| 2010 |
The RNA recognition motif (RRM) of yeast eIF3g/Tif35 is required for resumption of scanning by post-termination 40S ribosomes after uORF1 in GCN4 mRNA, and a triple-Ala substitution of conserved RRM residues (g/tif35-KLF) impairs reinitiation at GCN4, reduces processivity of scanning through stable mRNA secondary structures, and eIF3g specifically interacts with ribosomal proteins Rps3 and Rps20 near the mRNA entry channel. |
In vivo mutagenesis, growth assays, GCN4-lacZ reporter assays, ribosome sedimentation, and co-immunoprecipitation with ribosomal proteins in S. cerevisiae |
Molecular and cellular biology |
High |
20679478
|
| 2013 |
eIF3g contains a SLIP1-binding motif (SBM) that allows direct physical interaction with the MIF4G-like protein SLIP1, which bridges SLBP with translation initiation factors; the interaction was confirmed by pull-down assay and a 3.25 Å crystal structure of SLIP1 bound to an SBM-containing peptide from a related protein (DBP5). |
Crystal structure determination (2.5 Å and 3.25 Å), GST pull-down assay |
Nucleic acids research |
High |
23804756
|
| 2023 |
eIF3g directly interacts with eIF4A3 (a core EJC component), and this eIF4A3–eIF3g interaction acts as a molecular linker between the EJC and the eIF3 complex to facilitate internal ribosomal entry and translation of circular RNAs; disruption of this interaction abolishes eIF4A3-driven internal translation from in vitro-synthesized circRNA. |
Co-immunoprecipitation, in vitro circRNA translation assay, polysomal fractionation, transcriptome-wide ribosome association analysis |
Nucleic acids research |
High |
37811880
|
| 2006 |
Apoptosis-inducing factor (AIF) directly interacts with the N-terminus of eIF3g (via AIF's C-terminal region), inhibits protein synthesis in vitro, and this inhibition is competitively blocked by excess eIF3g; AIF overexpression also activates caspase-7 leading to cleavage of eIF3g. |
Yeast two-hybrid screen, GST pull-down assay, co-immunoprecipitation, confocal microscopy, in vitro TNT transcription-translation inhibition assay, cell-based overexpression |
FEBS letters |
Medium |
17094969
|
| 2000 |
Cytoskeletal protein 4.1R directly binds eIF3g (eIF3-p44) via its C-terminal domain (residues 525–622) interacting with eIF3g residues 54–321; depletion of eIF3g from reticulocyte lysates (by antibody or GST/4.1R fusion) severely impairs cell-free protein synthesis, demonstrating that eIF3g is essential for translation. |
Yeast two-hybrid screen, in vitro binding assay, co-immunoprecipitation, immunodepletion of cell-free translation system |
Blood |
Medium |
10887144
|
| 2023 |
In vitro reconstitution of SARS-CoV-2 Nsp1-induced mRNA cleavage demonstrated that the RRM domain of eIF3g is essential for cleavage: a minimal system of 40S subunits plus eIF3g's RRM domain was sufficient for CrPV IRES mRNA cleavage; mutational analysis identified a surface above the mRNA-binding channel on eIF3g's RRM domain with residues critical for cleavage across all tested mRNA types. |
In vitro reconstitution, mutational analysis, minimal-component cleavage assay with 40S subunits and isolated eIF3g RRM domain |
Genes & development |
High |
37821106
|
| 2013 |
During apoptosis induced by cisplatin, caspase activity cleaves eIF3g at SLRD(220)G; the resulting N-terminal fragment translocates to the nucleus, activates caspase-3, and exhibits strong DNase activity. |
Caspase cleavage site mapping by mutagenesis, subcellular fractionation/nuclear translocation assay, DNase activity assay in T24 cells |
FEBS letters |
Medium |
24080033
|
| 2010 |
PELO (Pelota) directly interacts with eIF3g; the interaction domain was mapped to PELO residues 268–385; protein complexes formed by PELO and eIF3g localize to actin cytoskeletal filaments as shown by bimolecular fluorescence complementation. |
Yeast two-hybrid screen, GST pull-down assay, co-immunoprecipitation, bimolecular fluorescence complementation (BiFC) |
BMC cell biology |
Medium |
20406461
|
| 2016 |
eIF3g is present in the nucleus of breast cancer cells and interacts there with hnRNP U/SAF-A, ZNF823, and β-actin, as identified by nuclear co-immunoprecipitation, mass spectrometry, cross-linking, GST pull-down, and confocal co-localization. |
Nuclear co-immunoprecipitation, mass spectrometry, GST pull-down, confocal microscopy |
Molecular medicine reports |
Low |
26935993
|
| 2026 |
eIF3g (and its binding partner eIF3i) mediates transcript-specific translational induction under mild heat stress in yeast by directly binding GUCG-centered motifs (GUCG boxes) located in the 5'-terminal coding regions of heat-stress-responsive mRNAs; SELEX identified the GUCG motif as the preferred eIF3g-binding sequence, biolayer interferometry confirmed direct binding, and disruption of the motif impairs both eIF3g binding and translational induction in reporter assays. |
SELEX, ribosome profiling, reporter assays, mutational analysis, biolayer interferometry |
Nucleic acids research |
High |
41556339
|
| 2025 |
Loss-of-function mutations in eIF3g (and eIF3i) in S. cerevisiae cause a similar reduction in translation of GFP reporters regardless of 5' UTR length (short vs. long unstructured UTRs), consistent with a role in ribosome recruitment or start-codon recognition rather than rate-limiting helicase-driven scanning; mutations in eIF3g did not specifically sensitize translation to 5' UTR secondary structures compared to helicase mutants. |
GFP reporter assays with variable-length 5' UTRs in S. cerevisiae, loss-of-function mutations, comparison with helicase mutants (eIF4A, Ded1) |
bioRxivpreprint |
Low |
bio_10.1101_2024.12.30.630811
|