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The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes
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SYSNO ASEP 0379100 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes Author(s) Kouba, Tomáš (MBU-M)
Rutkai, Edit (MBU-M)
Karásková, Martina (MBU-M)
Valášek, Leoš Shivaya (MBU-M) RID, ORCIDSource Title Nucleic Acids Research. - : Oxford University Press - ISSN 0305-1048
Roč. 40, č. 6 (2012), s. 2683-2699Number of pages 17 s. Language eng - English Country GB - United Kingdom Keywords START CODON SELECTION ; INITIATION-FACTOR 3 ; 40S RIBOSOMAL-SUBUNIT Subject RIV CE - Biochemistry CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000302312400033 DOI https://doi.org/10.1093/nar/gkr1083 Annotation Several subunits of the multifunctional eukaryotic translation initiation factor 3 (eIF3) contain well-defined domains. Among them is the conserved bipartite PCI domain, typically serving as the principal scaffold for multisubunit 26S proteasome lid, CSN and eIF3 complexes, which constitutes most of the C-terminal region of the c/NIP1 subunit. Interestingly, the c/NIP1-PCI domain is exceptional in that its deletion, despite being lethal, does not affect eIF3 integrity. Here, we show that a short C-terminal truncation and two clustered mutations directly disturbing the PCI domain produce lethal or slow growth phenotypes and significantly reduce amounts of 40S-bound eIF3 and eIF5 in vivo Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2013
Počet záznamů: 1