Translation termination in human mitochondria – substrate specificity of mitochondrial release factors

Abstract: Mitochondria are the essential players in eukaryotic ATP production by oxidative phosphorylation, which relies on the maintenance and accurate expression of the mitochondrial genome. Even though the basic principles of translation are conserved due to the descendance from a bacterial ancestor, some deviations regarding translation factors as well as mRNA characteristics and the applied genetic code are present in human mitochondria. Together, these features are certain challenges during translation the mitochondrion has to handle. Here, we discuss the current knowledge regarding mitochondrial translation focusing on the termination process and the associated quality control mechanisms. We describe how mtRF1a resembles bacterial RF1 mechanistically and summarize in vitro and recent in vivo data leading to the conclusion of mtRF1a being the major mitochondrial release factor. On the other hand, we discuss the ongoing debate about the function of the second codon-dependent mitochondrial release factor mtRF1 regarding its role as a specialized termination factor. Finally, we link defects in mitochondrial translation termination to the activation of mitochondrial rescue mechanisms highlighting the importance of ribosome-associated quality control for sufficient respiratory function and therefore for human health.

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch

References and Relationships

• Bibliographic citation: Translation termination in human mitochondria – substrate specificity of mitochondrial release factors ; volume:404 ; number:8-9 ; year:2023 ; pages:769-779 ; extent:011 ; Biological chemistry ; 404, Heft 8-9 (2023), 769-779 (gesamt 011)

Contributors, Places and Time

• Creator: Nadler, Franziska ; Richter-Dennerlein, Ricarda

Further information

• DOI: 10.1515/hsz-2023-0127
• URN: urn:nbn:de:101:1-2023090714210025606157
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 14.08.2025, 10:58 AM CEST