Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA.
Identifieur interne : 000229 ( Main/Exploration ); précédent : 000228; suivant : 000230Mechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA.
Auteurs : Ma Teresa Pellicer Martinez [Royaume-Uni] ; Jason C. Crack [Royaume-Uni] ; Melissa Yy Stewart [Royaume-Uni] ; Justin M. Bradley [Royaume-Uni] ; Dimitri A. Svistunenko [Royaume-Uni] ; Andrew Wb Johnston [Royaume-Uni] ; Myles R. Cheesman [Royaume-Uni] ; Jonathan D. Todd [Royaume-Uni] ; Nick E. Le Brun [Royaume-Uni]Source :
- eLife [ 2050-084X ] ; 2019.
Descripteurs français
- KwdFr :
- Fer (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Oxydoréduction (MeSH), Oxygène (métabolisme), Protéines bactériennes (composition chimique), Protéines bactériennes (métabolisme), Protéolyse (MeSH), Rhizobium (métabolisme), Spectrométrie de masse (MeSH), Spectroscopie de résonance de spin électronique (MeSH).
- MESH :
- composition chimique : Ferrosulfoprotéines, Protéines bactériennes.
- métabolisme : Fer, Ferrosulfoprotéines, Oxygène, Protéines bactériennes, Rhizobium.
- Oxydoréduction, Protéolyse, Spectrométrie de masse, Spectroscopie de résonance de spin électronique.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Electron Spin Resonance Spectroscopy (MeSH), Iron (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Mass Spectrometry (MeSH), Oxidation-Reduction (MeSH), Oxygen (metabolism), Proteolysis (MeSH), Rhizobium (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Bacterial Proteins, Iron, Iron-Sulfur Proteins, Oxygen.
- metabolism : Rhizobium.
- Electron Spin Resonance Spectroscopy, Mass Spectrometry, Oxidation-Reduction, Proteolysis.
Abstract
RirA is a global regulator of iron homeostasis in Rhizobium and related α-proteobacteria. In its [4Fe-4S] cluster-bound form it represses iron uptake by binding to IRO Box sequences upstream of RirA-regulated genes. Under low iron and/or aerobic conditions, [4Fe-4S] RirA undergoes cluster conversion/degradation to apo-RirA, which can no longer bind IRO Box sequences. Here, we apply time-resolved mass spectrometry and electron paramagnetic resonance spectroscopy to determine how the RirA cluster senses iron and O2. The data indicate that the key iron-sensing step is the O2-independent, reversible dissociation of Fe2+ from [4Fe-4S]2+ to form [3Fe-4S]0. The dissociation constant for this process was determined as Kd = ~3 µM, which is consistent with the sensing of 'free' iron in the cytoplasm. O2-sensing occurs through enhanced cluster degradation under aerobic conditions, via O2-mediated oxidation of the [3Fe-4S]0 intermediate to form [3Fe-4S]1+. This work provides a detailed mechanistic/functional view of an iron-responsive regulator.
DOI: 10.7554/eLife.47804
PubMed: 31526471
PubMed Central: PMC6748827
Affiliations:
Links toward previous steps (curation, corpus...)
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Crack</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Stewart, Melissa Yy" sort="Stewart, Melissa Yy" uniqKey="Stewart M" first="Melissa Yy" last="Stewart">Melissa Yy Stewart</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Bradley, Justin M" sort="Bradley, Justin M" uniqKey="Bradley J" first="Justin M" last="Bradley">Justin M. Bradley</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Svistunenko, Dimitri A" sort="Svistunenko, Dimitri A" uniqKey="Svistunenko D" first="Dimitri A" last="Svistunenko">Dimitri A. Svistunenko</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Essex, Colchester, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Essex, Colchester</wicri:regionArea><wicri:noRegion>Colchester</wicri:noRegion></affiliation></author><author><name sortKey="Johnston, Andrew Wb" sort="Johnston, Andrew Wb" uniqKey="Johnston A" first="Andrew Wb" last="Johnston">Andrew Wb Johnston</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Cheesman, Myles R" sort="Cheesman, Myles R" uniqKey="Cheesman M" first="Myles R" last="Cheesman">Myles R. Cheesman</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Todd, Jonathan D" sort="Todd, Jonathan D" uniqKey="Todd J" first="Jonathan D" last="Todd">Jonathan D. Todd</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author><author><name sortKey="Le Brun, Nick E" sort="Le Brun, Nick E" uniqKey="Le Brun N" first="Nick E" last="Le Brun">Nick E. Le Brun</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich</wicri:regionArea><wicri:noRegion>Norwich</wicri:noRegion></affiliation></author></analytic><series><title level="j">eLife</title><idno type="eISSN">2050-084X</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Electron Spin Resonance Spectroscopy (MeSH)</term><term>Iron (metabolism)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Mass Spectrometry (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxygen (metabolism)</term><term>Proteolysis (MeSH)</term><term>Rhizobium (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Oxygène (métabolisme)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéolyse (MeSH)</term><term>Rhizobium (métabolisme)</term><term>Spectrométrie de masse (MeSH)</term><term>Spectroscopie de résonance de spin électronique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Iron</term><term>Iron-Sulfur Proteins</term><term>Oxygen</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Rhizobium</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term><term>Ferrosulfoprotéines</term><term>Oxygène</term><term>Protéines bactériennes</term><term>Rhizobium</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Spin Resonance Spectroscopy</term><term>Mass Spectrometry</term><term>Oxidation-Reduction</term><term>Proteolysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term><term>Protéolyse</term><term>Spectrométrie de masse</term><term>Spectroscopie de résonance de spin électronique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">RirA is a global regulator of iron homeostasis in <i>Rhizobium</i> and related α-proteobacteria. In its [4Fe-4S] cluster-bound form it represses iron uptake by binding