{"gene":"EIF3G","run_date":"2026-06-09T23:54:42","timeline":{"discoveries":[{"year":2010,"finding":"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.","method":"In vivo mutagenesis, growth assays, GCN4-lacZ reporter assays, ribosome sedimentation, and co-immunoprecipitation with ribosomal proteins in S. cerevisiae","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (mutagenesis, reporter assays, sedimentation, co-IP), functionally characterized in vivo with specific mechanistic readouts","pmids":["20679478"],"is_preprint":false},{"year":2013,"finding":"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).","method":"Crystal structure determination (2.5 Å and 3.25 Å), GST pull-down assay","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure plus pull-down biochemistry in a single rigorous study; SBM identification confirmed experimentally","pmids":["23804756"],"is_preprint":false},{"year":2023,"finding":"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.","method":"Co-immunoprecipitation, in vitro circRNA translation assay, polysomal fractionation, transcriptome-wide ribosome association analysis","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP plus functional reconstitution with circRNA translation and polysomal fractionation in a single study","pmids":["37811880"],"is_preprint":false},{"year":2006,"finding":"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.","method":"Yeast two-hybrid screen, GST pull-down assay, co-immunoprecipitation, confocal microscopy, in vitro TNT transcription-translation inhibition assay, cell-based overexpression","journal":"FEBS letters","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (Y2H, GST pull-down, Co-IP, in vitro translation assay) from a single lab","pmids":["17094969"],"is_preprint":false},{"year":2000,"finding":"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.","method":"Yeast two-hybrid screen, in vitro binding assay, co-immunoprecipitation, immunodepletion of cell-free translation system","journal":"Blood","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (Y2H, in vitro binding, co-IP, functional depletion assay) from a single lab","pmids":["10887144"],"is_preprint":false},{"year":2023,"finding":"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.","method":"In vitro reconstitution, mutational analysis, minimal-component cleavage assay with 40S subunits and isolated eIF3g RRM domain","journal":"Genes & development","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro reconstitution with minimal components plus mutagenesis identifying specific RRM surface residues; confirmed in peer-reviewed publication (preprint also in corpus)","pmids":["37821106"],"is_preprint":false},{"year":2013,"finding":"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.","method":"Caspase cleavage site mapping by mutagenesis, subcellular fractionation/nuclear translocation assay, DNase activity assay in T24 cells","journal":"FEBS letters","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — specific cleavage site identified by mutagenesis, nuclear translocation confirmed, DNase activity directly measured; single lab","pmids":["24080033"],"is_preprint":false},{"year":2010,"finding":"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.","method":"Yeast two-hybrid screen, GST pull-down assay, co-immunoprecipitation, bimolecular fluorescence complementation (BiFC)","journal":"BMC cell biology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — multiple methods (Y2H, GST pull-down, co-IP, BiFC) converge on interaction and localization; single lab","pmids":["20406461"],"is_preprint":false},{"year":2016,"finding":"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.","method":"Nuclear co-immunoprecipitation, mass spectrometry, GST pull-down, confocal microscopy","journal":"Molecular medicine reports","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, primarily descriptive interactome in nucleus; no functional consequence of interactions established","pmids":["26935993"],"is_preprint":false},{"year":2026,"finding":"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.","method":"SELEX, ribosome profiling, reporter assays, mutational analysis, biolayer interferometry","journal":"Nucleic acids research","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in vitro SELEX plus biolayer interferometry for direct binding, corroborated by ribosome profiling and mutagenesis in vivo; single lab but multiple orthogonal methods","pmids":["41556339"],"is_preprint":false},{"year":2025,"finding":"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.","method":"GFP reporter assays with variable-length 5' UTRs in S. cerevisiae, loss-of-function mutations, comparison with helicase mutants (eIF4A, Ded1)","journal":"bioRxiv","confidence":"Low","confidence_rationale":"Tier 