{"gene":"TAF2","run_date":"2026-06-10T10:51:54","timeline":{"discoveries":[{"year":1994,"finding":"Drosophila TAFII150 (TAF2 ortholog) directly binds TBP and dTAFII250, and binds specifically to DNA sequences overlapping the transcription start site, demonstrating that TAFII150 together with TBP are responsible for TFIID interactions with an extended region of the core promoter including the initiator.","method":"Biochemical co-purification, direct DNA binding studies with purified recombinant protein, in vivo association assays","journal":"Science","confidence":"High","confidence_rationale":"Tier 1-2 / Strong — direct binding demonstrated with purified recombinant protein, multiple orthogonal methods (protein-protein binding, DNA binding), replicated across Drosophila and yeast systems","pmids":["8178153"],"is_preprint":false},{"year":1998,"finding":"Human TAFII150/CIF150 (TAF2) mediates TFIID-dependent initiator (Inr) activity; it directly interacts with hTAFII135, stabilizes TFIID binding to core promoters containing Inr elements, and can complement TFIID fractions lacking Inr activity.","method":"In vitro complementation assay, in vitro binding assays (direct protein-protein interaction), biochemical fractionation","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — complementation assay plus direct in vitro binding assays, two orthogonal methods in single study","pmids":["9418870"],"is_preprint":false},{"year":1998,"finding":"Human TAFII150-containing TFIID complex is not sufficient alone for initiator-directed transcription; novel cofactors TIC-1, TIC-2, and TIC-3 and TFIIA are additionally required for TAFII-mediated core promoter-selective transcription synergism.","method":"In vitro transcription reconstitution with purified GTFs, RNA polymerase II, and partially purified cofactor fractions","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — biochemical reconstitution with purified components, multiple cofactor fractions tested, clear functional readout","pmids":["9774672"],"is_preprint":false},{"year":1999,"finding":"Functional knockout of CIF150/hTAFII150 (TAF2) causes G2/M cell cycle arrest and selectively reduces transcription of cyclin B1 and cyclin A; a CIF150-responsive cis-element was identified in the cyclin B1 core promoter.","method":"Transient functional knockout, gel filtration, PCR display analysis, cotransfection assays, in vitro transcription assays","journal":"Molecular and cellular biology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — loss-of-function with specific phenotypic readout (G2/M arrest), supported by in vitro transcription and promoter element mapping","pmids":["10409744"],"is_preprint":false},{"year":2009,"finding":"Yeast Taf2p is positioned within the TFIID complex in the vicinity of Taf1p and TBP, as determined by cryo-EM structural mapping using a Taf2p-depleted TFIID preparation and immunolabeling with a subunit-specific antibody.","method":"Electron tomography, cryo-electron microscopy, immunolabeling with subunit-specific antibody, comparison of Taf2p-containing vs Taf2p-depleted TFIID","journal":"Structure","confidence":"High","confidence_rationale":"Tier 1 / Moderate — structural determination by cryo-EM with immunolabeling confirmation, multiple orthogonal approaches","pmids":["19278651"],"is_preprint":false},{"year":2009,"finding":"In yeast, a taf1 mutation specifically reduces Taf2 occupancy at promoters genome-wide, and sequential ChIP suggests different TFIID conformations exist at different promoters (RPGs vs non-RPGs), with SAGA and TFIID co-localizing on RPG promoters.","method":"ChIP-chip genome-wide localization, conventional and sequential ChIP","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — genome-wide ChIP-chip in single lab, clear specific effect of taf1 mutation on Taf2 occupancy, but single study","pmids":["20026583"],"is_preprint":false},{"year":2015,"finding":"TAF2 assembles with TAF8 and TAF10 into a heterotrimeric cytoplasmic subcomplex; TAF8 nucleates the complex; TAF2 binds multiple motifs within the TAF8 C-terminal region; this cytoplasmic assembly dictates TAF2 incorporation into nuclear core-TFIID, providing evidence for stepwise holo-TFIID assembly via nuclear import of preformed cytoplasmic submodules.","method":"Native mass spectrometry, X-ray crystallography of TAF8-TAF10 histone fold domains, co-immunoprecipitation, biochemical fractionation","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structure