The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite
Cys-3, the major sulfur regulatory gene of Neurospora crassa, encodes a regulatory protein that is capable of sequence-specific interaction with DNA. The interaction is mediated by a region within the CYS3 protein (the bzip region) which contains a potential dimer-forming surface, the leucine zipper...
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| Veröffentlicht in: | Biochemistry (Easton) 1992-03, Vol.31 (12), p.3197-3203 |
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| creator | Kanaan, Moien N Fu, Ying Hui Marzluf, George A |
| description | Cys-3, the major sulfur regulatory gene of Neurospora crassa, encodes a regulatory protein that is capable of sequence-specific interaction with DNA. The interaction is mediated by a region within the CYS3 protein (the bzip region) which contains a potential dimer-forming surface, the leucine zipper, and an adjacent basic DNA contact region, NH2-terminal to the leucine zipper. To investigate the bipartite nature of the bzip region, a series of cys-3 mutants obtained by oligonucleotide-directed mutagenesis were expressed and tested for dimer formation as well as DNA binding and in vivo function. The results demonstrate that CYS3 protein exists as a dimer in the presence and absence of the target DNA and that dimerization of CYS3 is mediated strictly by the leucine zipper, which is required for both cys-3 function in vivo and DNA-binding activity in vitro. Furthermore, a truncated CYS3 protein corresponding to just the bzip region was found to mediate dimer formation and to possess DNA-binding activity. A CYS3 mutant protein with a pure methionine zipper showed significant, although reduced, function in vivo and in vitro |
| doi_str_mv | 10.1021/bi00127a022 |
| format | Article |
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The interaction is mediated by a region within the CYS3 protein (the bzip region) which contains a potential dimer-forming surface, the leucine zipper, and an adjacent basic DNA contact region, NH2-terminal to the leucine zipper. To investigate the bipartite nature of the bzip region, a series of cys-3 mutants obtained by oligonucleotide-directed mutagenesis were expressed and tested for dimer formation as well as DNA binding and in vivo function. The results demonstrate that CYS3 protein exists as a dimer in the presence and absence of the target DNA and that dimerization of CYS3 is mediated strictly by the leucine zipper, which is required for both cys-3 function in vivo and DNA-binding activity in vitro. Furthermore, a truncated CYS3 protein corresponding to just the bzip region was found to mediate dimer formation and to possess DNA-binding activity. A CYS3 mutant protein with a pure methionine zipper showed significant, although reduced, function in vivo and in vitro</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00127a022</identifier><identifier>PMID: 1532511</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>ADN ; Amino Acid Sequence ; Biological and medical sciences ; Cystathionine gamma-Lyase ; DNA, Fungal - chemistry ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - physiology ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; GENE ; GENES ; Genes. Genome ; Genetic Vectors ; GENETICA ; GENETIQUE ; LEUCINA ; LEUCINE ; Leucine Zippers ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; NEUROSPORA ; Neurospora crassa ; Neurospora crassa - chemistry ; Neurospora crassa - genetics ; Neurospora crassa - physiology ; Protein Conformation ; PROTEINAS ; PROTEINE ; Recombinant Proteins - chemistry ; Saccharomyces cerevisiae Proteins ; Structure-Activity Relationship ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription Factors - physiology</subject><ispartof>Biochemistry (Easton), 1992-03, Vol.31 (12), p.3197-3203</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a433t-941d587b9512431911f46d4a5ce45a254ffe6aa3e0e3fa593e82e2878548572b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00127a022$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00127a022$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,778,782,2754,27059,27907,27908,56721,56771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5267530$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1532511$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanaan, Moien N</creatorcontrib><creatorcontrib>Fu, Ying Hui</creatorcontrib><creatorcontrib>Marzluf, George A</creatorcontrib><title>The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Cys-3, the major sulfur regulatory gene of Neurospora crassa, encodes a regulatory protein that is capable of sequence-specific interaction with DNA. The interaction is mediated by a region within the CYS3 protein (the bzip region) which contains a potential dimer-forming surface, the leucine zipper, and an adjacent basic DNA contact region, NH2-terminal to the leucine zipper. To investigate the bipartite nature of the bzip region, a series of cys-3 mutants obtained by oligonucleotide-directed mutagenesis were expressed and tested for dimer formation as well as DNA binding and in vivo function. The results demonstrate that CYS3 protein exists as a dimer in the presence and absence of the target DNA and that dimerization of CYS3 is mediated strictly by the leucine zipper, which is required for both cys-3 function in vivo and DNA-binding activity in vitro. Furthermore, a truncated CYS3 protein corresponding to just the bzip region was found to mediate dimer formation and to possess DNA-binding activity. A CYS3 mutant protein with a pure methionine zipper showed significant, although reduced, function in vivo and in