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

RNA Biol. 2022;19(1):117-131. doi: 10.1080/15476286.2021.2015561. Epub 2021 Dec 31.

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.

Keywords: Mitochondrial ribosome (mitoribosome); mitoribosome recycling; mitoribosome rescue; mitoribosome-associated quality control (mtRQC); translation termination.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacteria / genetics
  • Bacteria / metabolism
  • Eukaryota / physiology
  • Humans
  • Mitochondria / physiology*
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism
  • Mitochondrial Ribosomes / metabolism*
  • Protein Biosynthesis*

Substances

  • Mitochondrial Proteins

Grants and funding

Funded by the German Research Foundation (Deutsche Forschungsgemeinschaft, DFG): Emmy Noether grant [RI 2715/1-1 to R.R.-D.], SFB860 [A14 to R.R.-D.] and under Germany’s Excellence Strategy - EXC 2067/1- 390729940 [to R.R.-D.].