plus native MS plus Co-IP, multiple orthogonal methods, defines precise interaction domains","pmids":["25586196"],"is_preprint":false},{"year":2016,"finding":"The C-terminal region of yeast Taf2 directly interacts with Taf14 and mediates stable incorporation of Taf14 into the TFIID complex; a Taf2-ΔC separation-of-function variant incorporates into TFIID but lacks Taf14, demonstrating the Taf2 C-terminus specifically mediates Taf14 recruitment.","method":"Site-directed mutagenesis (systematic), temperature-sensitive allele screen, in vitro and in vivo co-immunoprecipitation, overexpression suppression genetics","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 / Strong — systematic mutagenesis, genetic suppression, in vitro and in vivo binding assays, separation-of-function allele, multiple orthogonal methods","pmids":["27587401"],"is_preprint":false},{"year":2021,"finding":"Four distinct regions in the TAF8 C-terminal proline-rich domain are each individually required for interaction with TAF2 in TFIID lobe C; CRISPR/Cas9 deletion of the TAF8 proline-rich domain that interacts with TAF2 abolishes mouse embryonic stem cell survival.","method":"In vitro assembly assays, co-immunoprecipitation, CRISPR/Cas9 gene editing with cell viability readout","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — domain mapping by in vitro assembly, CRISPR validation with functional readout (ESC survival), two orthogonal methods","pmids":["34634302"],"is_preprint":false},{"year":2022,"finding":"The YEATS and ET domains of yeast Taf14 bind the C-terminal tail of Taf2; Taf2 binding promotes a conformational rearrangement in Taf14 that releases an autoinhibited linker region, enabling Taf14 to bind DNA and nucleosomes; in vivo, Taf14 association with both Taf2 and DNA is essential for transcriptional regulation.","method":"X-ray crystallography/structural determination, in vitro binding assays, mutagenesis, in vivo genetic assays","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — structural determination of complex, mutagenesis, in vitro binding, in vivo genetic validation, multiple orthogonal methods","pmids":["35676274"],"is_preprint":false},{"year":2024,"finding":"TAF2 is sub-stoichiometrically associated with TFIID and regulates TBP/TFIID binding and transcription of only a small subset of protein-coding genes, including ribosomal protein genes RPL30 and RPL39; TAF2 depletion reduces ribosome assembly and global protein translation.","method":"Co-immunoprecipitation, inducible TAF2 degradation system, genome-wide ChIP-seq, ribosome assembly assay, protein translation assay","journal":"Cell death discovery","confidence":"High","confidence_rationale":"Tier 2 / Moderate — inducible degradation with genome-wide binding profiles, multiple orthogonal readouts (ChIP-seq, ribosome assembly, translation), single lab","pmids":["38773077"],"is_preprint":false},{"year":2025,"finding":"TAF2 contains a conserved intrinsically disordered region (IDR) that drives TAF2 condensation into nuclear speckles independently of other TFIID subunits; the TAF2 IDR directly interacts with the RNA splicing factor SRRM2 in nuclear speckles; IDR deletion does not majorly affect global gene expression but alters alternative splicing events and increases TAF2 promoter association.","method":"Live-cell imaging, quantitative proximity mass spectrometry, genome-wide ChIP-seq, alternative splicing analysis, IDR deletion mutant","journal":"Cell reports","confidence":"High","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (imaging, MS, genomics, splicing analysis), IDR deletion mutant with functional consequences, single lab","pmids":["40287942"],"is_preprint":false},{"year":2025,"finding":"Hepatocyte-specific conditional knockout of Taf2 causes hepatocyte death and compensatory proliferation leading to an inflammatory/fibrotic environment; TAF2 binds promoters of tumor-promoting genes and non-coding RNAs to regulate their transcription.","method":"Hepatocyte-specific conditional knockout mouse, ChIP (promoter binding), TAF2 knockdown and overexpression in human HCC cells","journal":"Hepatology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — conditional knockout with specific phenotype, ChIP for promoter binding, but abstract-level detail on mechanism is limited","pmids":["40392063"],"is_preprint":false}],"current_model":"TAF2 is a sub-stoichiometric subunit of the TFIID complex that