Studying protein import into mitochondria.
Identifieur interne : 000032 ( Main/Exploration ); précédent : 000031; suivant : 000033Studying protein import into mitochondria.
Auteurs : Chantal Priesnitz [Allemagne] ; Nikolaus Pfanner [Allemagne] ; Thomas Becker [Allemagne]Source :
- Methods in cell biology [ 0091-679X ] ; 2020.
Abstract
Mitochondria are deeply integrated into crucial functions of eukaryotic cells, including ATP production via oxidative phosphorylation, biosynthesis of iron-sulfur clusters, amino acids, lipids and heme, signaling pathways, and programmed cell death. The import of about 1000 different proteins that are produced as precursors on cytosolic ribosomes is essential for mitochondrial functions and biogenesis. The translocase of the outer mitochondrial membrane (TOM) forms the entry gate for the vast majority of mitochondrial proteins. Research of the last years has uncovered a complicated network of protein translocases and pathways that sort proteins into the mitochondrial subcompartments: outer and inner membranes, intermembrane space, and matrix. The in vitro import of a large number of different precursor proteins into mitochondria has been a pivotal experimental assay to identify these protein-sorting routes. This experimental set-up enables studies on the kinetics of protein transport into isolated mitochondria, on the processing of precursor proteins, and on their assembly into functional protein machineries. In vitro protein import assays are widely used and are indispensable for research on mitochondrial protein biogenesis.
DOI: 10.1016/bs.mcb.2019.11.006
PubMed: 32183973
Affiliations:
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Electronic address: thomas.becker@biochemie.uni-freiburg.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, 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">Methods in cell biology</title><idno type="ISSN">0091-679X</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 deeply integrated into crucial functions of eukaryotic cells, including ATP production via oxidative phosphorylation, biosynthesis of iron-sulfur clusters, amino acids, lipids and heme, signaling pathways, and programmed cell death. The import of about 1000 different proteins that are produced as precursors on cytosolic ribosomes is essential for mitochondrial functions and biogenesis. The translocase of the outer mitochondrial membrane (TOM) forms the entry gate for the vast majority of mitochondrial proteins. Research of the last years has uncovered a complicated network of protein translocases and pathways that sort proteins into the mitochondrial subcompartments: outer and inner membranes, intermembrane space, and matrix. The in vitro import of a large number of different precursor proteins into mitochondria has been a pivotal experimental assay to identify these protein-sorting routes. This experimental set-up enables studies on the kinetics of protein transport into isolated mitochondria, on the processing of precursor proteins, and on their assembly into functional protein machineries. In vitro protein import assays are widely used and are indispensable for research on mitochondrial protein biogenesis.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32183973</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0091-679X</ISSN><JournalIssue CitedMedium="Internet"><Volume>155</Volume><PubDate><Year>2020</Year></PubDate></JournalIssue><Title>Methods in cell biology</Title><ISOAbbreviation>Methods Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Studying protein import into mitochondria.</ArticleTitle><Pagination><MedlinePgn>45-79</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0091-679X(19)30136-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/bs.mcb.2019.11.006</ELocationID><Abstract><AbstractText>Mitochondria are deeply integrated into crucial functions of eukaryotic cells, including ATP production via oxidative phosphorylation, biosynthesis of iron-sulfur clusters, amino acids, lipids and heme, signaling pathways, and programmed cell death. The import of about 1000 different proteins that are produced as precursors on cytosolic ribosomes is essential for mitochondrial functions and biogenesis. The translocase of the outer mitochondrial membrane (TOM) forms the entry gate for the vast majority of mitochondrial proteins. Research of the last years has uncovered a complicated network of protein translocases and pathways that sort proteins into the mitochondrial subcompartments: outer and inner membranes, intermembrane space, and matrix. The in vitro import of a large number of different precursor proteins into mitochondria has been a pivotal experimental assay to identify these protein-sorting routes. This experimental set-up enables studies on the kinetics of protein transport into isolated mitochondria, on the processing of precursor proteins, and on their assembly into functional protein machineries. In vitro protein import assays are widely used and are indispensable for research on mitochondrial protein biogenesis.</AbstractText><CopyrightInformation>© 2020 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Priesnitz</LastName><ForeName>Chantal</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; Faculty of Biology, University of Freiburg, Freiburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pfanner</LastName><ForeName>Nikolaus</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany. Electronic address: nikolaus.pfanner@biochemie.uni-freiburg.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Becker</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany; CIBSS Centre for Integrative Biological Signalling Studies, University of Freiburg, Freiburg, Germany. Electronic address: thomas.becker@biochemie.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>2019</Year><Month>12</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Methods Cell Biol</MedlineTA><NlmUniqueID>0373334</NlmUniqueID><ISSNLinking>0091-679X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Blue native electrophoresis</Keyword><Keyword MajorTopicYN="Y">Mitochondria</Keyword><Keyword MajorTopicYN="Y">Protein assembly</Keyword><Keyword MajorTopicYN="Y">Protein import</Keyword><Keyword MajorTopicYN="Y">Protein sorting</Keyword><Keyword MajorTopicYN="Y">TIM23 complex</Keyword><Keyword MajorTopicYN="Y">TOM complex</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32183973</ArticleId><ArticleId IdType="pii">S0091-679X(19)30136-0</ArticleId><ArticleId IdType="doi">10.1016/bs.mcb.2019.11.006</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="Priesnitz, Chantal" sort="Priesnitz, Chantal" uniqKey="Priesnitz C" first="Chantal" last="Priesnitz">Chantal Priesnitz</name></region><name sortKey="Becker, Thomas" sort="Becker, Thomas" uniqKey="Becker T" first="Thomas" last="Becker">Thomas Becker</name><name sortKey="Pfanner, Nikolaus" sort="Pfanner, Nikolaus" uniqKey="Pfanner N" first="Nikolaus" last="Pfanner">Nikolaus Pfanner</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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