to IRO Box sequences upstream of RirA-regulated genes. Under low iron and/or aerobic conditions, [4Fe-4S] RirA undergoes cluster conversion/degradation to apo-RirA, which can no longer bind IRO Box sequences. Here, we apply time-resolved mass spectrometry and electron paramagnetic resonance spectroscopy to determine how the RirA cluster senses iron and O<sub>2</sub>. The data indicate that the key iron-sensing step is the O<sub>2</sub>-independent, reversible dissociation of Fe<sup>2+</sup> from [4Fe-4S]<sup>2+</sup> to form [3Fe-4S]<sup>0</sup>. The dissociation constant for this process was determined as <i>K</i><sub>d</sub> = ~3 µM, which is consistent with the sensing of 'free' iron in the cytoplasm. O<sub>2</sub>-sensing occurs through enhanced cluster degradation under aerobic conditions, via O<sub>2</sub>-mediated oxidation of the [3Fe-4S]<sup>0</sup> intermediate to form [3Fe-4S]<sup>1+</sup>. This work provides a detailed mechanistic/functional view of an iron-responsive regulator.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31526471</PMID><DateCompleted><Year>2020</Year><Month>02</Month><Day>14</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2050-084X</ISSN><JournalIssue CitedMedium="Internet"><Volume>8</Volume><PubDate><Year>2019</Year><Month>09</Month><Day>17</Day></PubDate></JournalIssue><Title>eLife</Title><ISOAbbreviation>Elife</ISOAbbreviation></Journal><ArticleTitle>Mechanisms of iron- and O<sub>2</sub>-sensing by the [4Fe-4S] cluster of the global iron regulator RirA.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.7554/eLife.47804</ELocationID><ELocationID EIdType="pii" ValidYN="Y">e47804</ELocationID><Abstract><AbstractText>RirA is a global regulator of iron homeostasis in <i>Rhizobium</i> and related α-proteobacteria. In its [4Fe-4S] cluster-bound form it represses iron uptake by binding to IRO Box sequences upstream of RirA-regulated genes. Under low iron and/or aerobic conditions, [4Fe-4S] RirA undergoes cluster conversion/degradation to apo-RirA, which can no longer bind IRO Box sequences. Here, we apply time-resolved mass spectrometry and electron paramagnetic resonance spectroscopy to determine how the RirA cluster senses iron and O<sub>2</sub>. The data indicate that the key iron-sensing step is the O<sub>2</sub>-independent, reversible dissociation of Fe<sup>2+</sup> from [4Fe-4S]<sup>2+</sup> to form [3Fe-4S]<sup>0</sup>. The dissociation constant for this process was determined as <i>K</i><sub>d</sub> = ~3 µM, which is consistent with the sensing of 'free' iron in the cytoplasm. O<sub>2</sub>-sensing occurs through enhanced cluster degradation under aerobic conditions, via O<sub>2</sub>-mediated oxidation of the [3Fe-4S]<sup>0</sup> intermediate to form [3Fe-4S]<sup>1+</sup>. This work provides a detailed mechanistic/functional view of an iron-responsive regulator.</AbstractText><CopyrightInformation>© 2019, Pellicer Martinez et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y" EqualContrib="Y"><LastName>Pellicer Martinez</LastName><ForeName>Ma Teresa</ForeName><Initials>MT</Initials><AffiliationInfo><Affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Crack</LastName><ForeName>Jason C</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y" EqualContrib="Y"><LastName>Stewart</LastName><ForeName>Melissa Yy</ForeName><Initials>MY</Initials><AffiliationInfo><Affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bradley</LastName><ForeName>Justin M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Svistunenko</LastName><ForeName>Dimitri A</ForeName><Initials>DA</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of Essex, Colchester, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Johnston</LastName><ForeName>Andrew Wb</ForeName><Initials>AW</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cheesman</LastName><ForeName>Myles R</ForeName><Initials>MR</Initials><AffiliationInfo><Affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Todd</LastName><ForeName>Jonathan D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Le Brun</LastName><ForeName>Nick E</ForeName><Initials>NE</Initials><Identifier Source="ORCID">0000-0001-9780-4061</Identifier><AffiliationInfo><Affiliation>Centre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, United Kingdom.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>BB/E003400/1</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/J003247/1</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/L006140/1</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>CA15133</GrantID><Agency>Horizon 2020 Framework Programme</Agency><Country>International</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>09</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Elife</MedlineTA><NlmUniqueID>101579614</NlmUniqueID><ISSNLinking>2050-084X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004578" MajorTopicYN="N">Electron Spin Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012231" MajorTopicYN="N">Rhizobium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">DNA regulation</Keyword><Keyword MajorTopicYN="Y">EPR</Keyword><Keyword MajorTopicYN="Y">biochemistry</Keyword><Keyword MajorTopicYN="Y">chemical biology</Keyword><Keyword MajorTopicYN="Y">iron sensor</Keyword><Keyword MajorTopicYN="Y">iron-sulfur</Keyword><Keyword MajorTopicYN="Y">mass spectrometry</Keyword><Keyword MajorTopicYN="Y">rhizobia</Keyword></KeywordList><CoiStatement>MP, JC, MS, JB, DS, AJ, MC, JT, NL No competing interests declared</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>04</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>07</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>2</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31526471</ArticleId><ArticleId IdType="doi">10.7554/eLife.47804</ArticleId><ArticleId IdType="pii">47804</ArticleId><ArticleId IdType="pmc">PMC6748827</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Microbiology. 2014 Jan;160(Pt 1):79-90</Citation><ArticleIdList><ArticleId 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