0379100 - MBÚ 2013 RIV GB eng J - Článek v odborném periodiku
Kouba, Tomáš - Rutkai, Edit - Karásková, Martina - Valášek, Leoš Shivaya
The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes.
Nucleic Acids Research. Roč. 40, č. 6 (2012), s. 2683-2699. ISSN 0305-1048. E-ISSN 1362-4962
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: START CODON SELECTION * INITIATION-FACTOR 3 * 40S RIBOSOMAL-SUBUNIT
Kód oboru RIV: CE - Biochemie
Impakt faktor: 8.278, rok: 2012 ; AIS: 3.271, rok: 2012
DOI: https://doi.org/10.1093/nar/gkr1083

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
Trvalý link: http://hdl.handle.net/11104/0210370