Naumenko, Nataliia

[["dc.bibliographiccitation.artnumber","1237"],["dc.bibliographiccitation.firstpage","1237"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.lastpage","1"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Morgenstern, Marcel"],["dc.contributor.author","Rucktäschel, Robert"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-01-09T14:08:26Z"],["dc.date.available","2018-01-09T14:08:26Z"],["dc.date.issued","2017"],["dc.description.abstract","The F1F0-ATP synthase translates a proton flux across the inner mitochondrial membrane into a mechanical rotation, driving anhydride bond formation in the catalytic portion. The complex's membrane-embedded motor forms a proteinaceous channel at the interface between Atp9 ring and Atp6. To prevent unrestricted proton flow dissipating the H+-gradient, channel formation is a critical and tightly controlled step during ATP synthase assembly. Here we show that the INA complex (INAC) acts at this decisive step promoting Atp9-ring association with Atp6. INAC binds to newly synthesized mitochondrial-encoded Atp6 and Atp8 in complex with maturation factors. INAC association is retained until the F1-portion is built on Atp6/8 and loss of INAC causes accumulation of the free F1. An independent complex is formed between INAC and the Atp9 ring. We conclude that INAC maintains assembly intermediates of the F1 F0-ATP synthase in a primed state for the terminal assembly step-motor module formation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2017"],["dc.format.extent","1"],["dc.identifier.doi","10.1038/s41467-017-01437-z"],["dc.identifier.pmid","29093463"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14823"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11598"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","INA complex liaises the F1Fo-ATP synthase membrane motor modules"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Naumenko, N."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2018-11-07T10:19:35Z"],["dc.date.available","2018-11-07T10:19:35Z"],["dc.date.issued","2016"],["dc.identifier.isi","000396047200471"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41691"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.publisher.place","Bethesda"],["dc.relation.conference","Annual Meeting of the American-Society-for-Cell-Biology (ASCB)"],["dc.relation.eventlocation","San Francisco, CA"],["dc.relation.issn","1939-4586"],["dc.relation.issn","1059-1524"],["dc.title","INA complex links assembly of the nuclear- and mitochondrial-encoded modules of ATP synthase."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","1624"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","1727"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Naumenko, Nataliia"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","von der Malsburg, Karina"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Warscheid, Bettina"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:45:41Z"],["dc.date.available","2017-09-07T11:45:41Z"],["dc.date.issued","2014"],["dc.description.abstract","Mitochondrial F1Fo-ATP synthase generates the bulk of cellular ATP. This molecular machine assembles from nuclear- and mitochondria-encoded subunits. Whereas chaperones for formation of the matrix-exposed hexameric F-1-ATPase core domain have been identified, insight into how the nuclear-encoded F-1-domain assembles with the membrane-embedded F-o-region is lacking. Here we identified the INA complex (INAC) in the inner membrane of mitochondria as an assembly factor involved in this process. Ina22 and Ina17 are INAC constituents that physically associate with the F-1-module and peripheral stalk, but not with the assembled F1Fo-ATP synthase. Our analyses show that loss of Ina22 and Ina17 specifically impairs formation of the peripheral stalk that connects the catalytic F-1-module to the membrane embedded F-o-domain. We conclude that INAC represents a matrix-exposed inner membrane protein complex that facilitates peripheral stalk assembly and thus promotes a key step in the biogenesis of mitochondrial F1Fo-ATP synthase."],["dc.identifier.doi","10.15252/embj.201488076"],["dc.identifier.gro","3142082"],["dc.identifier.isi","000339917000005"],["dc.identifier.pmid","24942160"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4345"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]