Analysis of the Nitric Oxide-sensing Non-heme Iron Center in the NorR Regulatory Protein
The NorR regulatory protein senses nitric oxide (NO) to activate genes required for NO detoxification under anaerobic and microaerobic conditions in Escherichia coli. NorR belongs to the σ54-dependent family of transcriptional activators and contains an N-terminal regulatory GAF (cGMP phosphodiester...
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| Veröffentlicht in: | The Journal of biological chemistry 2008-01, Vol.283 (2), p.908-918 |
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| container_title | The Journal of biological chemistry |
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| creator | Tucker, Nicholas P. D'Autréaux, Benoît Yousafzai, Faridoon K. Fairhurst, Shirley A. Spiro, Stephen Dixon, Ray |
| description | The NorR regulatory protein senses nitric oxide (NO) to activate genes required for NO detoxification under anaerobic and microaerobic conditions in Escherichia coli. NorR belongs to the σ54-dependent family of transcriptional activators and contains an N-terminal regulatory GAF (cGMP phosphodiesterase, adenylate cyclase, FhlA) domain that controls the ATPase activity of the central AAA+ domain to regulate productive interactions with σ54. Binding of NO to a non-heme iron center in the GAF domain results in the formation of a mononitrosyl-iron complex and releases intramolecular repression of the AAA+ domain to enable activation of transcription. In this study, we have further characterized NorR spectroscopically and substituted conserved residues in the GAF domain. This analysis, in combination with structural modeling of the GAF domain, has identified five candidate ligands to the non-heme iron and suggests a model in which the metal ion is coordinated in a pseudo-octahedral environment by three aspartate residues, an arginine, and a cysteine. |
| doi_str_mv | 10.1074/jbc.M705850200 |
| format | Article |
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NorR belongs to the σ54-dependent family of transcriptional activators and contains an N-terminal regulatory GAF (cGMP phosphodiesterase, adenylate cyclase, FhlA) domain that controls the ATPase activity of the central AAA+ domain to regulate productive interactions with σ54. Binding of NO to a non-heme iron center in the GAF domain results in the formation of a mononitrosyl-iron complex and releases intramolecular repression of the AAA+ domain to enable activation of transcription. In this study, we have further characterized NorR spectroscopically and substituted conserved residues in the GAF domain. This analysis, in combination with structural modeling of the GAF domain, has identified five candidate ligands to the non-heme iron and suggests a model in which the metal ion is coordinated in a pseudo-octahedral environment by three aspartate residues, an arginine, and a cysteine.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M705850200</identifier><identifier>PMID: 18003617</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Electron Spin Resonance Spectroscopy ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - genetics ; Escherichia coli Proteins - metabolism ; Inactivation, Metabolic ; Iron - analysis ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nitric Oxide - metabolism ; Nitric Oxide - toxicity ; Protein Conformation ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Spectrophotometry ; Trans-Activators - chemistry ; Trans-Activators - genetics ; Trans-Activators - metabolism ; Transcriptional Activation</subject><ispartof>The Journal of biological chemistry, 2008-01, Vol.283 (2), p.908-918</ispartof><rights>2008 © 2008 ASBMB. 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NorR belongs to the σ54-dependent family of transcriptional activators and contains an N-terminal regulatory GAF (cGMP phosphodiesterase, adenylate cyclase, FhlA) domain that controls the ATPase activity of the central AAA+ domain to regulate productive interactions with σ54. Binding of NO to a non-heme iron center in the GAF domain results in the formation of a mononitrosyl-iron complex and releases intramolecular repression of the AAA+ domain to enable activation of transcription. In this study, we have further characterized NorR spectroscopically and substituted conserved residues in the GAF domain. This analysis, in combination with structural modeling of the GAF domain, has identified five candidate ligands to the non-heme iron and suggests a model in which the metal ion is coordinated in a pseudo-octahedral environment by three aspartate residues, an arginine, and a cysteine.