Evidence map›Paper›PMID 22123745›Full record

ArticleNucleic acids research2012

The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes.

Tomáš Kouba, Edit Rutkai, Martina Karásková, Leoš Shivaya Valášek

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 79 citations in OpenAlex.

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  7. A dynamic compositional equilibrium governs mRNA recognition by eIF3.bioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Tomáš KoubaLaboratory of Regulation of Gene Expression, Institute of Microbiology AVCR, v.v.i., Prague, the Czech Republic.
Edit Rutkai
Martina Karásková
Leoš Shivaya Valášek
Czech Academy of Sciences, Institute of Microbiology · CZ

Funding

Wellcome Trust 076456Wellcome Trust 076456/Z/05/ZWellcome Trust 090812Wellcome Trust 090812/B/09/Z
6 · The paper itself

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 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. The extreme C-terminus directly interacts with blades 1-3 of the small ribosomal protein RACK1/ASC1, which is a part of the 40S head, and, consistently, deletion of the ASC1 coding region likewise affects eIF3 association with ribosomes. The PCI domain per se shows strong but unspecific binding to RNA, for the first time implicating this typical protein-protein binding domain in mediating protein-RNA interactions also. Importantly, as our clustered mutations severely reduce RNA binding, we conclude that the c/NIP1 C-terminal region forms an important intermolecular bridge between eIF3 and the 40S head region by contacting RACK1/ASC1 and most probably 18S rRNA.

Indexed as

Peptide Chain Initiation, TranslationalAdaptor Proteins, Signal TransducingAmino Acid SequenceBasic-Leucine Zipper Transcription FactorsEukaryotic Initiation Factor-3Gene DeletionGTP-Binding ProteinsModels, MolecularMolecular Sequence DataProtein Interaction Domains and MotifsProtein SubunitsRibosome Subunits, Small, EukaryoticRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingASC1 protein, S cerevisiaeBasic-Leucine Zipper Transcription FactorsEukaryotic Initiation Factor-3GCN4 protein, S cerevisiaeGTP-Binding ProteinsNIP1 protein, S cerevisiaeProtein SubunitsRNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID22123745
PMCPMC3315329
OpenAlexW2134860105

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.