Analysis of the nitric oxide-sensing non-heme iron center in the NorR regulatory protein.
Identifieur interne : 002170 ( Main/Exploration ); précédent : 002169; suivant : 002171Analysis of the nitric oxide-sensing non-heme iron center in the NorR regulatory protein.
Auteurs : Nicholas P. Tucker [Royaume-Uni] ; Benoît D'Autréaux ; Faridoon K. Yousafzai ; Shirley A. Fairhurst ; Stephen Spiro ; Ray DixonSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Activation de la transcription (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Fer (analyse), Inactivation métabolique (MeSH), Modèles moléculaires (MeSH), Monoxyde d'azote (métabolisme), Monoxyde d'azote (toxicité), Mutagenèse dirigée (MeSH), Protéines Escherichia coli (composition chimique), Protéines Escherichia coli (génétique), Protéines Escherichia coli (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Spectrophotométrie (MeSH), Spectroscopie de résonance de spin électronique (MeSH), Séquence d'acides aminés (MeSH), Transactivateurs (composition chimique), Transactivateurs (génétique), Transactivateurs (métabolisme).
- MESH :
- analyse : Fer.
- composition chimique : Protéines Escherichia coli, Protéines recombinantes, Transactivateurs.
- génétique : Escherichia coli, Protéines Escherichia coli, Transactivateurs.
- métabolisme : Escherichia coli, Monoxyde d'azote, Protéines Escherichia coli, Protéines recombinantes, Transactivateurs.
- toxicité : Monoxyde d'azote.
- Activation de la transcription, Conformation des protéines, Données de séquences moléculaires, Inactivation métabolique, Modèles moléculaires, Mutagenèse dirigée, Spectrophotométrie, Spectroscopie de résonance de spin électronique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Electron Spin Resonance Spectroscopy (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Inactivation, Metabolic (MeSH), Iron (analysis), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Nitric Oxide (metabolism), Nitric Oxide (toxicity), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Spectrophotometry (MeSH), Trans-Activators (chemistry), Trans-Activators (genetics), Trans-Activators (metabolism), Transcriptional Activation (MeSH).
- MESH :
- chemical , analysis : Iron.
- chemical , chemistry : Escherichia coli Proteins, Recombinant Proteins, Trans-Activators.
- genetics : Escherichia coli, Escherichia coli Proteins, Trans-Activators.
- metabolism : Escherichia coli, Escherichia coli Proteins, Nitric Oxide, Recombinant Proteins, Trans-Activators.
- chemical , toxicity : Nitric Oxide.
- Amino Acid Sequence, Electron Spin Resonance Spectroscopy, Inactivation, Metabolic, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation, Spectrophotometry, Transcriptional Activation.
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 sigma(54)-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 sigma(54). 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: 10.1074/jbc.M705850200
PubMed: 18003617
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Tucker</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Microbiology, John Innes Centre, Colney, Norwich Research Park, Norwich NR4 7UH, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Molecular Microbiology, John Innes Centre, Colney, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="D Autreaux, Benoit" sort="D Autreaux, Benoit" uniqKey="D Autreaux B" first="Benoît" last="D'Autréaux">Benoît D'Autréaux</name></author><author><name sortKey="Yousafzai, Faridoon K" sort="Yousafzai, Faridoon K" uniqKey="Yousafzai F" first="Faridoon K" last="Yousafzai">Faridoon K. Yousafzai</name></author><author><name sortKey="Fairhurst, Shirley A" sort="Fairhurst, Shirley A" uniqKey="Fairhurst S" first="Shirley A" last="Fairhurst">Shirley A. 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(MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Nitric Oxide (metabolism)</term><term>Nitric Oxide (toxicity)</term><term>Protein Conformation (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Spectrophotometry (MeSH)</term><term>Trans-Activators (chemistry)</term><term>Trans-Activators (genetics)</term><term>Trans-Activators (metabolism)</term><term>Transcriptional Activation (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation de la transcription (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Fer (analyse)</term><term>Inactivation métabolique (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Monoxyde d'azote (métabolisme)</term><term>Monoxyde d'azote (toxicité)</term><term>Mutagenèse dirigée (MeSH)</term><term>Protéines Escherichia coli (composition chimique)</term><term>Protéines Escherichia coli (génétique)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Spectrophotométrie (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transactivateurs (composition chimique)</term><term>Transactivateurs (génétique)</term><term>Transactivateurs (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Iron</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term><term>Recombinant Proteins</term><term>Trans-Activators</term></keywords><keywords scheme="MESH" qualifier="analyse" 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électronique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 sigma(54)-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 sigma(54). 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18003617</PMID><DateCompleted><Year>2008</Year><Month>03</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>02</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Jan</Month><Day>11</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Analysis of the nitric oxide-sensing non-heme iron center in the NorR regulatory protein.</ArticleTitle><Pagination><MedlinePgn>908-18</MedlinePgn></Pagination><Abstract><AbstractText>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 sigma(54)-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 sigma(54). 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tucker</LastName><ForeName>Nicholas P</ForeName><Initials>NP</Initials><AffiliationInfo><Affiliation>Department of Molecular Microbiology, John Innes Centre, Colney, Norwich Research Park, Norwich NR4 7UH, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>D'Autréaux</LastName><ForeName>Benoît</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Yousafzai</LastName><ForeName>Faridoon K</ForeName><Initials>FK</Initials></Author><Author ValidYN="Y"><LastName>Fairhurst</LastName><ForeName>Shirley A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Spiro</LastName><ForeName>Stephen</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Dixon</LastName><ForeName>Ray</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>BB/D009588/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BBS/E/J/00000016</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>11</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C504602">NorR protein, E coli</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015534">Trans-Activators</NameOfSubstance></Chemical><Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber><NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="N">Escherichia coli Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008658" MajorTopicYN="N">Inactivation, Metabolic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009569" MajorTopicYN="N">Nitric Oxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015534" MajorTopicYN="N">Trans-Activators</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015533" MajorTopicYN="N">Transcriptional Activation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>11</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>3</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>11</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18003617</ArticleId><ArticleId IdType="pii">M705850200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M705850200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="D Autreaux, Benoit" sort="D Autreaux, Benoit" uniqKey="D Autreaux B" first="Benoît" last="D'Autréaux">Benoît D'Autréaux</name><name sortKey="Dixon, Ray" sort="Dixon, Ray" uniqKey="Dixon R" first="Ray" last="Dixon">Ray Dixon</name><name sortKey="Fairhurst, Shirley A" sort="Fairhurst, Shirley A" uniqKey="Fairhurst S" first="Shirley A" last="Fairhurst">Shirley A. Fairhurst</name><name sortKey="Spiro, Stephen" sort="Spiro, Stephen" uniqKey="Spiro S" first="Stephen" last="Spiro">Stephen Spiro</name><name sortKey="Yousafzai, Faridoon K" sort="Yousafzai, Faridoon K" uniqKey="Yousafzai F" first="Faridoon K" last="Yousafzai">Faridoon K. Yousafzai</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Tucker, Nicholas P" sort="Tucker, Nicholas P" uniqKey="Tucker N" first="Nicholas P" last="Tucker">Nicholas P. Tucker</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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