Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9
CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9, activates the transcription of chlorocatechol-degradative enzymes. To activate the transcription, CbnR needs to bind not only to the cbnA promoter but also to the inducer. In this study, the transcriptional activity and DNA-bi...
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| creator | Moriuchi, Ryota Takada, Kaori Takabayashi, Masae Yamamoto, Yuko Shimodaira, Jun Kuroda, Naoko Akiyama, Emiko Udagawa, Mayumi Minai, Ryoichi Fukuda, Masao Senda, Toshiya Ogawa, Naoto |
| description | CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9, activates the transcription of chlorocatechol-degradative enzymes. To activate the transcription, CbnR needs to bind not only to the cbnA promoter but also to the inducer. In this study, the transcriptional activity and DNA-binding activity of twenty-five mutants of CbnR were analyzed. Of the 17 mutants of the DNA-binding domain, 11 mutants lost their ability to activate transcription. While most mutants without transcriptional activation did not show DNA-binding activity, Asn17Ala, Gln29Ala, and Pro30Ala retained DNA-binding activity, suggesting that transcriptional activation by CbnR requires more than its binding to promoter DNA. Of the 8 mutants of the regulatory domain, 6 mutants changed their responses to the inducer, when compared with wild-type CbnR. Interestingly, Arg199Ala and Val246Ala induced constitutive expression of the cbnA promoter without the inducer, suggesting that these mutations brought about a conformational change mimicking that induced by the inducer molecule.
Mutational analysis of a LysR-type transcriptional regulator, CbnR, revealed critical amino acids in regulatory domain (A and B) and DNA-binding domain (C and D). |
| doi_str_mv | 10.1080/09168451.2017.1373592 |
| format | Article |
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Mutational analysis of a LysR-type transcriptional regulator, CbnR, revealed critical amino acids in regulatory domain (A and B) and DNA-binding domain (C and D).</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1080/09168451.2017.1373592</identifier><identifier>PMID: 28936918</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; chlorinated aromatic degradation ; chlorocatechol ; Cupriavidus necator ; Cupriavidus necator - genetics ; Cupriavidus necator - metabolism ; DNA - metabolism ; LysR-type transcriptional regulator ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; site-directed mutagenesis ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transcriptional Activation</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2017-11, Vol.81 (11), p.2119-2129</ispartof><rights>2017 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-79eb16184c9a0ae5305459c1cf909856a5bc862b6a5c9914ba1ba660cc84170a3</citedby><cites>FETCH-LOGICAL-c544t-79eb16184c9a0ae5305459c1cf909856a5bc862b6a5c9914ba1ba660cc84170a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28936918$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moriuchi, Ryota</creatorcontrib><creatorcontrib>Takada, Kaori</creatorcontrib><creatorcontrib>Takabayashi, Masae</creatorcontrib><creatorcontrib>Yamamoto, Yuko</creatorcontrib><creatorcontrib>Shimodaira, Jun</creatorcontrib><creatorcontrib>Kuroda, Naoko</creatorcontrib><creatorcontrib>Akiyama, Emiko</creatorcontrib><creatorcontrib>Udagawa, Mayumi</creatorcontrib><creatorcontrib>Minai, Ryoichi</creatorcontrib><creatorcontrib>Fukuda, Masao</creatorcontrib><creatorcontrib>Senda, Toshiya</creatorcontrib><creatorcontrib>Ogawa, Naoto</creatorcontrib><title>Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9, activates the transcription of chlorocatechol-degradative enzymes. To activate the transcription, CbnR needs to bind not only to the cbnA promoter but also to the inducer. In this study, the transcriptional activity and DNA-binding activity of twenty-five mutants of CbnR were analyzed. Of the 17 mutants of the DNA-binding domain, 11 mutants lost their ability to activate transcription. While most mutants without transcriptional activation did not show DNA-binding activity, Asn17Ala, Gln29Ala, and Pro30Ala retained DNA-binding activity, suggesting that transcriptional activation by CbnR requires more than its binding to promoter DNA. Of the 8 mutants of the regulatory domain, 6 mutants changed their responses to the inducer, when compared with wild-type CbnR. Interestingly, Arg199Ala and Val246Ala induced constitutive expression of the cbnA promoter without the inducer, suggesting that these mutations brought about a conformational change mimicking that induced by the inducer molecule.
Mutational analysis of a LysR-type transcriptional regulator, CbnR, revealed critical amino acids in regulatory domain (A and B) and DNA-binding domain (C and D).</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>chlorinated aromatic degradation</subject><subject>chlorocatechol</subject><subject>Cupriavidus necator</subject><subject>Cupriavidus necator - genetics</subject><subject>Cupriavidus necator - metabolism</subject><subject>DNA - metabolism</subject><subject>LysR-type transcriptional regulator</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>site-directed mutagenesis</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transcriptional Activation</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkN1KwzAYhoMobk4vQckF2JmsSducOebPhDFh6HH5mqYj0iYlaZXdhZds6qaH4lE-vjzvm_AgdEnJlJKM3BBBk4xxOp0Rmk5pnMZczI7QmMYsjRLB0mM0HphogEbozPs3QsKC01M0mmUiTgTNxuhz3mhjMUhdYqe8LnvlsXS60xJqXFmH79ZzXGhTarPFYEocxl4qF2hptyaA1oQdXhRmc40Br3Z-E3W7VuHOgfGhqh2QUObUtq-hC5WVsw1e9K3T8B5e9Ngo-X2xXopzdFJB7dXF4Zyg14f7l8UyWj0_Pi3mq0hyxrooFaqgCc2YFEBA8ZhwxoWkshJEZDwBXsgsmRVhkEJQVgAtIEmIlBmjKYF4gvi-VzrrvVNVHr7TgNvllOSD4fzHcD4Yzg-GQ-5qn2v7olHlb-pHaQDIHrB9--_O231Em2C8gQ_r6jLvYFdbVwWLUvs8_rviCy1Nmf4</recordid><startdate>20171102</startdate><enddate>20171102</enddate><creator>Moriuchi, Ryota</creator><creator>Takada, Kaori</creator><creator>Takabayashi, Masae</creator><creator>Yamamoto, Yuko</creator><creator>Shimodaira, Jun</creator><creator>Kuroda, Naoko</creator><creator>Akiyama, Emiko</creator><creator>Udagawa, Mayumi</creator><creator>Minai, Ryoichi</creator><creator>Fukuda, Masao</creator><creator>Senda, Toshiya</creator><creator>Ogawa, Naoto</creator><general>Taylor & Francis</general><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20171102</creationdate><title>Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9</title><author>Moriuchi, Ryota ; Takada, Kaori ; Takabayashi, Masae ; Yamamoto, Yuko ; Shimodaira, Jun ; Kuroda, Naoko ; Akiyama, Emiko ; Udagawa, Mayumi ; Minai, Ryoichi ; Fukuda, Masao ; Senda, Toshiya ; Ogawa, Naoto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-79eb16184c9a0ae5305459c1cf909856a5bc862b6a5c9914ba1ba660cc84170a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>chlorinated aromatic degradation</topic><topic>chlorocatechol</topic><topic>Cupriavidus necator</topic><topic>Cupriavidus necator - genetics</topic><topic>Cupriavidus necator - metabolism</topic><topic>DNA - metabolism</topic><topic>LysR-type transcriptional regulator</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>site-directed mutagenesis</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcriptional Activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moriuchi, Ryota</creatorcontrib><creatorcontrib>Takada, Kaori</creatorcontrib><creatorcontrib>Takabayashi, Masae</creatorcontrib><creatorcontrib>Yamamoto, Yuko</creatorcontrib><creatorcontrib>Shimodaira, Jun</creatorcontrib><creatorcontrib>Kuroda, Naoko</creatorcontrib><creatorcontrib>Akiyama, Emiko</creatorcontrib><creatorcontrib>Udagawa, Mayumi</creatorcontrib><creatorcontrib>Minai, Ryoichi</creatorcontrib><creatorcontrib>Fukuda, Masao</creatorcontrib><creatorcontrib>Senda, Toshiya</creatorcontrib><creatorcontrib>Ogawa, Naoto</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moriuchi, Ryota</au><au>Takada, Kaori</au><au>Takabayashi, Masae</au><au>Yamamoto, Yuko</au><au>Shimodaira, Jun</au><au>Kuroda, Naoko</au><au>Akiyama, Emiko</au><au>Udagawa, Mayumi</au><au>Minai, Ryoichi</au><au>Fukuda, Masao</au><au>Senda, Toshiya</au><au>Ogawa, Naoto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2017-11-02</date><risdate>2017</risdate><volume>81</volume><issue>11</issue><spage>2119</spage><epage>2129</epage><pages>2119-2129</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9, activates the transcription of chlorocatechol-degradative enzymes. To activate the transcription, CbnR needs to bind not only to the cbnA promoter but also to the inducer. In this study, the transcriptional activity and DNA-binding activity of twenty-five mutants of CbnR were analyzed. Of the 17 mutants of the DNA-binding domain, 11 mutants lost their ability to activate transcription. While most mutants without transcriptional activation did not show DNA-binding activity, Asn17Ala, Gln29Ala, and Pro30Ala retained DNA-binding activity, suggesting that transcriptional activation by CbnR requires more than its binding to promoter DNA. Of the 8 mutants of the regulatory domain, 6 mutants changed their responses to the inducer, when compared with wild-type CbnR. Interestingly, Arg199Ala and Val246Ala induced constitutive expression of the cbnA promoter without the inducer, suggesting that these mutations brought about a conformational change mimicking that induced by the inducer molecule.
Mutational analysis of a LysR-type transcriptional regulator, CbnR, revealed critical amino acids in regulatory domain (A and B) and DNA-binding domain (C and D).</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>28936918</pmid><doi>10.1080/09168451.2017.1373592</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Freely Accessible Japanese Titles; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism chlorinated aromatic degradation chlorocatechol Cupriavidus necator Cupriavidus necator - genetics Cupriavidus necator - metabolism DNA - metabolism LysR-type transcriptional regulator Models, Molecular Mutation Protein Binding Protein Conformation site-directed mutagenesis Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism Transcriptional Activation |
| title | Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9 |
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