Meinecke, Michael

[["dc.bibliographiccitation.firstpage","2126"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","2134"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Montilla-Martinez, Malayko"],["dc.contributor.author","Beck, Sabrina"],["dc.contributor.author","Kluemper, Jessica"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Schliebs, Wolfgang"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2018-11-07T09:47:30Z"],["dc.date.available","2018-11-07T09:47:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Two peroxisomal targeting signals, PTS1 and PTS2, recognized by cytosolic receptors Pex5 and cooperating Pex7/Pex18, direct folded proteins to the peroxisomal matrix. A pore consisting of the PTS1 receptor Pex5 and the docking protein Pex14 imports PTS1 proteins. We identified a distinct PTS2-specific pore, which contains the PTS2 co-receptor Pex18 and the Pex14/Pex17-dockingcomplex as major constituents. The estimated maximal pore size of similar to 4.7 nm is large enough to allow import of folded PTS2 proteins. PTS2 cargo proteins modulate complex gating, open probability, and subconductance states of the pore. While the PTS1 channel is transiently activated by arriving receptor-cargo complexes, the reconstituted PTS2 channel is constitutively present in an open state. However, the cargo-loaded PTS2 channel is largely impermeable to solutes and ions. Our results demonstrate that import of PTS1 and PTS2 proteins does not converge at the peroxisomal membrane as previously anticipated but is performed by distinct pores."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [FOR1905]"],["dc.identifier.doi","10.1016/j.celrep.2015.11.016"],["dc.identifier.isi","000366534300011"],["dc.identifier.pmid","26673321"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12740"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35126"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","2211-1247"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Distinct Pores for Peroxisomal Import of PTS1 and PTS2 Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5009"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5021"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Reinhold, Robert"],["dc.contributor.author","Krüger, Vivien"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Grunau, Silke D."],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Dudek, Jan"],["dc.date.accessioned","2017-09-07T11:48:21Z"],["dc.date.available","2017-09-07T11:48:21Z"],["dc.date.issued","2012"],["dc.description.abstract","The majority of multispanning inner mitochondrial membrane proteins utilize internal targeting signals, which direct them to the carrier translocase (TIM22 complex), for their import. MPV17 and its Saccharomyces cerevisiae orthologue Sym1 are multispanning inner membrane proteins of unknown function with an amino-terminal presequence that suggests they may be targeted to the mitochondria. Mutations affecting MPV17 are associated with mitochondrial DNA depletion syndrome (MDDS). Reconstitution of purified Sym1 into planar lipid bilayers and electrophysiological measurements have demonstrated that Sym1 forms a membrane pore. To address the biogenesis of Sym1, which oligomerizes in the inner mitochondrial membrane, we studied its import and assembly pathway. Sym1 forms a transport intermediate at the translocase of the outer membrane (TOM) complex. Surprisingly, Sym1 was not transported into mitochondria by an amino-terminal signal, and in contrast to what has been observed in carrier proteins, Sym1 transport and assembly into the inner membrane were independent of small translocase of mitochondrial inner membrane (TIM) and TIM22 complexes. Instead, Sym1 required the presequence of translocase for its biogenesis. Our analyses have revealed a novel transport mechanism for a polytopic membrane protein in which internal signals direct the precursor into the inner membrane via the TIM23 complex, indicating a presequence-independent function of this translocase."],["dc.identifier.doi","10.1128/MCB.00843-12"],["dc.identifier.gro","3142435"],["dc.identifier.isi","000311492200011"],["dc.identifier.pmid","23045398"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8252"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0270-7306"],["dc.title","The Channel-Forming Sym1 Protein Is Transported by the TIM23 Complex in a Presequence-Independent Manner"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","33314"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","33326"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Krüger, Vivien"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Hellmers, Maike"],["dc.contributor.author","Dreker, Christina"],["dc.contributor.author","Preuss, Marc"],["dc.contributor.author","Herrmann, Johannes M."],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Meinecke, Michael"],["dc.date.accessioned","2017-09-07T11:48:24Z"],["dc.date.available","2017-09-07T11:48:24Z"],["dc.date.issued","2012"],["dc.description.abstract","The inner membrane of mitochondria is especially protein-rich. To direct proteins into the inner membrane, translocases mediate transport and membrane insertion of precursor proteins. Although the majority of mitochondrial proteins are imported from the cytoplasm, core subunits of respiratory chain complexes are inserted into the inner membrane from the matrix. Oxa1, a conserved membrane protein, mediates the insertion of mitochondrion-encoded precursors into the inner mitochondrial membrane. The molecular mechanism by which Oxa1 mediates insertion of membrane spans, entailing the translocation of hydrophilic domains across the inner membrane, is still unknown. We investigated if Oxa1 could act as a protein-conducting channel for precursor transport. Using a biophysical approach, we show that Oxa1 can form a pore capable of accommodating a translocating protein segment. After purification and reconstitution, Oxa1 acts as a cation-selective channel that specifically responds to mitochondrial export signals. The aqueous pore formed by Oxa1 displays highly dynamic characteristics with a restriction zone diameter between 0.6 and 2 nm, which would suffice for polypeptide translocation across the membrane. Single channel analyses revealed four discrete channels per active unit, suggesting that the Oxa1 complex forms several cooperative hydrophilic pores in the inner membrane. Hence, Oxa1 behaves as a pore-forming translocase that is regulated in a membrane potential and substrate-dependent