Determining residue-base interactions between AraC protein and araI DNA
Depurination/depyrimidation binding-interference experiments (missing contact probing) identified specific candidate residue-base interactions lost by mutants of Escherichia coli l-arabinose operon regulatory protein, AraC, to one of its binding sites, araI. These candidates were then checked more r...
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| Veröffentlicht in: | Journal of molecular biology 1989-10, Vol.209 (4), p.607-622 |
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| creator | Brunelle, Alan Schleif, Robert |
| description | Depurination/depyrimidation binding-interference experiments (missing contact probing) identified specific candidate residue-base interactions lost by mutants of
Escherichia coli
l-arabinose operon regulatory protein, AraC, to one of its binding sites,
araI. These candidates were then checked more rigorously by comparing the affinities of wild-type and alanine-substituted AraC protein to variants of
araI with alterations in the candidate contacted positions. Residues 208 and 212 apparently contact DNA and support, but do not prove the existence of a helix-turn-helix structure in this region of AraC protein whereas contacts by mutants with alterations at positions 256, 257 and 261 which are within another potential helix-turn-helix region do not support the existence of such a structure there. The missing contacts displayed by three AraC mutants are found within two major groove regions of the DNA and are spaced 21 base-pairs apart in a pattern indicating a direct repeat orientation for the subunits of AraC. |
| doi_str_mv | 10.1016/0022-2836(89)90598-6 |
| format | Article |
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Escherichia coli
l-arabinose operon regulatory protein, AraC, to one of its binding sites,
araI. These candidates were then checked more rigorously by comparing the affinities of wild-type and alanine-substituted AraC protein to variants of
araI with alterations in the candidate contacted positions. Residues 208 and 212 apparently contact DNA and support, but do not prove the existence of a helix-turn-helix structure in this region of AraC protein whereas contacts by mutants with alterations at positions 256, 257 and 261 which are within another potential helix-turn-helix region do not support the existence of such a structure there. The missing contacts displayed by three AraC mutants are found within two major groove regions of the DNA and are spaced 21 base-pairs apart in a pattern indicating a direct repeat orientation for the subunits of AraC.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(89)90598-6</identifier><identifier>PMID: 2531226</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Analytical, structural and metabolic biochemistry ; Binding and carrier proteins ; Binding Sites ; Biological and medical sciences ; DNA Mutational Analysis ; DNA Probes ; DNA-Binding Proteins - analysis ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Genes ; Genes, araC ; Genes, Regulator ; Genotype ; Mutation ; Protein Conformation ; Proteins ; Regulatory Sequences, Nucleic Acid</subject><ispartof>Journal of molecular biology, 1989-10, Vol.209 (4), p.607-622</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-7f52e1d13dc5d6dc58348bf8b106bfa2f7b1099448859ad14333016a3c851dd3</citedby><cites>FETCH-LOGICAL-c386t-7f52e1d13dc5d6dc58348bf8b106bfa2f7b1099448859ad14333016a3c851dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-2836(89)90598-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6686804$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2531226$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brunelle, Alan</creatorcontrib><creatorcontrib>Schleif, Robert</creatorcontrib><title>Determining residue-base interactions between AraC protein and araI DNA</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Depurination/depyrimidation binding-interference experiments (missing contact probing) identified specific candidate residue-base interactions lost by mutants of
Escherichia coli
l-arabinose operon regulatory protein, AraC, to one of its binding sites,
araI. These candidates were then checked more rigorously by comparing the affinities of wild-type and alanine-substituted AraC protein to variants of
