Pulse-chase SILAC-based analyses reveal selective oversynthesis and rapid turnover of mitochondrial protein components of respiratory complexes.
Identifieur interne : 000052 ( Main/Exploration ); précédent : 000051; suivant : 000053Pulse-chase SILAC-based analyses reveal selective oversynthesis and rapid turnover of mitochondrial protein components of respiratory complexes.
Auteurs : Daniel F. Bogenhagen [États-Unis] ; John D. Haley [États-Unis]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2020.
Descripteurs français
- KwdFr :
- ADN (génétique), Cellules HeLa (MeSH), Complexe I de la chaîne respiratoire (composition chimique), Complexe I de la chaîne respiratoire (génétique), Ferrosulfoprotéines (génétique), Humains (MeSH), Marquage isotopique (méthodes), Membranes mitochondriales (métabolisme), Mitochondries (génétique), NADH dehydrogenase (composition chimique), NADH dehydrogenase (génétique), Noyau de la cellule (génétique), Peptides (génétique), Proton-Translocating ATPases (composition chimique), Proton-Translocating ATPases (génétique), Protéines mitochondriales (génétique), Ribosomes mitochondriaux (métabolisme), Techniques de culture cellulaire (méthodes), Transport d'électrons (génétique), Transport des protéines (génétique).
- MESH :
- composition chimique : Complexe I de la chaîne respiratoire, NADH dehydrogenase, Proton-Translocating ATPases.
- génétique : ADN, Complexe I de la chaîne respiratoire, Ferrosulfoprotéines, Mitochondries, NADH dehydrogenase, Noyau de la cellule, Peptides, Proton-Translocating ATPases, Protéines mitochondriales, Transport d'électrons, Transport des protéines.
- métabolisme : Membranes mitochondriales, Ribosomes mitochondriaux.
- méthodes : Marquage isotopique, Techniques de culture cellulaire.
- Cellules HeLa, Humains.
English descriptors
- KwdEn :
- Cell Culture Techniques (methods), Cell Nucleus (genetics), DNA (genetics), Electron Transport (genetics), Electron Transport Complex I (chemistry), Electron Transport Complex I (genetics), HeLa Cells (MeSH), Humans (MeSH), Iron-Sulfur Proteins (genetics), Isotope Labeling (methods), Mitochondria (genetics), Mitochondrial Membranes (metabolism), Mitochondrial Proteins (genetics), Mitochondrial Ribosomes (metabolism), NADH Dehydrogenase (chemistry), NADH Dehydrogenase (genetics), Peptides (genetics), Protein Transport (genetics), Proton-Translocating ATPases (chemistry), Proton-Translocating ATPases (genetics).
- MESH :
- chemical , chemistry : Electron Transport Complex I, NADH Dehydrogenase, Proton-Translocating ATPases.
- chemical , genetics : DNA, Electron Transport Complex I, Iron-Sulfur Proteins, Mitochondrial Proteins, NADH Dehydrogenase, Peptides, Proton-Translocating ATPases.
- genetics : Cell Nucleus, Electron Transport, Mitochondria, Protein Transport.
- metabolism : Mitochondrial Membranes, Mitochondrial Ribosomes.
- methods : Cell Culture Techniques, Isotope Labeling.
- HeLa Cells, Humans.
Abstract
Mammalian mitochondria assemble four complexes of the respiratory chain (RCI, RCIII, RCIV, and RCV) by combining 13 polypeptides synthesized within mitochondria on mitochondrial ribosomes (mitoribosomes) with over 70 polypeptides encoded in nuclear DNA, translated on cytoplasmic ribosomes, and imported into mitochondria. We have previously observed that mitoribosome assembly is inefficient because some mitoribosomal proteins are produced in excess, but whether this is the case for other mitochondrial assemblies such as the RCs is unclear. We report here that pulse-chase stable isotope labeling with amino acids in cell culture (SILAC) is a valuable technique to study RC assembly because it can reveal considerable differences in the assembly rates and efficiencies of the different complexes. The SILAC analyses of HeLa cells indicated that assembly of RCV, comprising F1/Fo-ATPase, is rapid with little excess subunit synthesis, but that assembly of RCI (i.e. NADH dehydrogenase) is far less efficient, with dramatic oversynthesis of numerous proteins, particularly in the matrix-exposed N and Q domains. Unassembled subunits were generally degraded within 3 h. We also observed differential assembly kinetics for individual complexes that were immunoprecipitated with complex-specific antibodies. Immunoprecipitation with an antibody that recognizes the ND1 subunit of RCI co-precipitated a number of proteins implicated in FeS cluster assembly and newly synthesized ubiquinol-cytochrome c reductase Rieske iron-sulfur polypeptide 1 (UQCRFS1), the Rieske FeS protein in RCIII, reflecting some coordination between RCI and RCIII assemblies. We propose that pulse-chase SILAC labeling is a useful tool for studying rates of protein complex assembly and degradation.
