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Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts
A. Bochler, JB. Querido, T. Prilepskaja, H. Soufari, A. Simonetti, ML. Del Cistia, L. Kuhn, AR. Ribeiro, LS. Valášek, Y. Hashem
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
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Odkazy
PubMed
33357443
DOI
10.1016/j.celrep.2020.108534
Knihovny.cz E-zdroje
- MeSH
- molekulární modely MeSH
- proteosyntéza imunologie MeSH
- savci MeSH
- Trypanosomatina patogenita MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Canonical mRNA translation in eukaryotes begins with the formation of the 43S pre-initiation complex (PIC). Its assembly requires binding of initiator Met-tRNAiMet and several eukaryotic initiation factors (eIFs) to the small ribosomal subunit (40S). Compared to their mammalian hosts, trypanosomatids present significant structural differences in their 40S, suggesting substantial variability in translation initiation. Here, we determine the structure of the 43S PIC from Trypanosoma cruzi, the parasite causing Chagas disease. Our structure shows numerous specific features, such as the variant eIF3 structure and its unique interactions with the large rRNA expansion segments (ESs) 9S, 7S, and 6S, and the association of a kinetoplastid-specific DDX60-like helicase. It also reveals the 40S-binding site of the eIF5 C-terminal domain and structures of key terminal tails of several conserved eIFs underlying their activities within the PIC. Our results are corroborated by glutathione S-transferase (GST) pull-down assays in both human and T. cruzi and mass spectrometry data.
Charles University Faculty of Science Albertov 6 128 00 Prague 2 Czech Republic
INSERM U1212 Institut Européen de Chimie et Biologie Université de Bordeaux Pessac 33607 France
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