araI with alterations in the candidate contacted positions. Residues 208 and 212 apparently contact DNA and support, but do not prove the existence of a helix-turn-helix structure in this region of AraC protein whereas contacts by mutants with alterations at positions 256, 257 and 261 which are within another potential helix-turn-helix region do not support the existence of such a structure there. The missing contacts displayed by three AraC mutants are found within two major groove regions of the DNA and are spaced 21 base-pairs apart in a pattern indicating a direct repeat orientation for the subunits of AraC.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>DNA Mutational Analysis</subject><subject>DNA Probes</subject><subject>DNA-Binding Proteins - analysis</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genes, araC</subject><subject>Genes, Regulator</subject><subject>Genotype</subject><subject>Mutation</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Regulatory Sequences, Nucleic Acid</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KAzEURoMotVbfQGEWIroYzc9MmmyE0motFN10HzLJHYlMMzWZUXx7U1u6dJMEvnMvXw5ClwTfE0z4A8aU5lQwfivkncSlFDk_QkOChcwFZ-IYDQ_IKTqL8QNjXLJCDNCAloxQyodoPoMOwtp559-zANHZHvJKR8icT4E2nWt9zCrovgF8Ngl6mm1C24HzmfY200Evstnr5Byd1LqJcLG_R2j1_LSavuTLt_liOlnmhgne5eO6pEAsYdaUlqdDpD5VLSqCeVVrWo_TS8qiEKKU2pKCMZb-qpkRJbGWjdDNbm3q8NlD7NTaRQNNoz20fVSkZBITihNY7EAT2hgD1GoT3FqHH0Ww2upTWzdq60YJqf70KZ7Grvb7-2oN9jC095Xy632uo9FNHbQ3Lh4wzgUXuEjY4w6DpOLLQVDROPAGrAtgOmVb93-PX7BfihQ</recordid><startdate>19891020</startdate><enddate>19891020</enddate><creator>Brunelle, Alan</creator><creator>Schleif, Robert</creator><general>Elsevier Ltd</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>7QL</scope><scope>7TM</scope><scope>C1K</scope></search><sort><creationdate>19891020</creationdate><title>Determining residue-base interactions between AraC protein and araI DNA</title><author>Brunelle, Alan ; Schleif, Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-7f52e1d13dc5d6dc58348bf8b106bfa2f7b1099448859ad14333016a3c851dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding and carrier proteins</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>DNA Mutational Analysis</topic><topic>DNA Probes</topic><topic>DNA-Binding Proteins - analysis</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Genes, araC</topic><topic>Genes, Regulator</topic><topic>Genotype</topic><topic>Mutation</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Regulatory Sequences, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brunelle, Alan</creatorcontrib><creatorcontrib>Schleif, Robert</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brunelle, Alan</au><au>Schleif, Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Determining residue-base interactions between AraC protein and araI DNA</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1989-10-20</date><risdate>1989</risdate><volume>209</volume><issue>4</issue><spage>607</spage><epage>622</epage><pages>607-622</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>Depurination/depyrimidation binding-interference experiments (missing contact probing) identified specific candidate residue-base interactions lost by mutants of
Escherichia coli
l-arabinose operon regulatory protein, AraC, to one of its binding sites,
araI. These candidates were then checked more rigorously by comparing the affinities of wild-type and alanine-substituted AraC protein to variants of
araI with alterations in the candidate contacted positions. Residues 208 and 212 apparently contact DNA and support, but do not prove the existence of a helix-turn-helix structure in this region of AraC protein whereas contacts by mutants with alterations at positions 256, 257 and 261 which are within another potential helix-turn-helix region do not support the existence of such a structure there. The missing contacts displayed by three AraC mutants are found within two major groove regions of the DNA and are spaced 21 base-pairs apart in a pattern indicating a direct repeat orientation for the subunits of AraC.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>2531226</pmid><doi>10.1016/0022-2836(89)90598-6</doi><tpages>16</tpages></addata></record> |
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| ispartof | Journal of molecular biology, 1989-10, Vol.209 (4), p.607-622 |
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| language | eng |
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| subjects | Analytical, structural and metabolic biochemistry Binding and carrier proteins Binding Sites Biological and medical sciences DNA Mutational Analysis DNA Probes DNA-Binding Proteins - analysis Escherichia coli Fundamental and applied biological sciences. Psychology Genes Genes, araC Genes, Regulator Genotype Mutation Protein Conformation Proteins Regulatory Sequences, Nucleic Acid |
| title | Determining residue-base interactions between AraC protein and araI DNA |
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