DOI: 10.1074/jbc.RA119.011791
PubMed: 31974161
PubMed Central: PMC7049976
Affiliations:
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HeLa</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mammalian mitochondria assemble four complexes of the respiratory chain (RCI, RCIII, RCIV, and RCV) by combining 13 polypeptides synthesized within mitochondria on mitochondrial ribosomes (mitoribosomes) with over 70 polypeptides encoded in nuclear DNA, translated on cytoplasmic ribosomes, and imported into mitochondria. We have previously observed that mitoribosome assembly is inefficient because some mitoribosomal proteins are produced in excess, but whether this is the case for other mitochondrial assemblies such as the RCs is unclear. We report here that pulse-chase stable isotope labeling with amino acids in cell culture (SILAC) is a valuable technique to study RC assembly because it can reveal considerable differences in the assembly rates and efficiencies of the different complexes. The SILAC analyses of HeLa cells indicated that assembly of RCV, comprising F<sub>1</sub>/F<sub>o</sub>-ATPase, is rapid with little excess subunit synthesis, but that assembly of RCI (<i>i.e.</i> NADH dehydrogenase) is far less efficient, with dramatic oversynthesis of numerous proteins, particularly in the matrix-exposed N and Q domains. Unassembled subunits were generally degraded within 3 h. We also observed differential assembly kinetics for individual complexes that were immunoprecipitated with complex-specific antibodies. Immunoprecipitation with an antibody that recognizes the ND1 subunit of RCI co-precipitated a number of proteins implicated in FeS cluster assembly and newly synthesized ubiquinol-cytochrome <i>c</i> reductase Rieske iron-sulfur polypeptide 1 (UQCRFS1), the Rieske FeS protein in RCIII, reflecting some coordination between RCI and RCIII assemblies. We propose that pulse-chase SILAC labeling is a useful tool for studying rates of protein complex assembly and degradation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31974161</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>295</Volume><Issue>9</Issue><PubDate><Year>2020</Year><Month>02</Month><Day>28</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Pulse-chase SILAC-based analyses reveal selective oversynthesis and rapid turnover of mitochondrial protein components of respiratory complexes.</ArticleTitle><Pagination><MedlinePgn>2544-2554</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA119.011791</ELocationID><Abstract><AbstractText>Mammalian mitochondria assemble four complexes of the respiratory chain (RCI, RCIII, RCIV, and RCV) by combining 13 polypeptides synthesized within mitochondria on mitochondrial ribosomes (mitoribosomes) with over 70 polypeptides encoded in nuclear DNA, translated on cytoplasmic ribosomes, and imported into mitochondria. We have previously observed that mitoribosome assembly is inefficient because some mitoribosomal proteins are produced in excess, but whether this is the case for other mitochondrial assemblies such as the RCs is unclear. We report here that pulse-chase stable isotope labeling with amino acids in cell culture (SILAC) is a valuable technique to study RC assembly because it can reveal considerable differences in the assembly rates and efficiencies of the different complexes. The SILAC analyses of HeLa cells indicated that assembly of RCV, comprising F<sub>1</sub>/F<sub>o</sub>-ATPase, is rapid with little excess subunit synthesis, but that assembly of RCI (<i>i.e.</i> NADH dehydrogenase) is far less efficient, with dramatic oversynthesis of numerous proteins, particularly in the matrix-exposed N and Q domains. Unassembled subunits were generally degraded within 3 h. We also observed differential assembly kinetics for individual complexes that were immunoprecipitated with complex-specific antibodies. Immunoprecipitation with an antibody that recognizes the ND1 subunit of RCI co-precipitated a number of proteins implicated in FeS cluster assembly and newly synthesized ubiquinol-cytochrome <i>c</i> reductase Rieske iron-sulfur polypeptide 1 (UQCRFS1), the Rieske FeS protein in RCIII, reflecting some coordination between RCI and RCIII assemblies. We propose that pulse-chase SILAC labeling is a useful tool for studying rates of protein complex assembly and degradation.</AbstractText><CopyrightInformation>© 2020 Bogenhagen and Haley.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bogenhagen</LastName><ForeName>Daniel F</ForeName><Initials>DF</Initials><Identifier Source="ORCID">0000-0002-9993-2574</Identifier><AffiliationInfo><Affiliation>Department of Pharmacological Sciences, Stony Brook University, Stony Brook, New York 11794-8651 daniel.bogenhagen@stonybrook.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haley</LastName><ForeName>John D</ForeName><Initials>JD</Initials><Identifier Source="ORCID">0000-0002-0283-6413</Identifier><AffiliationInfo><Affiliation>Department of Pathology, Stony Brook University, Stony Brook, New York 11794-8691.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Proteomics Center, Stony Brook University, Stony Brook, New 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human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.3.14</RegistryNumber><NameOfSubstance UI="D006180">Proton-Translocating ATPases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 7.1.1.2</RegistryNumber><NameOfSubstance UI="D042967">Electron Transport Complex I</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D018929" MajorTopicYN="N">Cell Culture Techniques</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004247" MajorTopicYN="N">DNA</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042967" MajorTopicYN="N">Electron Transport Complex I</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007553" MajorTopicYN="N">Isotope Labeling</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008928" 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MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006180" MajorTopicYN="N">Proton-Translocating ATPases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">NADH dehydrogenase</Keyword><Keyword MajorTopicYN="Y">mitochondria</Keyword><Keyword MajorTopicYN="Y">mitochondrial biogenesis</Keyword><Keyword MajorTopicYN="Y">mitochondrial respiratory chain complex</Keyword><Keyword MajorTopicYN="Y">oxidative phosphorylation system</Keyword><Keyword MajorTopicYN="Y">protein assembly</Keyword><Keyword MajorTopicYN="Y">protein dynamics</Keyword><Keyword MajorTopicYN="Y">protein synthesis</Keyword><Keyword MajorTopicYN="Y">protein turnover</Keyword><Keyword MajorTopicYN="Y">proteomics</Keyword><Keyword MajorTopicYN="Y">respiratory complex assembly</Keyword><Keyword MajorTopicYN="Y">stable isotope labeling with amino acids in cell culture (SILAC)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>11</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>01</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>1</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Bogenhagen</name></noRegion><name sortKey="Haley, John D" sort="Haley, John D" uniqKey="Haley J" first="John D" last="Haley">John D. Haley</name><name sortKey="Haley, John D" sort="Haley, John D" uniqKey="Haley J" first="John D" last="Haley">John D. Haley</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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