Mechanistic concepts of iron-sulfur protein biogenesis in Biology.
Identifieur interne : 000049 ( Main/Exploration ); précédent : 000048; suivant : 000050Mechanistic concepts of iron-sulfur protein biogenesis in Biology.
Auteurs : Joseph J. Braymer [Allemagne] ; Sven A. Freibert [Allemagne] ; Magdalena Rakwalska-Bange [Allemagne] ; Roland Lill [Allemagne]Source :
- Biochimica et biophysica acta. Molecular cell research [ 1879-2596 ] ; 2020.
Abstract
Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are involved in numerous cellular processes such as respiration, photosynthesis, metabolic reactions, nitrogen fixation, radical biochemistry, protein synthesis, antiviral defense, and genome maintenance. Their versatile functions may go back to the proposed role of their Fe/S cofactors in the origin of life as efficient catalysts and electron carriers. More than two decades ago, it was discovered that the in vivo synthesis of cellular Fe/S clusters and their integration into polypeptide chains requires assistance by complex proteinaceous machineries, despite the fact that Fe/S proteins can be assembled chemically in vitro. In prokaryotes, three Fe/S protein biogenesis systems are known; ISC, SUF, and the more specialized NIF. The former two systems have been transferred by endosymbiosis from bacteria to mitochondria and plastids, respectively, of eukaryotes. In their cytosol, eukaryotes use the CIA machinery for the biogenesis of cytosolic and nuclear Fe/S proteins. Despite the structural diversity of the protein constituents of these four machineries, general mechanistic concepts underlie the complex process of Fe/S protein biogenesis. This review provides a comprehensive and comparative overview of the various known biogenesis systems in Biology, and summarizes their common or diverging molecular mechanisms, thereby illustrating both the conservation and diverse adaptions of these four machineries during evolution and under different lifestyles. Knowledge of these fundamental biochemical pathways is not only of basic scientific interest, but is important for the understanding of human 'Fe/S diseases' and can be used in biotechnology.
DOI: 10.1016/j.bbamcr.2020.118863
PubMed: 33007329
Affiliations:
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Braymer</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Freibert, Sven A" sort="Freibert, Sven A" uniqKey="Freibert S" first="Sven A" last="Freibert">Sven A. Freibert</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Rakwalska Bange, Magdalena" sort="Rakwalska Bange, Magdalena" uniqKey="Rakwalska Bange M" first="Magdalena" last="Rakwalska-Bange">Magdalena Rakwalska-Bange</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author><author><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; SYNMIKRO Center for Synthetic Microbiology, Philipps-Universität Marburg, Hans-Meerwein-Strasse, 35043 Marburg, Germany. Electronic address: Lill@staff.uni-marburg.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; SYNMIKRO Center for Synthetic Microbiology, Philipps-Universität Marburg, Hans-Meerwein-Strasse, 35043 Marburg</wicri:regionArea><placeName><region type="land" nuts="1">Hesse (Land)</region><region type="district" nuts="2">District de Giessen</region><settlement type="city">Marbourg</settlement></placeName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. Molecular cell research</title><idno type="eISSN">1879-2596</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">Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are involved in numerous cellular processes such as respiration, photosynthesis, metabolic reactions, nitrogen fixation, radical biochemistry, protein synthesis, antiviral defense, and genome maintenance. Their versatile functions may go back to the proposed role of their Fe/S cofactors in the origin of life as efficient catalysts and electron carriers. More than two decades ago, it was discovered that the in vivo synthesis of cellular Fe/S clusters and their integration into polypeptide chains requires assistance by complex proteinaceous machineries, despite the fact that Fe/S proteins can be assembled chemically in vitro. In prokaryotes, three Fe/S protein biogenesis systems are known; ISC, SUF, and the more specialized NIF. The former two systems have been transferred by endosymbiosis from bacteria to mitochondria and plastids, respectively, of eukaryotes. In their cytosol, eukaryotes use the CIA machinery for the biogenesis of cytosolic and nuclear Fe/S proteins. Despite the structural diversity of the protein constituents of these four machineries, general mechanistic concepts underlie the complex process of Fe/S protein biogenesis. This review provides a comprehensive and comparative overview of the various known biogenesis systems in Biology, and summarizes their common or diverging molecular mechanisms, thereby illustrating both the conservation and diverse adaptions of these four machineries during evolution and under different lifestyles. Knowledge of these fundamental biochemical pathways is not only of basic scientific interest, but is important for the understanding of human 'Fe/S diseases' and can be used in biotechnology.