Neumann, Piotr D.

[["dc.bibliographiccitation.artnumber","5715"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2021-10-01T09:57:33Z"],["dc.date.available","2021-10-01T09:57:33Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Nuclear-encoded mitochondrial proteins destined for the matrix have to be transported across two membranes. The TOM and TIM23 complexes facilitate the transport of precursor proteins with N-terminal targeting signals into the matrix. During transport, precursors are recognized by the TIM23 complex in the inner membrane for handover from the TOM complex. However, we have little knowledge on the organization of the TOM-TIM23 transition zone and on how precursor transfer between the translocases occurs. Here, we have designed a precursor protein that is stalled during matrix transport in a TOM-TIM23-spanning manner and enables purification of the translocation intermediate. Combining chemical cross-linking with mass spectrometric analyses and structural modeling allows us to map the molecular environment of the intermembrane space interface of TOM and TIM23 as well as the import motor interactions with amino acid resolution. Our analyses provide a framework for understanding presequence handover and translocation during matrix protein transport."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-021-26016-1"],["dc.identifier.pii","26016"],["dc.identifier.pmid","34588454"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89863"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/348"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/157"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["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 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","Mapping protein interactions in the active TOM-TIM23 supercomplex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1161"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","1178"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Parfentev, Iwan"],["dc.contributor.author","Pflanz, Ralf"],["dc.contributor.author","Homberg, Bettina"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2021-04-14T08:24:20Z"],["dc.date.available","2021-04-14T08:24:20Z"],["dc.date.issued","2020"],["dc.description.abstract","Protein cross-linking and the analysis of cross-linked peptides by mass spectrometry is currently receiving much attention. Not only is this approach applied to isolated complexes to provide information about spatial arrangements of proteins, but it is also increasingly applied to entire cells and their organelles. As in quantitative proteomics, the application of isotopic labeling further makes it possible to monitor quantitative changes in the protein-protein interactions between different states of a system. Here, we cross-linked mitochondria from Saccharomyces cerevisiae grown on either glycerol- or glucose-containing medium to monitor protein-protein interactions under non-fermentative and fermentative conditions. We investigated qualitatively the protein-protein interactions of the 400 most abundant proteins applying stringent data-filtering criteria, i.e. a minimum of two cross-linked peptide spectrum matches and a cut-off in the spectrum scoring of the used search engine. The cross-linker BS3 proved to be equally suited for connecting proteins in all compartments of mitochondria when compared with its water-insoluble but membrane-permeable derivative DSS. We also applied quantitative cross-linking to mitochondria of both the growth conditions using stable-isotope labeled BS3. Significant differences of cross-linked proteins under glycerol and glucose conditions were detected, however, mainly because of the different copy numbers of these proteins in mitochondria under both the conditions. Results obtained from the glycerol condition indicate that the internal NADH:ubiquinone oxidoreductase Ndi1 is part of an electron transport chain supercomplex. We have also detected several hitherto uncharacterized proteins and identified their interaction partners. Among those, Min8 was found to be associated with cytochrome c oxidase. BN-PAGE analyses of min8Δ mitochondria suggest that Min8 promotes the incorporation of Cox12 into cytochrome c oxidase."],["dc.identifier.doi","10.1074/mcp.RA120.002028"],["dc.identifier.pmid","33451406"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81250"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/188"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/134"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.issn","1535-9476"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","A Cross-linking Mass Spectrometry Approach Defines Protein Interactions in Yeast Mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","157"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","168"],["dc.bibliographiccitation.volume","595"],["dc.contributor.author","Valpadashi, Anusha"],["dc.contributor.author","Callegari, Sylvie"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2021-04-14T08:32:24Z"],["dc.date.available","2021-04-14T08:32:24Z"],["dc.date.issued","2020"],["dc.description.abstract","The majority of mitochondrial proteins are nuclear encoded and imported into mitochondria as precursor proteins via dedicated translocases. The translocase of the inner membrane 22 (TIM22) is a multisubunit molecular machine specialized for the translocation of hydrophobic, multi‐transmembrane‐spanning proteins with internal targeting signals into the inner mitochondrial membrane. Here, we undertook a crosslinking‐mass spectrometry (XL‐MS) approach to determine the molecular arrangement of subunits of the human TIM22 complex. Crosslinking of the isolated TIM22 complex using the BS3 crosslinker resulted in the broad generation of crosslinks across the majority of TIM22 components, including the small TIM chaperone complex. The crosslinking data uncovered several unexpected features, opening new avenues for a deeper investigation into the steps required for TIM22‐mediated translocation in humans."],["dc.description.abstract","image"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship","Max Planck Society http://dx.doi.org/10.13039/501100004189"],["dc.identifier.doi","10.1002/1873-3468.13978"],["dc.identifier.pmid","33125709"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83911"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/86"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/129"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.eissn","1873-3468"],["dc.relation.issn","0014-5793"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made."],["dc.title","Defining the architecture of the human TIM22 complex by chemical crosslinking"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]