directly binds TBP, TAF1/TAFII250, and—via multiple motifs in the TAF8 C-terminal region—is recruited into TFIID through a cytoplasmic TAF2-TAF8-TAF10 preassembly module; within TFIID it contacts DNA at the initiator/transcription start site, selectively regulates TBP/TFIID binding to a small subset of promoters (including ribosomal protein genes required for translation), controls cell cycle progression (G2/M) through cyclin B1/A transcription, and an intrinsically disordered region drives TAF2 into nuclear speckle condensates where it interacts with splicing factor SRRM2 to influence alternative splicing, while in yeast its C-terminal tail recruits Taf14 and allosterically activates Taf14's DNA/nucleosome-binding activity."},"narrative":{"mechanistic_narrative":"TAF2 is a subunit of the general transcription factor TFIID that confers core-promoter selectivity by recognizing the initiator element at the transcription start site, where it acts together with TBP to extend TFIID's contacts across the core promoter [PMID:8178153, PMID:9418870]. It is positioned within TFIID adjacent to TAF1 and TBP and stabilizes TFIID binding to initiator-containing promoters [PMID:9418870, PMID:19278651]. TAF2 reaches TFIID through an ordered assembly route: it first forms a cytoplasmic heterotrimer with TAF8 and TAF10, binding multiple motifs in the TAF8 C-terminal proline-rich region, and this preassembled submodule is imported and incorporated into nuclear core-TFIID—an interaction so central that loss of the TAF8 region engaging TAF2 abolishes embryonic stem cell survival [PMID:25586196, PMID:34634302]. Although associated only sub-stoichiometrically with TFIID, TAF2 governs TBP/TFIID occupancy and transcription at a restricted subset of genes: it selectively drives cyclin B1 and cyclin A transcription to permit G2/M progression, and it controls ribosomal protein genes such as RPL30 and RPL39, so that its loss impairs ribosome assembly and global translation [PMID:10409744, PMID:38773077]. Beyond its TFIID role, a conserved intrinsically disordered region partitions TAF2 into nuclear speckle condensates where it engages the splicing factor SRRM2 and modulates alternative splicing [PMID:40287942]. In yeast, the Taf2 C-terminal tail recruits Taf14 into TFIID and allosterically relieves Taf14 autoinhibition to license its DNA/nucleosome binding [PMID:27587401, PMID:35676274]. Hepatocyte-specific loss of Taf2 in mice triggers cell death, compensatory proliferation, and an inflammatory/fibrotic state, with TAF2 binding promoters of tumor-promoting genes [PMID:40392063].","teleology":[{"year":1994,"claim":"Established that the TAF2 ortholog is the TFIID component responsible for core-promoter recognition beyond TBP, answering how TFIID engages the initiator region.","evidence":"Biochemical co-purification and direct DNA/protein binding with purified recombinant Drosophila TAFII150","pmids":["8178153"],"confidence":"High","gaps":["Did not define the human ortholog's behavior","Initiator binding determinants within TAF2 not mapped at residue level"]},{"year":1998,"claim":"Showed the human protein mediates TFIID-dependent initiator activity and stabilizes TFIID on Inr promoters, but is insufficient alone—additional cofactors and TFIIA are required for promoter-selective synergism.","evidence":"In vitro complementation, direct binding assays, and reconstitution with purified GTFs and cofactor fractions","pmids":["9418870","9774672"],"confidence":"High","gaps":["Molecular identities/mechanism of TIC-1/2/3 cofactors unresolved","Promoter scope of Inr selectivity not defined genome-wide"]},{"year":1999,"claim":"Linked TAF2 function to cell cycle control by identifying selective transcriptional targets, demonstrating that loss causes G2/M arrest via reduced cyclin B1/A expression.","evidence":"Transient functional knockout, in vitro transcription, and cyclin B1 promoter element mapping","pmids":["10409744"],"confidence":"High","gaps":["Mechanism of target selectivity not explained","Direct vs indirect promoter effects not fully separated"]},{"year":2009,"claim":"Placed Taf2 spatially within TFIID near Taf1 and TBP and showed taf1-dependence of Taf2 promoter occupancy, providing structural and genome-wide context for its function.","evidence":"Cryo-EM/electron tomography with immunolabeling and ChIP-chip in yeast","pmids":["19278651","20026583"],"confidence":"High","gaps":["High-resolution atomic placement of