ArticlePloS one2012
Small ribosomal protein RPS0 stimulates translation initiation by mediating 40S-binding of eIF3 via its direct contact with the eIF3a/TIF32 subunit.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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.
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Who cites it
29 citing papers in PubMed, 35 citations in OpenAlex.
- Ribosome Heterogeneity in Plants: The Causes of This Phenomenon and Its Implications on Gene Expression.Plants (Basel, Switzerland) · 2026Review
- Ribosome heterogeneity and specialization in musculoskeletal physiology and pathology.JBMR plus · 2026Article
- eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation.Biochemical Society transactions · 2025Review
- Article
- Pre-emptive Quality Control of a Misfolded Membrane Protein by Ribosome-Driven Effects.Current biology : CB · 2020Article
- uS3/Rps3 controls fidelity of translation termination and programmed stop codon readthrough in co-operation with eIF3.Nucleic acids research · 2019Article
- Fission Yeast Asc1 Stabilizes the Interaction between Eukaryotic Initiation Factor 3a and Rps0A/uS2 for Protein Synthesis.Molecular and cellular biology · 2019Article
- Binding of eIF3 in complex with eIF5 and eIF1 to the 40S ribosomal subunit is accompanied by dramatic structural changes.Nucleic acids research · 2019Article
- Does functional specialization of ribosomes really exist?RNA (New York, N.Y.) · 2019Review
- Please do not recycle! Translation reinitiation in microbes and higher eukaryotes.FEMS microbiology reviews · 2018Review
- Does eIF3 promote reinitiation after translation of short upstream ORFs also in mammalian cells?RNA biology · 2017Review
- Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Nucleic acids research · 2017Article
- In vivo evidence that eIF3 stays bound to ribosomes elongating and terminating on short upstream ORFs to promote reinitiation.Nucleic acids research · 2017Article
- Article
- The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits.Nucleic acids research · 2016Article
- Review
- In-depth analysis of cis-determinants that either promote or inhibit reinitiation on GCN4 mRNA after translation of its four short uORFs.RNA (New York, N.Y.) · 2016Article
- Article
- Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex.Nature structural & molecular biology · 2015Article
- eIF3a is over-expressed in urinary bladder cancer and influences its phenotype independent of translation initiation.Cellular oncology (Dordrecht, Netherlands) · 2014Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The ribosome translates information encoded by mRNAs into proteins in all living cells. In eukaryotes, its small subunit together with a number of eukaryotic initiation factors (eIFs) is responsible for locating the mRNA's translational start to properly decode the genetic message that it carries. This multistep process requires timely and spatially coordinated placement of eIFs on the ribosomal surface. In our long-standing pursuit to map the 40S-binding site of one of the functionally most complex eIFs, yeast multisubunit eIF3, we identified several interactions that placed its major body to the head, beak and shoulder regions of the solvent-exposed side of the 40S subunit. Among them is the interaction between the N-terminal domain (NTD) of the a/TIF32 subunit of eIF3 and the small ribosomal protein RPS0A, residing near the mRNA exit channel. Previously, we demonstrated that the N-terminal truncation of 200 residues in tif32-Δ8 significantly reduced association of eIF3 and other eIFs with 40S ribosomes in vivo and severely impaired translation reinitiation that eIF3 ensures. Here we show that not the first but the next 200 residues of a/TIF32 specifically interact with RPS0A via its extreme C-terminal tail (CTT). Detailed analysis of the RPS0A conditional depletion mutant revealed a marked drop in the polysome to monosome ratio suggesting that the initiation rates of cells grown under non-permissive conditions were significantly impaired. Indeed, amounts of eIF3 and other eIFs associated with 40S subunits in the pre-initiation complexes in the RPS0A-depleted cells were found reduced; consistently, to the similar extent as in the tif32-Δ8 cells. Similar but less pronounced effects were also observed with the viable CTT-less mutant of RPS0A. Together we conclude that the interaction between the flexible RPS0A-CTT and the residues 200-400 of the a/TIF32-NTD significantly stimulates attachment of eIF3 and its associated eIFs to small ribosomal subunits in vivo.
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