3 / Weak — preprint, single-lab reporter assays; mechanistic conclusion is indirect (epistasis-style comparison without biochemical reconstitution)","pmids":["bio_10.1101_2024.12.30.630811"],"is_preprint":true}],"current_model":"EIF3G is a core eIF3 subunit whose RRM domain mediates sequence-specific RNA binding (preferring GUCG motifs in 5'-coding regions for stress-responsive translation), stimulates linear mRNA scanning and reinitiation (in yeast), interacts physically with ribosomal proteins Rps3/Rps20 near the mRNA entry channel, forms a direct bridge to eIF4A3 to facilitate internal ribosome entry on circRNAs, binds SLIP1 for histone mRNA translation, is cleaved by caspases during apoptosis releasing a nuclear DNase fragment, and its RRM domain is co-opted by SARS-CoV-2 Nsp1 to endonucleolytically cleave host mRNAs on 40S subunits."},"narrative":{"mechanistic_narrative":"EIF3G is a core subunit of the eIF3 translation initiation complex that is essential for cap-dependent protein synthesis and contributes to transcript-selective and non-canonical translation through its RNA recognition motif (RRM) [PMID:20679478, PMID:10887144]. Within the 40S preinitiation complex it positions near the mRNA entry channel, interacting with ribosomal proteins Rps3 and Rps20, and its RRM is required for post-termination scanning and reinitiation, promoting processive scanning through structured 5' regions in yeast [PMID:20679478]. The RRM confers sequence-specific RNA binding, with a preference for GUCG-centered motifs in 5'-terminal coding regions that drive transcript-specific translational induction of heat-stress-responsive mRNAs in concert with eIF3i [PMID:41556339]. EIF3G also enables specialized and non-canonical translation modes: it binds SLIP1 through a defined SLIP1-binding motif, linking histone mRNA machinery to initiation factors [PMID:23804756], and forms a direct bridge to the EJC component eIF4A3 to license internal ribosome entry and translation of circular RNAs [PMID:37811880]. Its RRM is co-opted by SARS-CoV-2 Nsp1, where a surface above the mRNA-binding channel is sufficient, together with 40S subunits, to endonucleolytically cleave host mRNAs [PMID:37821106]. During apoptosis, caspase cleavage at SLRD220G releases an N-terminal EIF3G fragment that translocates to the nucleus, activates caspase-3, and exhibits DNase activity, coupling translational regulation to cell death [PMID:24080033].","teleology":[{"year":2000,"claim":"Established that EIF3G is functionally required for translation, not merely a passive complex subunit, by showing its depletion abolishes cell-free protein synthesis.","evidence":"Yeast two-hybrid, in vitro binding, co-IP, and immunodepletion of reticulocyte translation system identifying cytoskeletal protein 4.1R as a direct partner","pmids":["10887144"],"confidence":"Medium","gaps":["Functional consequence of the 4.1R interaction for translation not defined","Single-lab interaction mapping without structural validation"]},{"year":2006,"claim":"Linked EIF3G to apoptotic translational shutdown by showing AIF binds its N-terminus, inhibits translation, and triggers caspase-7-dependent cleavage.","evidence":"Yeast two-hybrid, GST pull-down, co-IP, confocal microscopy, and in vitro translation inhibition assay","pmids":["17094969"],"confidence":"Medium","gaps":["Physiological context of AIF–eIF3G regulation in vivo not established","Fate and function of cleaved eIF3G not addressed here"]},{"year":2010,"claim":"Defined the RRM's role in scanning and reinitiation and placed eIF3g near the mRNA entry channel through contacts with Rps3 and Rps20, providing a structural rationale for its function in start-codon traversal.","evidence":"In vivo mutagenesis, GCN4-lacZ reporters, ribosome sedimentation, and co-IP in S. cerevisiae","pmids":["20679478"],"confidence":"High","gaps":["Direct RNA target of the RRM during scanning not yet identified","Generalizability beyond GCN4 reinitiation unresolved at this stage"]},{"year":2010,"claim":"Connected EIF3G to mRNA surveillance and cytoskeletal localization by identifying PELO as a direct partner localizing to actin filaments.","evidence":"Yeast two-hybrid, GST pull-down, co-IP, and BiFC with domain mapping","pmids":["20406461"],"confidence":"Medium","gaps":["Functional output of the PELO–eIF3G complex not determined","Significance of actin-filament localization unclear"]},{"year":2013,"claim":"Identified a discrete SLIP1-binding motif in eIF3g, providing a molecular route to couple histone mRNA machinery to translation initiation.","evidence":"Crystal structures of SLIP1 with an SBM peptide plus GST pull-down","pmids":["23804756"],"confidence":"High","gaps":["Direct structure of the eIF3g SBM bound to SLIP1 not solved (peptide