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33007329</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-2596</ISSN><JournalIssue CitedMedium="Internet"><Volume>1868</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>Sep</Month><Day>30</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Molecular cell research</Title><ISOAbbreviation>Biochim Biophys Acta Mol Cell Res</ISOAbbreviation></Journal><ArticleTitle>Mechanistic concepts of iron-sulfur protein biogenesis in Biology.</ArticleTitle><Pagination><MedlinePgn>118863</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0167-4889(20)30221-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamcr.2020.118863</ELocationID><Abstract><AbstractText>Iron-sulfur (Fe/S) proteins are present in virtually all living organisms and are involved in numerous cellular processes such as respiration, photosynthesis, metabolic reactions, nitrogen fixation, radical biochemistry, protein synthesis, antiviral defense, and genome maintenance. Their versatile functions may go back to the proposed role of their Fe/S cofactors in the origin of life as efficient catalysts and electron carriers. More than two decades ago, it was discovered that the in vivo synthesis of cellular Fe/S clusters and their integration into polypeptide chains requires assistance by complex proteinaceous machineries, despite the fact that Fe/S proteins can be assembled chemically in vitro. In prokaryotes, three Fe/S protein biogenesis systems are known; ISC, SUF, and the more specialized NIF. The former two systems have been transferred by endosymbiosis from bacteria to mitochondria and plastids, respectively, of eukaryotes. In their cytosol, eukaryotes use the CIA machinery for the biogenesis of cytosolic and nuclear Fe/S proteins. Despite the structural diversity of the protein constituents of these four machineries, general mechanistic concepts underlie the complex process of Fe/S protein biogenesis. This review provides a comprehensive and comparative overview of the various known biogenesis systems in Biology, and summarizes their common or diverging molecular mechanisms, thereby illustrating both the conservation and diverse adaptions of these four machineries during evolution and under different lifestyles. Knowledge of these fundamental biochemical pathways is not only of basic scientific interest, but is important for the understanding of human 'Fe/S diseases' and can be used in biotechnology.</AbstractText><CopyrightInformation>Copyright © 2020 The Author(s). Published by Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Braymer</LastName><ForeName>Joseph J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Freibert</LastName><ForeName>Sven A</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rakwalska-Bange</LastName><ForeName>Magdalena</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, Robert-Koch-Str. 6, 35032 Marburg, Germany; SYNMIKRO Center for Synthetic Microbiology, Philipps-Universität Marburg, Hans-Meerwein-Strasse, 35043 Marburg, Germany. Electronic address: Lill@staff.uni-marburg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Mol Cell Res</MedlineTA><NlmUniqueID>101731731</NlmUniqueID><ISSNLinking>0167-4889</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">CIA</Keyword><Keyword MajorTopicYN="N">Cysteine desulfurase</Keyword><Keyword MajorTopicYN="N">Fe/S cluster</Keyword><Keyword MajorTopicYN="N">Fe/S disease</Keyword><Keyword MajorTopicYN="N">Ferredoxin</Keyword><Keyword MajorTopicYN="N">Friedreich ataxia</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">ISC</Keyword><Keyword MajorTopicYN="N">MMDS</Keyword><Keyword MajorTopicYN="N">Mitochondria</Keyword><Keyword MajorTopicYN="N">Mitosomes</Keyword><Keyword MajorTopicYN="N">NIF</Keyword><Keyword MajorTopicYN="N">Plastids</Keyword><Keyword MajorTopicYN="N">Reductive evolution</Keyword><Keyword MajorTopicYN="N">SUF</Keyword><Keyword MajorTopicYN="N">Scaffold</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors are not aware of any affiliations, memberships, funding, or financial holdings that might be perceived as affecting the objectivity of this review.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>07</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>09</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>09</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>10</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>10</Month><Day>2</Day><Hour>20</Hour><Minute>9</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33007329</ArticleId><ArticleId IdType="pii">S0167-4889(20)30221-4</ArticleId><ArticleId IdType="doi">10.1016/j.bbamcr.2020.118863</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Giessen</li><li>Hesse (Land)</li></region><settlement><li>Marbourg</li></settlement></list><tree><country name="Allemagne"><region name="Hesse (Land)"><name sortKey="Braymer, Joseph J" sort="Braymer, Joseph J" uniqKey="Braymer J" first="Joseph J" last="Braymer">Joseph J. Braymer</name></region><name sortKey="Freibert, Sven A" sort="Freibert, Sven A" uniqKey="Freibert S" first="Sven A" last="Freibert">Sven A. Freibert</name><name sortKey="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</name><name sortKey="Rakwalska Bange, Magdalena" sort="Rakwalska Bange, Magdalena" uniqKey="Rakwalska Bange M" first="Magdalena" last="Rakwalska-Bange">Magdalena Rakwalska-Bange</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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