Abstract
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, mtRF1a, 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?
Highlights
Maintaining the efficiency and accuracy of protein synthesis is one of the most important aspects of cell survival
Despite similarities between YaeJ and immature colon carcinoma transcript-1 (ICT1) and their common divergence from standard release factors (RFs), we cannot assume a similar mechanism using the bacterial paradigm, as the integration of ICT1 into the mitoribosome excludes a similar mechanism of action
Since bacteria have more than one rescue pathway, it seems probable that mitochondria will too
Summary
Protein synthesis is central to life and maintaining a highly accurate and efficient mechanism is essential. Mammalian mitochondria synthesize just thirteen highly hydrophobic polypeptides. Many highly intricate processes have been documented in the cytosol of numerous species, but how does organellar protein synthesis resolve this stalling issue? These proteins are all integral components of the machinery that couples oxidative phosphorylation. It is essential that stalled mitochondrial ribosomes can be efficiently recycled. Could the other members be involved in the process of recycling stalled mitochondrial ribosomes?
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