from related protein used)","Functional impact on histone mRNA translation not measured here"]},{"year":2013,"claim":"Revealed a moonlighting pro-apoptotic activity: caspase cleavage at SLRD220G generates a nuclear N-terminal fragment with DNase activity that activates caspase-3.","evidence":"Cleavage-site mapping by mutagenesis, nuclear translocation assays, and DNase activity assays in T24 cells","pmids":["24080033"],"confidence":"Medium","gaps":["Mechanism of DNase activity by an initiation factor fragment unexplained","Single-lab finding without reciprocal confirmation"]},{"year":2016,"claim":"Reported a nuclear interactome of eIF3g in breast cancer cells, raising the possibility of nuclear roles beyond cytoplasmic translation.","evidence":"Nuclear co-IP, mass spectrometry, cross-linking, GST pull-down, and confocal co-localization","pmids":["26935993"],"confidence":"Low","gaps":["Descriptive interactome with no functional consequence established","Single-lab, low-confidence observations not independently validated"]},{"year":2023,"claim":"Showed EIF3G bridges the EJC to eIF3, enabling internal ribosome entry and translation of circular RNAs.","evidence":"Reciprocal co-IP, in vitro circRNA translation, polysomal fractionation, and transcriptome-wide ribosome association","pmids":["37811880"],"confidence":"High","gaps":["Structural basis of the eIF4A3–eIF3g bridge not resolved","Scope of circRNAs dependent on this interaction not fully mapped"]},{"year":2023,"claim":"Defined the EIF3G RRM as the catalytic determinant co-opted by SARS-CoV-2 Nsp1 for host mRNA cleavage, with a minimal 40S+RRM system sufficient for cleavage.","evidence":"In vitro reconstitution with minimal components and mutational mapping of a surface above the mRNA-binding channel","pmids":["37821106"],"confidence":"High","gaps":["Whether the RRM surface is intrinsically nucleolytic or requires Nsp1 catalysis unresolved","Endogenous (non-viral) function of this RRM surface not addressed"]},{"year":2026,"claim":"Established that eIF3g directly reads GUCG-centered motifs in 5'-coding regions to drive transcript-specific translational induction under heat stress, defining a sequence-specific mRNA selection function.","evidence":"SELEX, biolayer interferometry, ribosome profiling, reporter assays, and mutagenesis in yeast","pmids":["41556339"],"confidence":"High","gaps":["Whether GUCG-motif recognition operates in mammalian cells not tested","Mechanism coupling motif binding to enhanced initiation not fully defined"]},{"year":null,"claim":"How the same RRM domain reconciles sequence-specific mRNA selection, scanning/reinitiation, circRNA IRES function, and viral-coopted endonucleolytic cleavage within the intact 40S–eIF3 complex remains unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No unified structural model of the eIF3g RRM engaging different RNA classes","Relationship between yeast scanning role and mammalian motif-recognition role unclear","Endogenous physiological substrates of the RRM cleavage surface unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[0,5,9]},{"term_id":"GO:0045182","term_label":"translation regulator activity","supporting_discovery_ids":[0,4,2,9]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[1,2]},{"term_id":"GO:0140098","term_label":"catalytic activity, acting on RNA","supporting_discovery_ids":[5]},{"term_id":"GO:0140097","term_label":"catalytic activity, acting on DNA","supporting_discovery_ids":[6]}],"localization":[{"term_id":"GO:0005840","term_label":"ribosome","supporting_discovery_ids":[0]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[4]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[6]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[7]}],"pathway":[{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[0,4,2]},{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[2,9]},{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[6,3]}],"complexes":["eIF3"],"partners":["RPS3","RPS20","SLIP1","EIF4A3","AIF","PELO","EIF3I"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O75821","full_name":"Eukaryotic translation initiation factor 3 subunit G","aliases":["Eukaryotic translation initiation factor 3 RNA-binding subunit","eIF-3 RNA-binding subunit","Eukaryotic translation initiation factor 3 subunit 4","eIF-3-delta","eIF3 p42","eIF3 p44"],"length_aa":320,"mass_kda":35.6,"function":"RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426)","subcellular_location":"Cytoplasm; Nucleus; Cytoplasm, perinuclear region","url":"https://www.uniprot.org/uniprotkb/O75821/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/EIF3G","classification":"Common