2011
DOI: 10.1093/nar/gkr1083
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The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes

Abstract: 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 tru… Show more

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Cited by 70 publications
(107 citation statements)
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References 62 publications
(132 reference statements)
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“…DNA association with the 26S proteasome could be required for its role in transcription (65), but no experimental evidence for recruitment of the 26S proteasomes to DNA or RNA exists to date. Interestingly, for subunit eIF3c of the lid paralog eIF3, RNA interaction of its PCI domain has been shown recently (66).…”
Section: Aaa-atpase Hexamermentioning
confidence: 99%
“…DNA association with the 26S proteasome could be required for its role in transcription (65), but no experimental evidence for recruitment of the 26S proteasomes to DNA or RNA exists to date. Interestingly, for subunit eIF3c of the lid paralog eIF3, RNA interaction of its PCI domain has been shown recently (66).…”
Section: Aaa-atpase Hexamermentioning
confidence: 99%
“…Indeed, loss of RACK1 impairs the recruitment of the ternary complex, suggesting that RACK1 could regulate the initiation phase of translation. 58 Intriguingly, eIF3 is released upon 80S assembly, while RACK1 remains associated to translating ribosomes, namely polysomes. This observation suggests that RACK1 could modulate not only translation initiation but also subsequent steps of protein synthesis (e.g., elongation).…”
Section: Monographsmentioning
confidence: 99%
“…6B, cpc2⌬). Although most previous studies have not taken this point into account, it has been recently reported that in S. cerevisiae, the ribosome assembly defect (half-mer polysomes) observed in the cells deleted within the asc1-containing genomic region is ascribed to the loss of a small nucleolar RNA carried in an intron of the ASC1 gene (35), underlining the importance of testing whether defective snoU24b is responsible for phenotypes observed in cpc2⌬ cells. To that end, we generated cells (cpc2_W43*) harboring a nonsense mutation in place of Trp43 in Cpc2 (Fig.…”
Section: Fission Yeast Cpc2 Facilitates Gcn2-mediated Stress Responsementioning
confidence: 99%
“…The absence of S. cerevisiae ASC1 increased the Gcn4-mediated transcription of amino acid biosynthesis genes under nonstarvation conditions (34), presumably by the destabilization of translation initiation complexes on ribosomes (35). ASC1 deletion suppressed the growth defect of gcn2⌬ cells under limiting amino acid conditions, indicating that Asc1 negatively regulates the GAAC response in S. cerevisiae.…”
mentioning
confidence: 98%