Lookup NU author(s): Maria Wesolowska,
Professor Robert Lightowlers,
Professor Zofia Chrzanowska-Lightowlers
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Protein synthesis is central to life and maintaining a highly accurate and efficient mechanism is essential. What happens when a translating ribosome stalls on a messenger RNA? Many highly intricate processes have been documented in the cytosol of numerous species, but how does organellar protein synthesis resolve this stalling issue? Mammalian mitochondria synthesize just thirteen highly hydrophobic polypeptides. These proteins are all integral components of the machinery that couples oxidative phosphorylation. Consequently, it is essential that stalled mitochondrial ribosomes can be efficiently recycled. To date, there is no evidence to support any particular molecular mechanism to resolve this problem. However, here we discuss the observation that there are four predicted members of the mitochondrial translation release factor family and that only one member, mtRF1 a, is necessary to terminate the translation of all thirteen open reading frames in the mitochondrion. Could the other members be involved in the process of recycling stalled mitochondrial ribosomes?
Author(s): Wesolowska MT, Richter-Dennerlein R, Lightowlers RN, Chrzanowska-Lightowlers ZMA
Publication type: Article
Publication status: Published
Journal: Frontiers in Microbiology
Online publication date: 18/07/2014
Acceptance date: 03/07/2014
ISSN (electronic): 1664-302X
Publisher: Frontiers Research Foundation
Altmetrics provided by Altmetric