%0 Journal Article %1 cristoderoMitochondrialTranslationFactors2013 %A Cristodero, Marina %A Mani, Jan %A Oeljeklaus, Silke %A Aeberhard, Lukas %A Hashimi, Hassan %A Ramrath, David J. F. %A Lukes, Julius %A Warscheid, Bettina %A Schneider, André %C England %D 2013 %J Molecular microbiology %K & *Amino Acid Alignment,to_read,Trypanosoma Complex Data,Mutation,Oxidative Elongation Expression Factor Factors/genetics/metabolism,Peptide Factors/genetics/metabolism,Proteomics,Protozoan G/genetics/metabolism,Peptide IV/metabolism,Gene Interference,Sequence Line,Electron Motifs,Amino Phosphorylation,Peptide Proteins/*chemistry/genetics/physiology,Ribosomes/*metabolism,RNA Proteins/*chemistry/physiology,Molecular Regulation,Mitochondria/genetics/*metabolism,Mitochondrial Sequence Sequence,Cell Termination Transport Tu/*chemistry/genetics/physiology,Peptide brucei brucei/genetics/growth development/*metabolism %N 4 %P 744--755 %R 10.1111/mmi.12397 %T Mitochondrial Translation Factors of Trypanosoma Brucei: Elongation Factor-Tu Has a Unique Subdomain That Is Essential for Its Function. %V 90 %X Mitochondrial translation in the parasitic protozoan Trypanosoma brucei relies on imported eukaryotic-type tRNAs as well as on bacterial-type ribosomes that have the shortest known rRNAs. Here we have identified the mitochondrial translation elongation factors EF-Tu, EF-Ts, EF-G1 and release factor RF1 of trypanosomatids and show that their ablation impairs growth and oxidative phosphorylation. In vivo labelling experiments and a SILAC-based analysis of the global proteomic changes induced by EF-Tu RNAi directly link EF-Tu to mitochondrial translation. Moreover, EF-Tu RNAi reveals downregulation of many nuclear encoded subunits of cytochrome oxidase as well as of components of the bc1-complex, whereas most cytosolic ribosomal proteins were upregulated. Interestingly, T.\,brucei\>EF-Tu has a 30-amino-acid-long, highly charged subdomain, which is unique to trypanosomatids. A combination of RNAi and complementation experiments shows that this subdomain is essential for EF-Tu function, but that it can be replaced by a similar sequence found in eukaryotic EF-1a, the cytosolic counterpart of EF-Tu. A recent cryo-electron microscopy study revealed that trypanosomatid mitochondrial ribosomes have a unique intersubunit space that likely harbours the EF-Tu binding site. These findings suggest that the trypanosomatid-specific EF-Tu subdomain serves as an adaption for binding to these unusual mitochondrial ribosomes.

@article{cristoderoMitochondrialTranslationFactors2013, abstract = {Mitochondrial translation in the parasitic protozoan Trypanosoma brucei relies on imported eukaryotic-type tRNAs as well as on bacterial-type ribosomes that have the shortest known rRNAs. Here we have identified the mitochondrial translation elongation factors EF-Tu, EF-Ts, EF-G1 and release factor RF1 of trypanosomatids and show that their ablation impairs growth and oxidative phosphorylation. In vivo labelling experiments and a SILAC-based analysis of the global proteomic changes induced by EF-Tu RNAi directly link EF-Tu to mitochondrial translation. Moreover, EF-Tu RNAi reveals downregulation of many nuclear encoded subunits of cytochrome oxidase as well as of components of the bc1-complex, whereas most cytosolic ribosomal proteins were upregulated. Interestingly, T.\,brucei\>EF-Tu has a 30-amino-acid-long, highly charged subdomain, which is unique to trypanosomatids. A combination of RNAi and complementation experiments shows that this subdomain is essential for EF-Tu function, but that it can be replaced by a similar sequence found in eukaryotic EF-1a, the cytosolic counterpart of EF-Tu. A recent cryo-electron microscopy study revealed that trypanosomatid mitochondrial ribosomes have a unique intersubunit space that likely harbours the EF-Tu binding site. These findings suggest that the trypanosomatid-specific EF-Tu subdomain serves as an adaption for binding to these unusual mitochondrial ribosomes.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {England}, author = {Cristodero, Marina and Mani, Jan and Oeljeklaus, Silke and Aeberhard, Lukas and Hashimi, Hassan and Ramrath, David J. F. and Luke{\v s}, Julius and Warscheid, Bettina and Schneider, Andr{\'e}}, biburl = {https://www.bibsonomy.org/bibtex/23c56f864ccad0e5379b298484fdfbf1f/warscheidlab}, copyright = {{\copyright} 2013 John Wiley \& Sons Ltd.}, doi = {10.1111/mmi.12397}, interhash = {53047b225e9eb0fa6221a3120dd369bc}, intrahash = {3c56f864ccad0e5379b298484fdfbf1f}, issn = {1365-2958 0950-382X}, journal = {Molecular microbiology}, keywords = {& *Amino Acid Alignment,to_read,Trypanosoma Complex Data,Mutation,Oxidative Elongation Expression Factor Factors/genetics/metabolism,Peptide Factors/genetics/metabolism,Proteomics,Protozoan G/genetics/metabolism,Peptide IV/metabolism,Gene Interference,Sequence Line,Electron Motifs,Amino Phosphorylation,Peptide Proteins/*chemistry/genetics/physiology,Ribosomes/*metabolism,RNA Proteins/*chemistry/physiology,Molecular Regulation,Mitochondria/genetics/*metabolism,Mitochondrial Sequence Sequence,Cell Termination Transport Tu/*chemistry/genetics/physiology,Peptide brucei brucei/genetics/growth development/*metabolism}, langid = {english}, month = nov, number = 4, pages = {744--755}, pmid = {24033548}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Mitochondrial Translation Factors of {{Trypanosoma}} Brucei: Elongation Factor-{{Tu}} Has a Unique Subdomain That Is Essential for Its Function.}, volume = 90, year = 2013 }