vitro</description><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Cystathionine gamma-Lyase</subject><subject>DNA, Fungal - chemistry</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - physiology</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>GENE</subject><subject>GENES</subject><subject>Genes. Genome</subject><subject>Genetic Vectors</subject><subject>GENETICA</subject><subject>GENETIQUE</subject><subject>LEUCINA</subject><subject>LEUCINE</subject><subject>Leucine Zippers</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>NEUROSPORA</subject><subject>Neurospora crassa</subject><subject>Neurospora crassa - chemistry</subject><subject>Neurospora crassa - genetics</subject><subject>Neurospora crassa - physiology</subject><subject>Protein Conformation</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Recombinant Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Structure-Activity Relationship</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - physiology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM9rFDEYhoNY6lo9eROEHEQPZTS_Z3KsW1uFUpXdgrfwzcw3a-rsZE1mwP3vzTJL9eApfDwPL29eQl5w9o4zwd_XnjEuSmBCPCILrgUrlLX6MVkwxkwhrGFPyNOU7vOpWKlOySnXUmjOF-T7-gfSy9uLovZD64cNbcMW_EBDR8dMlvtUSBpxM_UwhrinuxhGnPktTjGkXYhAmwgpAfWJ1n4HcfQjPiMnHfQJnx_fM3J39XG9_FTcfLn-vLy4KUBJORZW8VZXZW01F0pyy3mnTKtAN6g0CK26Dg2ARIayA20lVgJFVVZaVboUtTwjb-bc3OzXhGl0W58a7HsYMEzJcaOVNNZm8XwWm9w6RezcLvotxL3jzB12dP_smO1Xx9ip3mL7152Hy_z1kUNqoO8iDI1PD5oWptSSZa2YNZ9G_P2AIf50ppSlduuvKyfMt0tmVx_cIfbl7HcQHGxijrxbWW6NMocfvJ0hNMndhykOedj_tv8DIcqbuw</recordid><startdate>19920331</startdate><enddate>19920331</enddate><creator>Kanaan, Moien N</creator><creator>Fu, Ying Hui</creator><creator>Marzluf, George A</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><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>M7N</scope></search><sort><creationdate>19920331</creationdate><title>The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite</title><author>Kanaan, Moien N ; Fu, Ying Hui ; Marzluf, George A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a433t-941d587b9512431911f46d4a5ce45a254ffe6aa3e0e3fa593e82e2878548572b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Cystathionine gamma-Lyase</topic><topic>DNA, Fungal - chemistry</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - physiology</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>GENE</topic><topic>GENES</topic><topic>Genes. Genome</topic><topic>Genetic Vectors</topic><topic>GENETICA</topic><topic>GENETIQUE</topic><topic>LEUCINA</topic><topic>LEUCINE</topic><topic>Leucine Zippers</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>NEUROSPORA</topic><topic>Neurospora crassa</topic><topic>Neurospora crassa - chemistry</topic><topic>Neurospora crassa - genetics</topic><topic>Neurospora crassa - physiology</topic><topic>Protein Conformation</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Recombinant Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Structure-Activity Relationship</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanaan, Moien N</creatorcontrib><creatorcontrib>Fu, Ying Hui</creatorcontrib><creatorcontrib>Marzluf, George A</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanaan, Moien N</au><au>Fu, Ying Hui</au><au>Marzluf, George A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1992-03-31</date><risdate>1992</risdate><volume>31</volume><issue>12</issue><spage>3197</spage><epage>3203</epage><pages>3197-3203</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Cys-3, the major sulfur regulatory gene of Neurospora crassa, encodes a regulatory protein that is capable of sequence-specific interaction with DNA. The interaction is mediated by a region within the CYS3 protein (the bzip region) which contains a potential dimer-forming surface, the leucine zipper, and an adjacent basic DNA contact region, NH2-terminal to the leucine zipper. To investigate the bipartite nature of the bzip region, a series of cys-3 mutants obtained by oligonucleotide-directed mutagenesis were expressed and tested for dimer formation as well as DNA binding and in vivo function. The results demonstrate that CYS3 protein exists as a dimer in the presence and absence of the target DNA and that dimerization of CYS3 is mediated strictly by the leucine zipper, which is required for both cys-3 function in vivo and DNA-binding activity in vitro. Furthermore, a truncated CYS3 protein corresponding to just the bzip region was found to mediate dimer formation and to possess DNA-binding activity. A CYS3 mutant protein with a pure methionine zipper showed significant, although reduced, function in vivo and in vitro</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1532511</pmid><doi>10.1021/bi00127a022</doi><tpages>7</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | ADN Amino Acid Sequence Biological and medical sciences Cystathionine gamma-Lyase DNA, Fungal - chemistry DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - physiology EXPRESION GENICA EXPRESSION DES GENES Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics GENE GENES Genes. Genome Genetic Vectors GENETICA GENETIQUE LEUCINA LEUCINE Leucine Zippers Molecular and cellular biology Molecular genetics Molecular Sequence Data NEUROSPORA Neurospora crassa Neurospora crassa - chemistry Neurospora crassa - genetics Neurospora crassa - physiology Protein Conformation PROTEINAS PROTEINE Recombinant Proteins - chemistry Saccharomyces cerevisiae Proteins Structure-Activity Relationship Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - physiology |
| title | The DNA-binding domain of the Cys-3 regulatory protein of Neurospora crassa is bipartite |
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