Now showing 1 - 2 of 2
  • 2019Journal Article
    [["dc.bibliographiccitation.firstpage","598"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","614"],["dc.bibliographiccitation.volume","218"],["dc.contributor.author","Richter, Frank"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Nikolov, Miroslav"],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Aich, Abhishek"],["dc.contributor.author","MacVicar, Thomas"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Langer, Thomas"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2019-07-09T11:50:27Z"],["dc.date.available","2019-07-09T11:50:27Z"],["dc.date.issued","2019"],["dc.description.abstract","The mitochondrial presequence translocation machinery (TIM23 complex) is conserved between the yeast Saccharomyces cerevisiae and humans; however, functional characterization has been mainly performed in yeast. Here, we define the constituents of the human TIM23 complex using mass spectrometry and identified ROMO1 as a new translocase constituent with an exceptionally short half-life. Analyses of a ROMO1 knockout cell line revealed aberrant inner membrane structure and altered processing of the GTPase OPA1. We show that in the absence of ROMO1, mitochondria lose the inner membrane YME1L protease, which participates in OPA1 processing and ROMO1 turnover. While ROMO1 is dispensable for general protein import along the presequence pathway, we show that it participates in the dynamics of TIM21 during respiratory chain biogenesis and is specifically required for import of YME1L. This selective import defect can be linked to charge distribution in the unusually long targeting sequence of YME1L. Our analyses establish an unexpected link between mitochondrial protein import and inner membrane protein quality control."],["dc.identifier.doi","10.1083/jcb.201806093"],["dc.identifier.pmid","30598479"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15943"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59776"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation.issn","1540-8140"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","ROMO1 is a constituent of the human presequence translocase required for YME1L protease import"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC
  • 2016Journal Article Research Paper
    [["dc.bibliographiccitation.firstpage","4147"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","4158"],["dc.bibliographiccitation.volume","590"],["dc.contributor.author","Callegari, Sylvie"],["dc.contributor.author","Richter, Frank"],["dc.contributor.author","Chojnacka, Katarzyna"],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Lorenzi, Isotta"],["dc.contributor.author","Pacheu-Grau, David"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:53:09Z"],["dc.date.available","2017-09-07T11:53:09Z"],["dc.date.issued","2016"],["dc.description.abstract","Hydrophobic inner mitochondrial membrane proteins with internal targeting signals, such as the metabolite carriers, use the carrier translocase (TIM22 complex) for transport into the inner membrane. Defects in this transport pathway have been associated with neurodegenerative disorders. While the TIM22 complex is well studied in baker's yeast, very little is known about the mammalian TIM22 complex. Using immunoprecipitation, we purified the human carrier translocase and identified a mitochondrial inner membrane protein TIM29 as a novel component, specific to metazoa. We show that TIM29 is a constituent of the 440 kDa TIM22 complex and interacts with oxidized TIM22. Our analyses demonstrate that TIM29 is required for the structural integrity of the TIM22 complex and for import of substrate proteins by the carrier translocase."],["dc.identifier.doi","10.1002/1873-3468.12450"],["dc.identifier.fs","625768"],["dc.identifier.gro","3145043"],["dc.identifier.pmid","27718247"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14166"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2736"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/59"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.issn","0014-5793"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","TIM29 is a subunit of the human carrier translocase required for protein transport"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC