Maintaining mitochondrial ribosome function: The role of ribosome rescue and recycling factors

2021 | journal article; overview. A publication with affiliation to the University of Göttingen.

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​Maintaining mitochondrial ribosome function: The role of ribosome rescue and recycling factors​
Nadler, F.; Lavdovskaia, E. & Richter-Dennerlein, R. ​ (2021) 
RNA Biology, pp. 1​-15​.​ DOI: https://doi.org/10.1080/15476286.2021.2015561 

Details

Authors
Nadler, Franziska; Lavdovskaia, Elena; Richter-Dennerlein, Ricarda 
Abstract
The universally conserved process of protein biosynthesis is crucial for maintaining cellular homoeostasis and in eukaryotes, mitochondrial translation is essential for aerobic energy production. Mitochondrial ribosomes (mitoribosomes) are highly specialized to synthesize 13 core subunits of the oxidative phosphorylation (OXPHOS) complexes. Although the mitochondrial translation machinery traces its origin from a bacterial ancestor, it has acquired substantial differences within this endosymbiotic environment. The cycle of mitoribosome function proceeds through the conserved canonical steps of initiation, elongation, termination and mitoribosome recycling. However, when mitoribosomes operate in the context of limited translation factors or on aberrant mRNAs, they can become stalled and activation of rescue mechanisms is required. This review summarizes recent advances in the understanding of protein biosynthesis in mitochondria, focusing especially on the mechanistic and physiological details of translation termination, and mitoribosome recycling and rescue.
Issue Date
2021
Journal
RNA Biology 
Project
EXC 2067: Multiscale Bioimaging 
SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente 
SFB 1190 | P23: Strukturelle Grundlagen des Proteintransports über die äußere mitochondriale Membran humaner Mitochondrien 
Working Group
RG Richter-Dennerlein (Mitoribosome Assembly) 
RG K. Bohnsack (RNA Metabolism) 
RG Hillen (Structure and Function of Molecular Machines) 
RG Urlaub (Bioanalytische Massenspektrometrie) 
External URL
https://mbexc.uni-goettingen.de/literature/publications/377
https://sfb1190.med.uni-goettingen.de/production/literature/publications/224
ISSN
1547-6286
eISSN
1555-8584
Language
English

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