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Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78500

Pfeffer,  Stefan
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77965

Förster,  Friedrich
Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Pfeffer, S., Woellhaf, M. W., Herrmann, J. M., & Förster, F. (2015). Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography. Nature Communications, 6: 6019. doi:10.1038/ncomms7019.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0025-73C3-C
Zusammenfassung
Whereas the structure and function of cytosolic ribosomes have been studied in great detail, we know surprisingly little about the structural basis of mitochondrial protein synthesis. Here we used cryoelectron tomography and subtomogram analysis to visualize mitoribosomes in isolated yeast mitochondria, avoiding perturbations during ribosomal purification. Most mitoribosomes reside in immediate proximity to the inner mitochondrial membrane, in line with their specialization in the synthesis of hydrophobic membrane proteins. The subtomogram average of membrane-associated mitoribosomes reveals two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein Mba1. On the basis of our data, we further hypothesize that Mba1 is not just a passive mitoribosome receptor on the inner membrane, but that it spatially aligns mitoribosomes with the membrane insertion machinery. This study reveals detailed insights into the supramolecular organization of the mitochondrial translation machinery and its association with the inner membrane in translation-competent mitochondria.