide or the whole protein is zinc dependent and corresponds to a dissociation constant of approximately 5 X 10(-9) M for the purified peptide. It has previously been thought that a single zinc finger of the Cys2-His2 family is incapable of specific, high-affinity binding to DNA. The combination of an N-terminal basic region with a single Cys2-His2 zinc finger in the GAGA protein can thus be viewed as a novel DNA binding domain. This raises the possibility that other proteins carrying only one Cys2-His2 finger are also capable of high-affinity specific binding to DNA. |
| doi_str_mv | 10.1073/pnas.93.7.2822 |
| format | Article |
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Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding (residues 310-372) includes a single zinc finger of the Cys2-His2 family and a stretch of basic amino acids located on the N-terminal end of the zinc finger. In gel retardation assays, the specific binding seen with either the peptide or the whole protein is zinc dependent and corresponds to a dissociation constant of approximately 5 X 10(-9) M for the purified peptide. It has previously been thought that a single zinc finger of the Cys2-His2 family is incapable of specific, high-affinity binding to DNA. The combination of an N-terminal basic region with a single Cys2-His2 zinc finger in the GAGA protein can thus be viewed as a novel DNA binding domain. This raises the possibility that other proteins carrying only one Cys2-His2 finger are also capable of high-affinity specific binding to DNA.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.7.2822</identifier><identifier>PMID: 8610125</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Amino acids ; Animals ; Base Sequence ; Binding Sites ; Biochemistry ; Cell Line ; Cloning, Molecular ; cysteine ; Deoxyribonucleic acid ; DNA ; DNA - metabolism ; DNA binding proteins ; DNA Primers ; DNA-binding domains ; Drosophila ; Drosophila - metabolism ; Drosophila melanogaster ; Drosophila Proteins ; Gels ; histidine ; Homeodomain Proteins - biosynthesis ; Homeodomain Proteins - chemistry ; Homeodomain Proteins - metabolism ; Insects ; Kinetics ; Molecular Sequence Data ; Oligonucleotides ; Peptide Fragments - chemistry ; Peptide Fragments - isolation & purification ; Peptide Fragments - metabolism ; Peptides ; Polymerase Chain Reaction - methods ; Promoter regions ; Protein Conformation ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; transcription factors ; Transcription Factors - biosynthesis ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; Transfection ; Zinc ; Zinc Fingers</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-04, Vol.93 (7), p.2822-2826</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Apr 2, 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4872-4ec13121a2ef4e2a404ef298642ca897f76bb94ff6109b74da440361e5c07a6f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/39071$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/39071$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8610125$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pedone, P.V</creatorcontrib><creatorcontrib>Ghirlando, R</creatorcontrib><creatorcontrib>Clore, G.M</creatorcontrib><creatorcontrib>Gronenborn, A.M</creatorcontrib><creatorcontrib>Felsenfeld, G</creatorcontrib><creatorcontrib>Omichinski, J.G</creatorcontrib><title>single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Specific DNA binding to the core consensus site GAGAGAG has been shown with an 82-residue peptide (residues 310-391) taken from the Drosophila transcription factor GAGA. Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding (residues 310-372) includes a single zinc finger of the Cys2-His2 family and a stretch of basic amino acids located on the N-terminal end of the zinc finger. In gel retardation assays, the specific binding seen with either the peptide or the whole protein is zinc dependent and corresponds to a dissociation constant of approximately 5 X 10(-9) M for the purified peptide. It has previously been thought that a single zinc finger of the Cys2-His2 family is incapable of specific, high-affinity binding to DNA. The combination of an N-terminal basic region with a single Cys2-His2 zinc finger in the GAGA protein can thus be viewed as a novel DNA binding domain. This raises the possibility that other proteins carrying only one Cys2-His2 finger are also capable of high-affinity specific binding to DNA.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>cysteine</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA binding proteins</subject><subject>DNA Primers</subject><subject>DNA-binding domains</subject><subject>Drosophila</subject><subject>Drosophila - metabolism</subject><subject>Drosophila melanogaster</subject><subject>Drosophila Proteins</subject><subject>Gels</subject><subject>histidine</subject><subject>Homeodomain Proteins - biosynthesis</subject><subject>Homeodomain Proteins - chemistry</subject><subject>Homeodomain Proteins - metabolism</subject><subject>Insects</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Oligonucleotides</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptides</subject><subject>Polymerase Chain Reaction - methods</subject><subject>Promoter regions</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>transcription factors</subject><subject>Transcription Factors - biosynthesis</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>Transfection</subject><subject>Zinc</subject><subject>Zinc Fingers</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc2O0zAUhS0EGjoDWxZICGsWs0vwX-JYYlMV6CCNYAGzthzHbl1Su2MniPIAPDeOWqrCgpWle75j3-MDwAuMSow4fbPzKpWClrwkDSGPwAwjgYuaCfQYzBAivGgYYU_BZUobhJCoGnQBLpoaI0yqGfiVnF_1Bi72iRS3LhH403kNbZ6aCLuwVc7DYOGwNnA5X87hLobB5Jntlf9mOtjuYauS0zCa5LrRJOgSTKO1TjvjB2hDhGu3Whcqj7wb9jDtjHZZhu8-zWHrfJffegaeWNUn8_x4XoH7D--_Lm6Lu8_Lj4v5XaFZw0nBjMYUE6yIscwQxRAzloimZkSrRnDL67YVzNocT7ScdYoxRGtsKo24qi29Am8P9-7Gdms6nTeMqpe76LYq7mVQTv6teLeWq_BdUsExz_aboz2Gh5x1kFuXtOnzX5gwJsm54Cg_mMHrf8BNGKPP0SRBOQKtapKh8gDpGFKKxp72wEhO5cqpXCmo5HIqNxtenW9_wo9tnumT74967r_5ny7t2PeD-TFk8OUB3KQhxBNJBeI4i68PolVBqlV0Sd5_mVIhXOE6R6O_AZflyqw</recordid><startdate>19960402</startdate><enddate>19960402</enddate><creator>Pedone, P.V</creator><creator>Ghirlando, R</creator><creator>Clore, G.M</creator><creator>Gronenborn, A.M</creator><creator>Felsenfeld, G</creator><creator>Omichinski, J.G</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19960402</creationdate><title>single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding</title><author>Pedone, P.V ; Ghirlando, R ; Clore, G.M ; Gronenborn, A.M ; Felsenfeld, G ; Omichinski, J.G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4872-4ec13121a2ef4e2a404ef298642ca897f76bb94ff6109b74da440361e5c07a6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>cysteine</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA - metabolism</topic><topic>DNA binding proteins</topic><topic>DNA Primers</topic><topic>DNA-binding domains</topic><topic>Drosophila</topic><topic>Drosophila - metabolism</topic><topic>Drosophila melanogaster</topic><topic>Drosophila Proteins</topic><topic>Gels</topic><topic>histidine</topic><topic>Homeodomain Proteins - biosynthesis</topic><topic>Homeodomain Proteins - chemistry</topic><topic>Homeodomain Proteins - metabolism</topic><topic>Insects</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Oligonucleotides</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptides</topic><topic>Polymerase Chain Reaction - methods</topic><topic>Promoter regions</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>transcription factors</topic><topic>Transcription Factors - biosynthesis</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><topic>Transfection</topic><topic>Zinc</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pedone, P.V</creatorcontrib><creatorcontrib>Ghirlando, R</creatorcontrib><creatorcontrib>Clore, G.M</creatorcontrib><creatorcontrib>Gronenborn, A.M</creatorcontrib><creatorcontrib>Felsenfeld, G</creatorcontrib><creatorcontrib>Omichinski, J.G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pedone, P.V</au><au>Ghirlando, R</au><au>Clore, G.M</au><au>Gronenborn, A.M</au><au>Felsenfeld, G</au><au>Omichinski, J.G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-04-02</date><risdate>1996</risdate><volume>93</volume><issue>7</issue><spage>2822</spage><epage>2826</epage><pages>2822-2826</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Specific DNA binding to the core consensus site GAGAGAG has been shown with an 82-residue peptide (residues 310-391) taken from the Drosophila transcription factor GAGA. Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding (residues 310-372) includes a single zinc finger of the Cys2-His2 family and a stretch of basic amino acids located on the N-terminal end of the zinc finger. In gel retardation assays, the specific binding seen with either the peptide or the whole protein is zinc dependent and corresponds to a dissociation constant of approximately 5 X 10(-9) M for the purified peptide. It has previously been thought that a single zinc finger of the Cys2-His2 family is incapable of specific, high-affinity binding to DNA. The combination of an N-terminal basic region with a single Cys2-His2 zinc finger in the GAGA protein can thus be viewed as a novel DNA binding domain. This raises the possibility that other proteins carrying only one Cys2-His2 finger are also capable of high-affinity specific binding to DNA.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8610125</pmid><doi>10.1073/pnas.93.7.2822</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1996-04, Vol.93 (7), p.2822-2826 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | PubMed Central Free; MEDLINE; Jstor Complete Legacy; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence amino acid sequences Amino acids Animals Base Sequence Binding Sites Biochemistry Cell Line Cloning, Molecular cysteine Deoxyribonucleic acid DNA DNA - metabolism DNA binding proteins DNA Primers DNA-binding domains Drosophila Drosophila - metabolism Drosophila melanogaster Drosophila Proteins Gels histidine Homeodomain Proteins - biosynthesis Homeodomain Proteins - chemistry Homeodomain Proteins - metabolism Insects Kinetics Molecular Sequence Data Oligonucleotides Peptide Fragments - chemistry Peptide Fragments - isolation & purification Peptide Fragments - metabolism Peptides Polymerase Chain Reaction - methods Promoter regions Protein Conformation Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism transcription factors Transcription Factors - biosynthesis Transcription Factors - chemistry Transcription Factors - metabolism Transfection Zinc Zinc Fingers |
| title | single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding |
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