Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis.
Identifieur interne : 000081 ( Main/Exploration ); précédent : 000080; suivant : 000082Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis.
Auteurs : Roland Lill [Allemagne] ; Sven-A Freibert [Allemagne]Source :
- Annual review of biochemistry [ 1545-4509 ] ; 2020.
Abstract
Mitochondria are essential in most eukaryotes and are involved in numerous biological functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and steroid metabolism. Work over the past two decades has uncovered the biogenesis of cellular iron-sulfur (Fe/S) proteins as the essential and minimal function of mitochondria. This process is catalyzed by the bacteria-derived iron-sulfur cluster assembly (ISC) machinery and has been dissected into three major steps: de novo synthesis of a [2Fe-2S] cluster on a scaffold protein; Hsp70 chaperone-mediated trafficking of the cluster and insertion into [2Fe-2S] target apoproteins; and catalytic conversion of the [2Fe-2S] into a [4Fe-4S] cluster and subsequent insertion into recipient apoproteins. ISC components of the first two steps are also required for biogenesis of numerous essential cytosolic and nuclear Fe/S proteins, explaining the essentiality of mitochondria. This review summarizes the molecular mechanisms underlying the ISC protein-mediated maturation of mitochondrial Fe/S proteins and the importance for human disease.
DOI: 10.1146/annurev-biochem-013118-111540
PubMed: 31935115
Affiliations:
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email: Lill@staff.uni-marburg.de.</nlm:affiliation><country wicri:rule="url">Allemagne</country><wicri:regionArea>Institut für Zytobiologie, Philipps-Universität Marburg, 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></analytic><series><title level="j">Annual review of biochemistry</title><idno type="eISSN">1545-4509</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">Mitochondria are essential in most eukaryotes and are involved in numerous biological functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and steroid metabolism. Work over the past two decades has uncovered the biogenesis of cellular iron-sulfur (Fe/S) proteins as the essential and minimal function of mitochondria. This process is catalyzed by the bacteria-derived iron-sulfur cluster assembly (ISC) machinery and has been dissected into three major steps: de novo synthesis of a [2Fe-2S] cluster on a scaffold protein; Hsp70 chaperone-mediated trafficking of the cluster and insertion into [2Fe-2S] target apoproteins; and catalytic conversion of the [2Fe-2S] into a [4Fe-4S] cluster and subsequent insertion into recipient apoproteins. ISC components of the first two steps are also required for biogenesis of numerous essential cytosolic and nuclear Fe/S proteins, explaining the essentiality of mitochondria. This review summarizes the molecular mechanisms underlying the ISC protein-mediated maturation of mitochondrial Fe/S proteins and the importance for human disease.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">31935115</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1545-4509</ISSN><JournalIssue CitedMedium="Internet"><Volume>89</Volume><PubDate><Year>2020</Year><Month>06</Month><Day>20</Day></PubDate></JournalIssue><Title>Annual review of biochemistry</Title><ISOAbbreviation>Annu Rev Biochem</ISOAbbreviation></Journal><ArticleTitle>Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis.</ArticleTitle><Pagination><MedlinePgn>471-499</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1146/annurev-biochem-013118-111540</ELocationID><Abstract><AbstractText>Mitochondria are essential in most eukaryotes and are involved in numerous biological functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and steroid metabolism. Work over the past two decades has uncovered the biogenesis of cellular iron-sulfur (Fe/S) proteins as the essential and minimal function of mitochondria. This process is catalyzed by the bacteria-derived iron-sulfur cluster assembly (ISC) machinery and has been dissected into three major steps: de novo synthesis of a [2Fe-2S] cluster on a scaffold protein; Hsp70 chaperone-mediated trafficking of the cluster and insertion into [2Fe-2S] target apoproteins; and catalytic conversion of the [2Fe-2S] into a [4Fe-4S] cluster and subsequent insertion into recipient apoproteins. ISC components of the first two steps are also required for biogenesis of numerous essential cytosolic and nuclear Fe/S proteins, explaining the essentiality of mitochondria. This review summarizes the molecular mechanisms underlying the ISC protein-mediated maturation of mitochondrial Fe/S proteins and the importance for human disease.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lill</LastName><ForeName>Roland</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institut für Zytobiologie, Philipps-Universität Marburg, 35032 Marburg, Germany; email: Lill@staff.uni-marburg.de.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>SYNMIKRO Zentrum für synthetische Mikrobiologie, Philipps-Universität Marburg, 35043 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, 35032 Marburg, Germany; email: Lill@staff.uni-marburg.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>01</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Annu Rev Biochem</MedlineTA><NlmUniqueID>2985150R</NlmUniqueID><ISSNLinking>0066-4154</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">ABC protein</Keyword><Keyword MajorTopicYN="Y">CIA machinery</Keyword><Keyword MajorTopicYN="Y">FRDA</Keyword><Keyword MajorTopicYN="Y">Fe/S cluster</Keyword><Keyword MajorTopicYN="Y">Fe/S disease</Keyword><Keyword MajorTopicYN="Y">Friedrich's ataxia</Keyword><Keyword MajorTopicYN="Y">ISC machinery</Keyword><Keyword MajorTopicYN="Y">MMDS</Keyword><Keyword MajorTopicYN="Y">cysteine desulfurase</Keyword><Keyword MajorTopicYN="Y">cytosolic iron-sulfur protein assembly machinery</Keyword><Keyword MajorTopicYN="Y">ferredoxin</Keyword><Keyword MajorTopicYN="Y">frataxin</Keyword><Keyword MajorTopicYN="Y">glutaredoxin</Keyword><Keyword MajorTopicYN="Y">iron-sulfur cluster assembly machinery</Keyword><Keyword MajorTopicYN="Y">multiple mitochondrial dysfunction syndromes</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>1</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>1</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>1</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31935115</ArticleId><ArticleId IdType="doi">10.1146/annurev-biochem-013118-111540</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="Lill, Roland" sort="Lill, Roland" uniqKey="Lill R" first="Roland" last="Lill">Roland Lill</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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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