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- W2080852048 endingPage "17458" @default.
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- W2080852048 abstract "Numerous transport processes occur between the two mitochondrial (mt) membranes due to the diverse functions and metabolic processes of the mt organelle. The metabolite and ion transport through the mt outer membrane (OM) is widely assumed to be mediated by the porin pore, whereas in the mt inner membrane (IM) specific carriers are responsible for transport processes. Here, we provide evidence by means of Blue Native (BN)-PAGE analysis, co-immunoprecipitation, and tandem affinity purification that the two mt OM proteins Om14p and Om45p associate with the porin pore. Porin molecules seem to assemble independently to build the core unit. A subpopulation of these core units interacts with Om14p and Om45p. With preparative tandem affinity purification followed by MS analysis, we could identify interaction partners of this OM complex, which are mainly localized within the mt IM and function as carriers for diverse molecules. We propose a model for the role of the two OM proteins in addressing the porin pore to bind to specific channels in the mt IM to facilitate transport of metabolites. Numerous transport processes occur between the two mitochondrial (mt) membranes due to the diverse functions and metabolic processes of the mt organelle. The metabolite and ion transport through the mt outer membrane (OM) is widely assumed to be mediated by the porin pore, whereas in the mt inner membrane (IM) specific carriers are responsible for transport processes. Here, we provide evidence by means of Blue Native (BN)-PAGE analysis, co-immunoprecipitation, and tandem affinity purification that the two mt OM proteins Om14p and Om45p associate with the porin pore. Porin molecules seem to assemble independently to build the core unit. A subpopulation of these core units interacts with Om14p and Om45p. With preparative tandem affinity purification followed by MS analysis, we could identify interaction partners of this OM complex, which are mainly localized within the mt IM and function as carriers for diverse molecules. We propose a model for the role of the two OM proteins in addressing the porin pore to bind to specific channels in the mt IM to facilitate transport of metabolites." @default.
- W2080852048 created "2016-06-24" @default.
- W2080852048 creator A5001250870 @default.
- W2080852048 creator A5006904583 @default.
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- W2080852048 creator A5055624846 @default.
- W2080852048 creator A5060598459 @default.
- W2080852048 creator A5085180375 @default.
- W2080852048 date "2012-05-01" @default.
- W2080852048 modified "2023-10-17" @default.
- W2080852048 title "Saccharomyces cerevisiae Porin Pore Forms Complexes with Mitochondrial Outer Membrane Proteins Om14p and Om45p" @default.
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- W2080852048 doi "https://doi.org/10.1074/jbc.m111.328328" @default.
- W2080852048 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3366824" @default.
- W2080852048 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22461620" @default.
- W2080852048 hasPublicationYear "2012" @default.
- W2080852048 type Work @default.