manner."],["dc.identifier.doi","10.1074/jbc.M112.387563"],["dc.identifier.gro","3142462"],["dc.identifier.isi","000309602100020"],["dc.identifier.pmid","22829595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8551"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9258"],["dc.title","The Mitochondrial Oxidase Assembly Protein1 (Oxa1) Insertase Forms a Membrane Pore in Lipid Bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1152"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nature Cell Biology"],["dc.bibliographiccitation.lastpage","1159"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Dudek, Jan"],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Lind, Maria"],["dc.contributor.author","Perschil, Inge"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:49:24Z"],["dc.date.available","2017-09-07T11:49:24Z"],["dc.date.issued","2007"],["dc.description.abstract","The mitochondrial inner membrane is the central energy-converting membrane of eukaryotic cells. the electrochemical proton gradient generated by the respiratory chain drives the ATP synthase. to maintain this proton-motive force, the inner membrane forms a tight barrier and strictly controls the translocation of ions(1). However, the major preprotein transport machinery of the inner membrane, termed the presequence translocase, translocates polypeptide chains into or across the membrane(2-9). Different views exist of the molecular mechanism of the translocase, in particular of the coupling with the import motor of the matrix(8,10,11). Wehave reconstituted preprotein transport into the mitochondrial inner membrane by incorporating the purified presequence translocase into cardiolipin-containing liposomes. We show that the motor-free form of the presequence translocase integrates preproteins into the membrane. the reconstituted presequence translocase responds to targeting peptides and mediates voltage-driven preprotein translocation, lateral release and insertion into the lipid phase. thus, the minimal system for preprotein integration into the mitochondrial inner membrane is the presequence translocase, a cardiolipin-rich membrane and a membrane potential."],["dc.identifier.doi","10.1038/ncb1635"],["dc.identifier.gro","3143432"],["dc.identifier.isi","000249882300010"],["dc.identifier.pmid","17828250"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/945"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1465-7392"],["dc.title","Motor-free mitochondrial presequence translocase drives membrane integration of preproteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1523"],["dc.bibliographiccitation.issue","5779"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1526"],["dc.bibliographiccitation.volume","312"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Kovermann, Peter"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Mick, David U."],["dc.contributor.author","Hutu, Dana P."],["dc.contributor.author","Voos, Wolfgang"],["dc.contributor.author","Truscott, Kaye N."],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:52:41Z"],["dc.date.available","2017-09-07T11:52:41Z"],["dc.date.issued","2006"],["dc.description.abstract","Transport of metabolites across the mitochondrial inner membrane is highly selective, thereby maintaining the electrochemical proton gradient that functions as the main driving force for cellular adenosine triphosphate synthesis. Mitochondria import many preproteins via the presequence translocase of the inner membrane. However, the reconstituted Tim23 protein constitutes a pore remaining mainly in its open form, a state that would be deleterious in organello. We found that the intermembrane space domain of Tim50 induced the Tim23 channel to close. Presequences overcame this effect and activated the channel for translocation. Thus, the hydrophilic cis domain of Tim50 maintains the permeability barrier of mitochondria by closing the translocation pore in a presequence-regulated manner."],["dc.identifier.doi","10.1126/science.1127628"],["dc.identifier.gro","3143677"],["dc.identifier.isi","000238124100048"],["dc.identifier.pmid","16763150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1217"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0036-8075"],["dc.title","Tim50 maintains the permeability barrier of the mitochondrial inner membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","821"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","827"],["dc.bibliographiccitation.volume","1863"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Bartsch, Philipp"],["dc.contributor.author","Wagner, Richard"],["dc.date.accessioned","2018-11-07T10:15:17Z"],["dc.date.available","2018-11-07T10:15:17Z"],["dc.date.issued","2016"],["dc.description.abstract","Peroxisomal protein import is essentially different to the translocation of proteins into other organelles. The molecular mechanisms by which completely folded or even oligomerized proteins cross the peroxisomal membrane remain to be disclosed. The identification of a water-filled pore that is mainly constituted by Pex5 and Pex14 led to the assumption that proteins are translocated through a large, probably transient, protein-conducting channel. Here, we will review the work that led to the identification of this translocation pore. In addition, we will discuss the main biophysical features of the pore and compare it with other protein-translocation channels. This article is part of a Special Issue entitled: Peroxisomes edited by Ralf Erdmann. (C) 2015 Published by Elsevier B.V."],["dc.description.sponsorship","DFG [FOR 1905]"],["dc.identifier.doi","10.1016/j.bbamcr.2015.10.013"],["dc.identifier.isi","000374071600005"],["dc.identifier.pmid","26497277"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40782"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0006-3002"],["dc.relation.issn","0167-4889"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Peroxisomal protein import pores"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Beck, Sabrina"],["dc.contributor.author","Martinez, Malayko Montilla"],["dc.contributor.author","Krueger, Vivien"],["dc.contributor.author","Meinecke, Michael"],["dc.contributor.author","Schliebs, Wolfgang"],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2018-11-07T09:20:12Z"],["dc.date.available","2018-11-07T09:20:12Z"],["dc.date.issued","2013"],["dc.format.extent","55"],["dc.identifier.isi","000327927400060"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28820"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-Blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.relation.orgunit","Institut für Zellbiochemie"],["dc.title","Identification of the peroxisomal translocon for PTS2-proteins"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]