</description><subject>Amino Acid Sequence</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - genetics</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Inactivation, Metabolic</subject><subject>Iron - analysis</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nitric Oxide - metabolism</subject><subject>Nitric Oxide - toxicity</subject><subject>Protein Conformation</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Spectrophotometry</subject><subject>Trans-Activators - chemistry</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><subject>Transcriptional Activation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1vEzEQhi0EoiFw5Qjmwm3DjL0f9rGK-KhUWlSo1Jvl9c4mrjZ2a2-A_Hs22kg9MZe5PPPO6BnG3iKsEJry033rVt8bqFQFAuAZWyAoWcgK756zBYDAQotKnbFXOd_DVKXGl-wMFYCssVmwu_Ngh0P2mceej1viV35M3vHrv76jIlPIPmz4VQzFlnbEL1IMfE1hpMR9mAdiuuE3tNkPdozpwH-kOJIPr9mL3g6Z3pz6kt1--fxr_a24vP56sT6_LFxZy7FAKaUW0MumddpVvbXQW0e67SQgEJS1pcrKRuumVQpr0CgQe6y1dNj1Ti7Zxzn3IcXHPeXR7Hx2NAw2UNxnI0CVopHVBK5m0KWYc6LePCS_s-lgEMzRpZlcmieX08C7U_K-3VH3hJ_kTcCHGdj6zfaPT2RaH93kyQgljTB6esWSvZ-Z3kZjN8lnc_tTAEo43qXwuEbNBE2WfntKJjtPwVE3JbrRdNH_78J_mEyVqA</recordid><startdate>20080111</startdate><enddate>20080111</enddate><creator>Tucker, Nicholas P.</creator><creator>D'Autréaux, Benoît</creator><creator>Yousafzai, Faridoon K.</creator><creator>Fairhurst, Shirley A.</creator><creator>Spiro, Stephen</creator><creator>Dixon, Ray</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>7TM</scope><scope>C1K</scope></search><sort><creationdate>20080111</creationdate><title>Analysis of the Nitric Oxide-sensing Non-heme Iron Center in the NorR Regulatory Protein</title><author>Tucker, Nicholas P. ; D'Autréaux, Benoît ; Yousafzai, Faridoon K. ; Fairhurst, Shirley A. ; Spiro, Stephen ; Dixon, Ray</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-1333920f37bc9c5faa0face9bd3010e046ae5a37997b8816091211f1693c1dfc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - genetics</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Inactivation, Metabolic</topic><topic>Iron - analysis</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nitric Oxide - metabolism</topic><topic>Nitric Oxide - toxicity</topic><topic>Protein Conformation</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Spectrophotometry</topic><topic>Trans-Activators - chemistry</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - metabolism</topic><topic>Transcriptional Activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tucker, Nicholas P.</creatorcontrib><creatorcontrib>D'Autréaux, Benoît</creatorcontrib><creatorcontrib>Yousafzai, Faridoon K.</creatorcontrib><creatorcontrib>Fairhurst, Shirley A.</creatorcontrib><creatorcontrib>Spiro, Stephen</creatorcontrib><creatorcontrib>Dixon, Ray</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tucker, Nicholas P.</au><au>D'Autréaux, Benoît</au><au>Yousafzai, Faridoon K.</au><au>Fairhurst, Shirley A.</au><au>Spiro, Stephen</au><au>Dixon, Ray</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the Nitric Oxide-sensing Non-heme Iron Center in the NorR Regulatory Protein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2008-01-11</date><risdate>2008</risdate><volume>283</volume><issue>2</issue><spage>908</spage><epage>918</epage><pages>908-918</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The NorR regulatory protein senses nitric oxide (NO) to activate genes required for NO detoxification under anaerobic and microaerobic conditions in Escherichia coli. NorR belongs to the σ54-dependent family of transcriptional activators and contains an N-terminal regulatory GAF (cGMP phosphodiesterase, adenylate cyclase, FhlA) domain that controls the ATPase activity of the central AAA+ domain to regulate productive interactions with σ54. Binding of NO to a non-heme iron center in the GAF domain results in the formation of a mononitrosyl-iron complex and releases intramolecular repression of the AAA+ domain to enable activation of transcription. In this study, we have further characterized NorR spectroscopically and substituted conserved residues in the GAF domain. 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| subjects | Amino Acid Sequence Electron Spin Resonance Spectroscopy Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Inactivation, Metabolic Iron - analysis Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nitric Oxide - metabolism Nitric Oxide - toxicity Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Spectrophotometry Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism Transcriptional Activation |
| title | Analysis of the Nitric Oxide-sensing Non-heme Iron Center in the NorR Regulatory Protein |
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