L
Leoš Shivaya Valášek
Researcher at Academy of Sciences of the Czech Republic
Publications - 82
Citations - 4052
Leoš Shivaya Valášek is an academic researcher from Academy of Sciences of the Czech Republic. The author has contributed to research in topics: Eukaryotic translation & Initiation factor. The author has an hindex of 37, co-authored 73 publications receiving 3563 citations. Previous affiliations of Leoš Shivaya Valášek include Charles University in Prague & University of Vienna.
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Journal ArticleDOI
Robust heat shock induces eIF2α-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae
Tomas Grousl,Pavel Ivanov,Ivana Frydlova,Pavla Vasicova,Filip Janda,Jana Vojtova,Kateřina Malínská,Ivana Malcova,Lenka Martinec Nováková,Dana Janošková,Leoš Shivaya Valášek,Jiří Hašek +11 more
TL;DR: It is concluded that under specific stress conditions, such as robust heat shock, yeast SGs do contain eIF3 and 40S ribosomes and utilize alternative routes for their assembly.
Journal ArticleDOI
Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection.
TL;DR: The NIP1-NTD is required for efficient assembly of preinitiation complexes and also regulates the selection of AUG start codons in vivo, indicating that MFC formation stimulates TC recruitment to 40S ribosomes.
Journal ArticleDOI
The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
Leoš Shivaya Valášek,Amy A. Mathew,Byung-Sik Shin,Klaus H. Nielsen,Béla Szamecz,Alan G. Hinnebusch +5 more
TL;DR: EIF3 binds to the solvent side of the 40S subunit in a way that provides access to the interface side for the two eIF3 segments (NIP1-NTD and TIF32-CTD) that interact with eIF1, eIF5, and the eIF2/GTP/Met-tRNA(i)(Met) ternary complex.
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Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo.
TL;DR: Two independent eIF2–eIF3 contacts have additive effects on translation in vivo, providing the first in vivo evidence that association with eIF3 promotes binding of eIFs 1, 2, 5 and Met‐tRNAiMet to 40S ribosomes.
Journal ArticleDOI
Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation.
Katsura Asano,Anath Shalev,Lon Phan,Klaus H. Nielsen,Jason Clayton,Leoš Shivaya Valášek,Thomas F. Donahue,Alan G. Hinnebusch +7 more
TL;DR: It is proposed that eIF5‐CTD stimulates binding of Met‐tRNAiMet and mRNA to 40S subunits through interactions with eIF2, eIF3 and eIF4G; however, its most important function is to anchor eif5 to other components of the 48S complex in a manner required to couple GTP hydrolysis to AUG recognition during the scanning phase of initiation.