Essential","n_dependent_lines":1207,"n_total_lines":1208,"dependency_fraction":0.9991721854304636},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000130811","cell_line_id":"CID001756","localizations":[{"compartment":"cytoplasmic","grade":3}],"interactors":[{"gene":"EIF3B","stoichiometry":10.0},{"gene":"RPS26;RPS26P11","stoichiometry":10.0},{"gene":"RPS7","stoichiometry":10.0},{"gene":"RPS8","stoichiometry":10.0},{"gene":"RPS16","stoichiometry":10.0},{"gene":"RPS23","stoichiometry":10.0},{"gene":"RPS18","stoichiometry":10.0},{"gene":"EIF3E","stoichiometry":10.0},{"gene":"EIF3A","stoichiometry":10.0},{"gene":"EIF3L","stoichiometry":10.0}],"url":"https://opencell.sf.czbiohub.org/target/CID001756","total_profiled":1310},"omim":[{"mim_id":"609596","title":"EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT K; EIF3K","url":"https://www.omim.org/entry/609596"},{"mim_id":"603913","title":"EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT G; EIF3G","url":"https://www.omim.org/entry/603913"},{"mim_id":"603910","title":"EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT J; EIF3J","url":"https://www.omim.org/entry/603910"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Cytosol","reliability":"Enhanced"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/EIF3G"},"hgnc":{"alias_symbol":["eIF3-delta","eIF3-p44"],"prev_symbol":["EIF3S4"]},"alphafold":{"accession":"O75821","domains":[{"cath_id":"-","chopping":"16-31_48-125","consensus_level":"medium","plddt":74.5055,"start":16,"end":125},{"cath_id":"3.30.70.330","chopping":"237-313","consensus_level":"high","plddt":90.4455,"start":237,"end":313}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O75821","model_url":"https://alphafold.ebi.ac.uk/files/AF-O75821-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O75821-F1-predicted_aligned_error_v6.png","plddt_mean":70.19},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=EIF3G","jax_strain_url":"https://www.jax.org/strain/search?query=EIF3G"},"sequence":{"accession":"O75821","fasta_url":"https://rest.uniprot.org/uniprotkb/O75821.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O75821/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O75821"}},"corpus_meta":[{"pmid":"20679478","id":"PMC_20679478","title":"The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning.","date":"2010","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/20679478","citation_count":93,"is_preprint":false},{"pmid":"23804756","id":"PMC_23804756","title":"Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.","date":"2013","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/23804756","citation_count":32,"is_preprint":false},{"pmid":"37811880","id":"PMC_37811880","title":"An interaction between eIF4A3 and eIF3g drives the internal initiation of translation.","date":"2023","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/37811880","citation_count":31,"is_preprint":false},{"pmid":"17094969","id":"PMC_17094969","title":"Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g).","date":"2006","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/17094969","citation_count":28,"is_preprint":false},{"pmid":"10887144","id":"PMC_10887144","title":"Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translation apparatus.","date":"2000","source":"Blood","url":"https://pubmed.ncbi.nlm.nih.gov/10887144","citation_count":28,"is_preprint":false},{"pmid":"20406461","id":"PMC_20406461","title":"Pelota interacts with HAX1, EIF3G and SRPX and the resulting protein complexes are associated with the actin cytoskeleton.","date":"2010","source":"BMC cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/20406461","citation_count":24,"is_preprint":false},{"pmid":"25669430","id":"PMC_25669430","title":"EIF3G is associated with narcolepsy across ethnicities.","date":"2015","source":"European journal of 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cerevisiae.","date":"2026","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/41556339","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.12.30.630811","title":"40S ribosomal subunits scan mRNA for the start codon by one-dimensional diffusion","date":"2025-01-01","source":"bioRxiv","url":"https://doi.org/10.1101/2024.12.30.630811","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10177,"output_tokens":2958,"usd":0.03745,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10292,"output_tokens":3689,"usd":0.071843,"stage2_stop_reason":"end_turn"},"total_usd":0.109293,"stage1_batch_id":"msgbatch_01AsR7g8dGTEiEw9U83bJeWn","stage2_batch_id":"msgbatch_01YV5ZyxtFNUZEjxRcpd9jzb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"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.