ErpA is important but not essential for the Fe/S cluster biogenesis of Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
Identifieur interne : 000138 ( Main/Exploration ); précédent : 000137; suivant : 000139ErpA is important but not essential for the Fe/S cluster biogenesis of Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
Auteurs : Sabrina Oppermann [Allemagne] ; Simon Höfflin [Allemagne] ; Thorsten Friedrich [Allemagne]Source :
- Biochimica et biophysica acta. Bioenergetics [ 1879-2650 ] ; 2020.
Abstract
Energy converting NADH:ubiquinone oxidoreductase, complex I, is the first enzyme of respiratory chains in most eukaryotes and many bacteria. The complex comprises a peripheral arm catalyzing electron transfer and a membrane arm involved in proton-translocation. In Escherichia coli, the peripheral arm features a non-covalently bound flavin mononucleotide and nine iron-sulfur (Fe/S)-clusters. Very little is known about the incorporation of the Fe/S-clusters into the E. coli complex I. ErpA, an A-type carrier protein is discussed to act as a Fe/S-cluster carrier protein. To contribute to the understanding of ErpA for the assembly of E. coli complex I, we analyzed an erpA knock-out strain. Deletion of erpA decreased the complex I content in cytoplasmic membranes to approximately one third and the NADH oxidase activity to one fifth. EPR spectroscopy showed the presence of all Fe/S-clusters of the complex in the membrane but only in minor quantities. Sucrose gradient centrifugation and native PAGE revealed the presence of a marginal amount of a stable and fully assembled complex extractable from the membrane. Thus, ErpA is not essential for the assembly of complex I but its absence leads to a strong decrease of a functional complex in the cytoplasmic membrane due to a major lack of all EPR-detectable Fe/S-clusters.
DOI: 10.1016/j.bbabio.2020.148286
PubMed: 32777304
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Electronic address: friedrich@bio.chemie.uni-freiburg.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Albert-Ludwigs-Universität, Institut für Biochemie, Albertstr. 21, D-79104 Freiburg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Fribourg-en-Brisgau</region><settlement type="city">Fribourg-en-Brisgau</settlement></placeName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. Bioenergetics</title><idno type="eISSN">1879-2650</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Energy converting NADH:ubiquinone oxidoreductase, complex I, is the first enzyme of respiratory chains in most eukaryotes and many bacteria. The complex comprises a peripheral arm catalyzing electron transfer and a membrane arm involved in proton-translocation. In Escherichia coli, the peripheral arm features a non-covalently bound flavin mononucleotide and nine iron-sulfur (Fe/S)-clusters. Very little is known about the incorporation of the Fe/S-clusters into the E. coli complex I. ErpA, an A-type carrier protein is discussed to act as a Fe/S-cluster carrier protein. To contribute to the understanding of ErpA for the assembly of E. coli complex I, we analyzed an erpA knock-out strain. Deletion of erpA decreased the complex I content in cytoplasmic membranes to approximately one third and the NADH oxidase activity to one fifth. EPR spectroscopy showed the presence of all Fe/S-clusters of the complex in the membrane but only in minor quantities. Sucrose gradient centrifugation and native PAGE revealed the presence of a marginal amount of a stable and fully assembled complex extractable from the membrane. Thus, ErpA is not essential for the assembly of complex I but its absence leads to a strong decrease of a functional complex in the cytoplasmic membrane due to a major lack of all EPR-detectable Fe/S-clusters.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32777304</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-2650</ISSN><JournalIssue CitedMedium="Internet"><Volume>1861</Volume><Issue>12</Issue><PubDate><Year>2020</Year><Month>12</Month><Day>01</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Bioenergetics</Title><ISOAbbreviation>Biochim Biophys Acta Bioenerg</ISOAbbreviation></Journal><ArticleTitle>ErpA is important but not essential for the Fe/S cluster biogenesis of Escherichia coli NADH:ubiquinone oxidoreductase (complex I).</ArticleTitle><Pagination><MedlinePgn>148286</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0005-2728(20)30136-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbabio.2020.148286</ELocationID><Abstract><AbstractText>Energy converting NADH:ubiquinone oxidoreductase, complex I, is the first enzyme of respiratory chains in most eukaryotes and many bacteria. The complex comprises a peripheral arm catalyzing electron transfer and a membrane arm involved in proton-translocation. In Escherichia coli, the peripheral arm features a non-covalently bound flavin mononucleotide and nine iron-sulfur (Fe/S)-clusters. Very little is known about the incorporation of the Fe/S-clusters into the E. coli complex I. ErpA, an A-type carrier protein is discussed to act as a Fe/S-cluster carrier protein. To contribute to the understanding of ErpA for the assembly of E. coli complex I, we analyzed an erpA knock-out strain. Deletion of erpA decreased the complex I content in cytoplasmic membranes to approximately one third and the NADH oxidase activity to one fifth. EPR spectroscopy showed the presence of all Fe/S-clusters of the complex in the membrane but only in minor quantities. Sucrose gradient centrifugation and native PAGE revealed the presence of a marginal amount of a stable and fully assembled complex extractable from the membrane. Thus, ErpA is not essential for the assembly of complex I but its absence leads to a strong decrease of a functional complex in the cytoplasmic membrane due to a major lack of all EPR-detectable Fe/S-clusters.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Oppermann</LastName><ForeName>Sabrina</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Albert-Ludwigs-Universität, Institut für Biochemie, Albertstr. 21, D-79104 Freiburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Höfflin</LastName><ForeName>Simon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Albert-Ludwigs-Universität, Institut für Biochemie, Albertstr. 21, D-79104 Freiburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Friedrich</LastName><ForeName>Thorsten</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Albert-Ludwigs-Universität, Institut für Biochemie, Albertstr. 21, D-79104 Freiburg, Germany. Electronic address: friedrich@bio.chemie.uni-freiburg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>08</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Bioenerg</MedlineTA><NlmUniqueID>101731706</NlmUniqueID><ISSNLinking>0005-2728</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Complex I</Keyword><Keyword MajorTopicYN="Y">EPR-spectroscopy</Keyword><Keyword MajorTopicYN="Y">Fe/S cluster biogenesis</Keyword><Keyword MajorTopicYN="Y">Iron‑sulfur cluster</Keyword><Keyword MajorTopicYN="Y">NADH dehydrogenase</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>05</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>07</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>8</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>8</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>8</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32777304</ArticleId><ArticleId IdType="pii">S0005-2728(20)30136-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbabio.2020.148286</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Fribourg-en-Brisgau</li></region><settlement><li>Fribourg-en-Brisgau</li></settlement></list><tree><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Oppermann, Sabrina" sort="Oppermann, Sabrina" uniqKey="Oppermann S" first="Sabrina" last="Oppermann">Sabrina Oppermann</name></region><name sortKey="Friedrich, Thorsten" sort="Friedrich, Thorsten" uniqKey="Friedrich T" first="Thorsten" last="Friedrich">Thorsten Friedrich</name><name sortKey="Hofflin, Simon" sort="Hofflin, Simon" uniqKey="Hofflin S" first="Simon" last="Höfflin">Simon Höfflin</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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