Abstract
Mitochondrial translation synthesizes key subunits of the respiratory complexes. In Schizosaccharomyces pombe, strains lacking Mrf1, the mitochondrial stop codon recognition factor, are viable, suggesting that other factors can play a role in translation termination. S. pombe contains four predicted peptidyl tRNA hydrolases, two of which (Pth3 and Pth4), have a GGQ motif that is conserved in class I release factors. We show that high dosage of Pth4 can compensate for the absence of Mrf1 and loss of Pth4 exacerbates the lack of Mrf1. Also Pth4 is a component of the mitochondrial ribosome, suggesting that it could help recycling stalled ribosomes.
Highlights
Mitochondria are essential organelles that are found in almost all eukaryotic cells, it is generally accepted that they arose from the endosymbiosis of α proteobacteria, closely related to Rickettsia, into a eukaryotic ancestor (Emelyanov, 2003)
In an attempt to further our understanding of the termination of mitochondrial translation in S. pombe, we decided to investigate the role of the mitochondrial Pth proteins and their possible interaction with the mitochondrial release factor, Mrf1
Crystallographic studies of the eubacterial release factors, RF1 and RF2, in complex with the 70S ribosome show that the glutamine residue in a conserved GGQ motif is positioned in such a way that it can contribute directly to the hydrolysis of the peptidyl-transfer RNAs (tRNA) bond (Laurberg et al, 2008 and Weixlbaumer et al, 2008)
Summary
Mitochondria are essential organelles that are found in almost all eukaryotic cells, it is generally accepted that they arose from the endosymbiosis of α proteobacteria, closely related to Rickettsia, into a eukaryotic ancestor (Emelyanov, 2003). Their main function is to provide the cell with energy in the form of ATP, via oxidative phosphorylation (OXPHOS), a process completed by multi-protein complexes located in the inner mitochondrial membrane.
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