\",\n      \"method\": \"In vivo mutagenesis, growth assays, GCN4-lacZ reporter assays, ribosome sedimentation, and co-immunoprecipitation with ribosomal proteins in S. cerevisiae\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (mutagenesis, reporter assays, sedimentation, co-IP), functionally characterized in vivo with specific mechanistic readouts\",\n      \"pmids\": [\"20679478\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"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).\",\n      \"method\": \"Crystal structure determination (2.5 Å and 3.25 Å), GST pull-down assay\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure plus pull-down biochemistry in a single rigorous study; SBM identification confirmed experimentally\",\n      \"pmids\": [\"23804756\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"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.\",\n      \"method\": \"Co-immunoprecipitation, in vitro circRNA translation assay, polysomal fractionation, transcriptome-wide ribosome association analysis\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus functional reconstitution with circRNA translation and polysomal fractionation in a single study\",\n      \"pmids\": [\"37811880\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"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.\",\n      \"method\": \"Yeast two-hybrid screen, GST pull-down assay, co-immunoprecipitation, confocal microscopy, in vitro TNT transcription-translation inhibition assay, cell-based overexpression\",\n      \"journal\": \"FEBS letters\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (Y2H, GST pull-down, Co-IP, in vitro translation assay) from a single lab\",\n      \"pmids\": [\"17094969\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2000,\n      \"finding\": \"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.\",\n      \"method\": \"Yeast two-hybrid screen, in vitro binding assay, co-immunoprecipitation, immunodepletion of cell-free translation system\",\n      \"journal\": \"Blood\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (Y2H, in vitro binding, co-IP, functional depletion assay) from a single lab\",\n      \"pmids\": [\"10887144\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"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.\",\n      \"method\": \"In vitro reconstitution, mutational analysis, minimal-component cleavage assay with 40S subunits and isolated eIF3g RRM domain\",\n      \"journal\": \"Genes & development\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro reconstitution with minimal components plus mutagenesis identifying specific RRM surface residues; confirmed in peer-reviewed publication (preprint also in corpus)\",\n      \"pmids\": [\"37821106\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"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.\",\n      \"method\": \"Caspase cleavage site mapping by mutagenesis, subcellular fractionation/nuclear translocation assay, DNase activity assay in T24 cells\",\n      \"journal\": \"FEBS letters\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — specific cleavage site identified by mutagenesis, nuclear translocation confirmed, DNase activity directly measured; single lab\",\n      \"pmids\": [\"24080033\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"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.\",\n      \"method\": \"Yeast two-hybrid screen, GST pull-down assay, co-immunoprecipitation, bimolecular fluorescence complementation (BiFC)\",\n      \"journal\": \"BMC cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — multiple methods (Y2H, GST pull-down, co-IP, BiFC) converge on interaction and localization; single lab\",\n      \"pmids\": [\"20406461\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"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.\",\n      \"method\": \"Nuclear co-immunoprecipitation, mass spectrometry, GST pull-down, confocal microscopy\",\n      \"journal\": \"Molecular medicine reports\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, primarily descriptive interactome in nucleus; no functional consequence of interactions established\",\n      \"pmids\": [\"26935993\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"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.\",\n      \"method\": \"SELEX, ribosome profiling, reporter assays, mutational analysis, biolayer interferometry\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vitro SELEX plus biolayer interferometry for direct binding, corroborated by ribosome profiling and mutagenesis in vivo; single lab but multiple orthogonal methods\",\n      \"pmids\": [\"41556339\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"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.