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  Structure of the Human Mitochondrial Ribosome Studied In Situ by Cryoelectron Tomography

Englmeier, R., Pfeffer, S., & Förster, F. (2017). Structure of the Human Mitochondrial Ribosome Studied In Situ by Cryoelectron Tomography. Structure, 25(10), 1574-1581. doi:10.1016/j.str.2017.07.011.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-0C39-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-0C3A-1
Genre: Journal Article

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 Creators:
Englmeier, Robert1, Author
Pfeffer, Stefan2, Author              
Förster, Friedrich2, Author              
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: CRYO-EM; SUBTOMOGRAM ANALYSIS; ELECTRON TOMOGRAPHY; INSERTION MACHINERY; PHASE PLATE; TOOLBOX; MBA1; VISUALIZATION; ORGANIZATION; COMPLEXESBiochemistry & Molecular Biology; Biophysics; Cell Biology;
 Abstract: Mitochondria maintain their own genome and its corresponding protein synthesis machine, the mitochondrial ribosome (mitoribosome). Mitoribosomes primarily synthesize highly hydrophobic proteins of the inner mitochondrial membrane. Recent studies revealed the complete structure of the isolated mammalian mitoribosome, but its mode of membrane association remained hypothetical. In this study, we used cryoelectron tomography to visualize human mitoribosomes in isolated mitochondria. The subtomogram average of themembrane-associated human mitoribosome reveals a single major contact site with the inner membrane, mediated by the mitochondria-specific protein mL45. A second rRNA-mediated contact site that is present in yeast is absent in humans, resulting in a more variable association of the human mitoribosome with the inner membrane. Despite extensive structural differences of mammalian and fungal mitoribosomal structure, the principal organization of peptide exit tunnel and the mL45 homolog remains invariant, presumably to align the mitoribosome with the membrane-embedded insertion machinery.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000412114800012
DOI: 10.1016/j.str.2017.07.011
 Degree: -

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Project name : FO 716/4-1 and the German Research Council GRK1721
Grant ID : -
Funding program : -
Funding organization : Deutsche Forschungsgemeinschaft

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Title: Structure
  Other : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Cell Press
Pages: - Volume / Issue: 25 (10) Sequence Number: - Start / End Page: 1574 - 1581 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1