Taf2 not achieved","Conformational differences across promoter classes only inferred"]},{"year":2015,"claim":"Defined the assembly pathway by showing TAF2 enters TFIID via a cytoplasmic TAF8-nucleated TAF2-TAF8-TAF10 submodule, establishing stepwise holo-TFIID formation through nuclear import.","evidence":"Native mass spectrometry, X-ray crystallography of TAF8-TAF10 histone folds, and Co-IP","pmids":["25586196"],"confidence":"High","gaps":["Nuclear import machinery for the submodule not identified","Kinetics of submodule integration into core-TFIID unknown"]},{"year":2021,"claim":"Mapped four discrete TAF8 proline-rich regions each required for TAF2 binding and demonstrated this interface is essential for cell viability.","evidence":"In vitro assembly assays, Co-IP, and CRISPR/Cas9 deletion with ESC survival readout","pmids":["34634302"],"confidence":"High","gaps":["Whether viability loss reflects TFIID disassembly specifically not isolated","Structure of the TAF2-TAF8 interface unresolved"]},{"year":2016,"claim":"Identified the yeast Taf2 C-terminus as the recruiter of Taf14 into TFIID using a separation-of-function allele, distinguishing TFIID incorporation from Taf14 recruitment.","evidence":"Systematic mutagenesis, ts allele screen, in vitro/in vivo Co-IP, and suppression genetics","pmids":["27587401"],"confidence":"High","gaps":["Conservation of this recruitment in human TAF2 not established","Functional consequence of Taf14 loss from TFIID not fully detailed here"]},{"year":2022,"claim":"Provided the mechanism for Taf2-Taf14 functional coupling: Taf2 binding to Taf14 YEATS/ET domains relieves an autoinhibitory linker, licensing Taf14 DNA/nucleosome binding required for transcription.","evidence":"X-ray crystallography, in vitro binding, mutagenesis, and in vivo genetics in yeast","pmids":["35676274"],"confidence":"High","gaps":["Human relevance of the allosteric mechanism unknown","How this gates promoter-specific transcription not resolved"]},{"year":2024,"claim":"Demonstrated that despite sub-stoichiometric TFIID association, TAF2 selectively controls a small gene subset including ribosomal protein genes, linking TAF2 loss to impaired ribosome assembly and translation.","evidence":"Inducible TAF2 degradation, genome-wide ChIP-seq, ribosome assembly and translation assays","pmids":["38773077"],"confidence":"High","gaps":["Basis for promoter selectivity at the sequence level unresolved","Single-lab observation"]},{"year":2025,"claim":"Revealed a TFIID-independent role: a conserved IDR drives TAF2 into nuclear speckles where it binds SRRM2 and influences alternative splicing, expanding TAF2 function beyond transcription initiation.","evidence":"Live-cell imaging, proximity mass spectrometry, ChIP-seq, splicing analysis, and IDR deletion mutant","pmids":["40287942"],"confidence":"High","gaps":["Direct vs scaffolding role in splicing not distinguished","Relationship between condensate partitioning and TFIID occupancy unclear"]},{"year":2025,"claim":"Established an in vivo physiological/pathological role by showing hepatocyte Taf2 loss causes cell death, fibrosis, and inflammation, with TAF2 binding tumor-promoting gene promoters.","evidence":"Hepatocyte-specific conditional knockout mouse, ChIP, and knockdown/overexpression in HCC cells","pmids":["40392063"],"confidence":"Medium","gaps":["Mechanistic detail limited to abstract-level promoter binding","Causal link between specific targets and phenotype not dissected"]},{"year":null,"claim":"How TAF2 achieves selectivity for its restricted target gene set and how its TFIID-bound and condensate/splicing functions are mechanistically coordinated remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No sequence/structural determinant for promoter selectivity defined","Interplay between IDR-driven condensation and core-promoter occupancy unknown","Human conservation of yeast Taf2-Taf14 allostery untested"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003677","term_label":"DNA binding","supporting_discovery_ids":[0,1]},{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[3,10]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[6,7]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[6]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[6]},{"term_id":"GO:0005654","term_label":"nucleoplasm","supporting_discovery_ids":[11]}],"pathway":[{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[0,1,10]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[3]},{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[11]}],"complexes":["TFIID","cytoplasmic