\",\n      \"method\": \"GFP reporter assays with variable-length 5' UTRs in S. cerevisiae, loss-of-function mutations, comparison with helicase mutants (eIF4A, Ded1)\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — preprint, single-lab reporter assays; mechanistic conclusion is indirect (epistasis-style comparison without biochemical reconstitution)\",\n      \"pmids\": [\"bio_10.1101_2024.12.30.630811\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"EIF3G is a core eIF3 subunit whose RRM domain mediates sequence-specific RNA binding (preferring GUCG motifs in 5'-coding regions for stress-responsive translation), stimulates linear mRNA scanning and reinitiation (in yeast), interacts physically with ribosomal proteins Rps3/Rps20 near the mRNA entry channel, forms a direct bridge to eIF4A3 to facilitate internal ribosome entry on circRNAs, binds SLIP1 for histone mRNA translation, is cleaved by caspases during apoptosis releasing a nuclear DNase fragment, and its RRM domain is co-opted by SARS-CoV-2 Nsp1 to endonucleolytically cleave host mRNAs on 40S subunits.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"EIF3G is a core subunit of the eIF3 translation initiation complex that is essential for cap-dependent protein synthesis and contributes to transcript-selective and non-canonical translation through its RNA recognition motif (RRM) [#0, #4]. Within the 40S preinitiation complex it positions near the mRNA entry channel, interacting with ribosomal proteins Rps3 and Rps20, and its RRM is required for post-termination scanning and reinitiation, promoting processive scanning through structured 5' regions in yeast [#0]. The RRM confers sequence-specific RNA binding, with a preference for GUCG-centered motifs in 5'-terminal coding regions that drive transcript-specific translational induction of heat-stress-responsive mRNAs in concert with eIF3i [#9]. EIF3G also enables specialized and non-canonical translation modes: it binds SLIP1 through a defined SLIP1-binding motif, linking histone mRNA machinery to initiation factors [#1], and forms a direct bridge to the EJC component eIF4A3 to license internal ribosome entry and translation of circular RNAs [#2]. Its RRM is co-opted by SARS-CoV-2 Nsp1, where a surface above the mRNA-binding channel is sufficient, together with 40S subunits, to endonucleolytically cleave host mRNAs [#5]. During apoptosis, caspase cleavage at SLRD220G releases an N-terminal EIF3G fragment that translocates to the nucleus, activates caspase-3, and exhibits DNase activity, coupling translational regulation to cell death [#6].\",\n  \"teleology\": [\n    {\n      \"year\": 2000,\n      \"claim\": \"Established that EIF3G is functionally required for translation, not merely a passive complex subunit, by showing its depletion abolishes cell-free protein synthesis.\",\n      \"evidence\": \"Yeast two-hybrid, in vitro binding, co-IP, and immunodepletion of reticulocyte translation system identifying cytoskeletal protein 4.1R as a direct partner\",\n      \"pmids\": [\"10887144\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Functional consequence of the 4.1R interaction for translation not defined\", \"Single-lab interaction mapping without structural validation\"]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"Linked EIF3G to apoptotic translational shutdown by showing AIF binds its N-terminus, inhibits translation, and triggers caspase-7-dependent cleavage.\",\n      \"evidence\": \"Yeast two-hybrid, GST pull-down, co-IP, confocal microscopy, and in vitro translation inhibition assay\",\n      \"pmids\": [\"17094969\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Physiological context of AIF–eIF3G regulation in vivo not established\", \"Fate and function of cleaved eIF3G not addressed here\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Defined the RRM's role in scanning and reinitiation and placed eIF3g near the mRNA entry channel through contacts with Rps3 and Rps20, providing a structural rationale for its function in start-codon traversal.\",\n      \"evidence\": \"In vivo mutagenesis, GCN4-lacZ reporters, ribosome sedimentation, and co-IP in S. cerevisiae\",\n      \"pmids\": [\"20679478\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Direct RNA target of the RRM during scanning not yet identified\", \"Generalizability beyond GCN4 reinitiation unresolved at this stage\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Connected EIF3G to mRNA surveillance and cytoskeletal localization by identifying PELO as a direct partner localizing to actin filaments.\",\n      \"evidence\": \"Yeast two-hybrid, GST pull-down, co-IP, and BiFC with domain mapping\",\n      \"pmids\": [\"20406461\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Functional output of the PELO–eIF3G complex not determined\", \"Significance of actin-filament localization unclear\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Identified a discrete SLIP1-binding motif in eIF3g, providing a molecular route to couple histone mRNA machinery to translation initiation.