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Mitochondrial translation factors of Trypanosoma brucei: elongation factor-Tu has a unique subdomain that is essential for its function
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SYSNO ASEP 0420949 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Mitochondrial translation factors of Trypanosoma brucei: elongation factor-Tu has a unique subdomain that is essential for its function Tvůrce(i) Cristodero, M. (CH)
Mani, J. (CH)
Oeljeklaus, S. (DE)
Aeberhard, L. (CH)
Hashimi, Hassan (BC-A) RID, ORCID
Ramrath, D.J.F. (CH)
Lukeš, Julius (BC-A) RID, ORCID
Warscheid, B. (DE)
Schneider, A. (CH)Zdroj.dok. Molecular Microbiology - ISSN 0950-382X
Roč. 90, č. 4 (2013), s. 744-755Poč.str. 12 s. Forma vydání Tištěná - P Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova mitochondrial translation ; Trypanosoma brucei ; EF-Tu Vědní obor RIV EB - Genetika a molekulární biologie CEP GAP305/12/2261 GA ČR - Grantová agentura ČR Institucionální podpora BC-A - RVO:60077344 UT WOS 000330108000006 EID SCOPUS 84887407096 DOI 10.1111/mmi.12397 Anotace 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. Pracoviště Biologické centrum (od r. 2006) Kontakt Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Rok sběru 2014
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