DC Field | Value | Language |
dc.contributor.author | Harsman, Anke | |
dc.contributor.author | Niemann, Moritz | |
dc.contributor.author | Pusnik, Mascha | |
dc.contributor.author | Schmidt, Oliver | |
dc.contributor.author | Burmann, Bjoern M. | |
dc.contributor.author | Hiller, Sebastian | |
dc.contributor.author | Meisinger, Chris | |
dc.contributor.author | Schneider, Andre | |
dc.contributor.author | Wagner, Richard | |
dc.date.accessioned | 2021-12-23T16:20:08Z | - |
dc.date.available | 2021-12-23T16:20:08Z | - |
dc.date.issued | 2012 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/13338 | - |
dc.description.abstract | Mitochondria are of bacterial ancestry and have to import most of their proteins from the cytosol. This process is mediated by Tom40, an essential protein that forms the protein-translocating pore in the outer mitochondrial membrane. Tom40 is conserved in virtually all eukaryotes, but its evolutionary origin is unclear because bacterial orthologues have not been identified so far. Recently, it was shown that the parasitic protozoon Trypanosoma brucei lacks a conventional Tom40 and instead employs the archaic translocase of the outer mitochondrial membrane (ATOM), a protein that shows similarities to both eukaryotic Tom40 and bacterial protein translocases of the Omp85 family. Here we present electrophysiological single channel data showing that ATOM forms a hydrophilic pore of large conductance and high open probability. Moreover, ATOM channels exhibit a preference for the passage of cationic molecules consistent with the idea that it may translocate unfolded proteins targeted by positively charged N-terminal presequences. This is further supported by the fact that the addition of a presequence peptide induces transient pore closure. An in-depth comparison of these single channel properties with those of other protein translocases reveals that ATOM closely resembles bacterial-type protein export channels rather than eukaryotic Tom40. Our results support the idea that ATOM represents an evolutionary intermediate between a bacterial Omp85-like protein export machinery and the conventional Tom40 that is found in mitochondria of other eukaryotes. | |
dc.description.sponsorship | Deutsche Forschungsgemeinschaft (DFG)German Research Foundation (DFG) [WA681/2-1, FOR967, ME1921]; Swiss National Science Foundation (SNSF)Swiss National Science Foundation (SNSF) [31003A_13855, PP00P3_128419]; European Research Council FP7 ContractEuropean Research Council (ERC) [MOMP 281764]; This work was supported by Deutsche Forschungsgemeinschaft (DFG) Grant WA681/2-1 (to R. W.) and DFG Grant FOR967 (to R. W.), by DFG Grant ME1921 (to C. M.), by Swiss National Science Foundation (SNSF) Grant 31003A_13855 (to A. S.) as well as by Swiss National Science Foundation grant PP00P3_128419 and European Research Council FP7 Contract MOMP 281764 (to S. H.). | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | BROWNIAN DYNAMICS | |
dc.subject | CONDUCTING PORE | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | FUNCTIONAL DOMAINS | |
dc.subject | IMPORT | |
dc.subject | OMP85 FAMILY | |
dc.subject | PREPROTEIN TRANSLOCASE | |
dc.subject | TOM40 FORMS | |
dc.subject | TRANSPORTER | |
dc.subject | TRYPANOSOMA-BRUCEI | |
dc.title | Bacterial Origin of a Mitochondrial Outer Membrane Protein Translocase NEW PERSPECTIVES FROM COMPARATIVE SINGLE CHANNEL ELECTROPHYSIOLOGY | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.M112.392118 | |
dc.identifier.isi | ISI:000308791300054 | |
dc.description.volume | 287 | |
dc.description.issue | 37 | |
dc.description.startpage | 31437 | |
dc.description.endpage | 31445 | |
dc.contributor.orcid | 0000-0002-3135-7964 | |
dc.contributor.orcid | 0000-0002-6709-4684 | |
dc.contributor.orcid | 0000-0002-8326-3548 | |
dc.contributor.orcid | 0000-0002-3135-7964 | |
dc.contributor.orcid | 0000-0002-7921-4663 | |
dc.contributor.researcherid | M-8913-2015 | |
dc.contributor.researcherid | B-3573-2008 | |
dc.contributor.researcherid | J-1110-2014 | |
dc.contributor.researcherid | AAI-7760-2021 | |
dc.contributor.researcherid | AAR-7399-2020 | |
dc.identifier.eissn | 1083351X | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | hybrid, Green Published | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | WaRi703 | - |