\",\n      \"evidence\": \"Crystal structures of SLIP1 with an SBM peptide plus GST pull-down\",\n      \"pmids\": [\"23804756\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Direct structure of the eIF3g SBM bound to SLIP1 not solved (peptide from related protein used)\", \"Functional impact on histone mRNA translation not measured here\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Revealed a moonlighting pro-apoptotic activity: caspase cleavage at SLRD220G generates a nuclear N-terminal fragment with DNase activity that activates caspase-3.\",\n      \"evidence\": \"Cleavage-site mapping by mutagenesis, nuclear translocation assays, and DNase activity assays in T24 cells\",\n      \"pmids\": [\"24080033\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Mechanism of DNase activity by an initiation factor fragment unexplained\", \"Single-lab finding without reciprocal confirmation\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Reported a nuclear interactome of eIF3g in breast cancer cells, raising the possibility of nuclear roles beyond cytoplasmic translation.\",\n      \"evidence\": \"Nuclear co-IP, mass spectrometry, cross-linking, GST pull-down, and confocal co-localization\",\n      \"pmids\": [\"26935993\"],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Descriptive interactome with no functional consequence established\", \"Single-lab, low-confidence observations not independently validated\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Showed EIF3G bridges the EJC to eIF3, enabling internal ribosome entry and translation of circular RNAs.\",\n      \"evidence\": \"Reciprocal co-IP, in vitro circRNA translation, polysomal fractionation, and transcriptome-wide ribosome association\",\n      \"pmids\": [\"37811880\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Structural basis of the eIF4A3–eIF3g bridge not resolved\", \"Scope of circRNAs dependent on this interaction not fully mapped\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Defined the EIF3G RRM as the catalytic determinant co-opted by SARS-CoV-2 Nsp1 for host mRNA cleavage, with a minimal 40S+RRM system sufficient for cleavage.\",\n      \"evidence\": \"In vitro reconstitution with minimal components and mutational mapping of a surface above the mRNA-binding channel\",\n      \"pmids\": [\"37821106\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Whether the RRM surface is intrinsically nucleolytic or requires Nsp1 catalysis unresolved\", \"Endogenous (non-viral) function of this RRM surface not addressed\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Established that eIF3g directly reads GUCG-centered motifs in 5'-coding regions to drive transcript-specific translational induction under heat stress, defining a sequence-specific mRNA selection function.\",\n      \"evidence\": \"SELEX, biolayer interferometry, ribosome profiling, reporter assays, and mutagenesis in yeast\",\n      \"pmids\": [\"41556339\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Whether GUCG-motif recognition operates in mammalian cells not tested\", \"Mechanism coupling motif binding to enhanced initiation not fully defined\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How the same RRM domain reconciles sequence-specific mRNA selection, scanning/reinitiation, circRNA IRES function, and viral-coopted endonucleolytic cleavage within the intact 40S–eIF3 complex remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"No unified structural model of the eIF3g RRM engaging different RNA classes\", \"Relationship between yeast scanning role and mammalian motif-recognition role unclear\", \"Endogenous physiological substrates of the RRM cleavage surface unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0, 5, 9]},\n      {\"term_id\": \"GO:0045182\", \"supporting_discovery_ids\": [0, 4, 2, 9]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [1, 2]},\n      {\"term_id\": \"GO:0140098\", \"supporting_discovery_ids\": [5]},\n      {\"term_id\": \"GO:0140097\", \"supporting_discovery_ids\": [6]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005840\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [4]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [6]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [7]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-72613\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [0, 4, 2]},\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [2, 9]},\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [6, 3]}\n    ],\n    \"complexes\": [\"eIF3\"],\n    \"partners\": [\"RPS3\", \"RPS20\", \"SLIP1\", \"EIF4A3\", \"AIF\", \"PELO\", \"EIF3I\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}