TAF2-TAF8-TAF10 submodule"],"partners":["TBP","TAF1","TAF8","TAF10","TAF14","SRRM2"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q6P1X5","full_name":"Transcription initiation factor TFIID subunit 2","aliases":["150 kDa cofactor of initiator function","RNA polymerase II TBP-associated factor subunit B","TBP-associated factor 150 kDa","Transcription initiation factor TFIID 150 kDa subunit","TAF(II)150","TAFII-150","TAFII150"],"length_aa":1199,"mass_kda":137.0,"function":"The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, PubMed:9418870, PubMed:9774672). TAF2 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF1 (PubMed:33795473, PubMed:9774672)","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/Q6P1X5/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/TAF2","classification":"Common Essential","n_dependent_lines":1047,"n_total_lines":1208,"dependency_fraction":0.8667218543046358},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/TAF2","total_profiled":1310},"omim":[{"mim_id":"615599","title":"NEURODEVELOPMENTAL DISORDER WITH FEEDING DIFFICULTIES, THIN CORPUS CALLOSUM, AND FOOT DEFORMITY; NEDFCF","url":"https://www.omim.org/entry/615599"},{"mim_id":"604912","title":"TAF2 RNA POLYMERASE II, TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR, 150-KD; TAF2","url":"https://www.omim.org/entry/604912"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in many","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TAF2"},"hgnc":{"alias_symbol":["TAFII150","CIF150"],"prev_symbol":["TAF2B"]},"alphafold":{"accession":"Q6P1X5","domains":[{"cath_id":"2.60.40.1730","chopping":"23-88_126-254","consensus_level":"medium","plddt":88.5566,"start":23,"end":254},{"cath_id":"1.10.390","chopping":"370-524","consensus_level":"medium","plddt":81.5456,"start":370,"end":524},{"cath_id":"2.60.40","chopping":"530-637","consensus_level":"medium","plddt":81.1756,"start":530,"end":637}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6P1X5","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q6P1X5-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q6P1X5-F1-predicted_aligned_error_v6.png","plddt_mean":73.56},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TAF2","jax_strain_url":"https://www.jax.org/strain/search?query=TAF2"},"sequence":{"accession":"Q6P1X5","fasta_url":"https://rest.uniprot.org/uniprotkb/Q6P1X5.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q6P1X5/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6P1X5"}},"corpus_meta":[{"pmid":"8178153","id":"PMC_8178153","title":"Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding to core promoter DNA.","date":"1994","source":"Science (New York, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/8178153","citation_count":199,"is_preprint":false},{"pmid":"25586196","id":"PMC_25586196","title":"Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.","date":"2015","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/25586196","citation_count":80,"is_preprint":false},{"pmid":"9774672","id":"PMC_9774672","title":"Novel cofactors and TFIIA mediate functional core promoter selectivity by the human TAFII150-containing TFIID complex.","date":"1998","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/9774672","citation_count":62,"is_preprint":false},{"pmid":"9418870","id":"PMC_9418870","title":"CIF150, a human cofactor for transcription factor IID-dependent initiator function.","date":"1998","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/9418870","citation_count":58,"is_preprint":false},{"pmid":"19278651","id":"PMC_19278651","title":"Mapping the initiator binding Taf2 subunit in the structure of hydrated yeast TFIID.","date":"2009","source":"Structure (London, England : 1993)","url":"https://pubmed.ncbi.nlm.nih.gov/19278651","citation_count":37,"is_preprint":false},{"pmid":"24084144","id":"PMC_24084144","title":"Microcephaly thin corpus callosum intellectual disability syndrome caused by mutated TAF2.","date":"2013","source":"Pediatric neurology","url":"https://pubmed.ncbi.nlm.nih.gov/24084144","citation_count":31,"is_preprint":false},{"pmid":"10409744","id":"PMC_10409744","title":"Human transcription factor hTAF(II)150 (CIF150) is involved in transcriptional regulation of cell cycle progression.","date":"1999","source":"Molecular and cellular biology","url":"https://pubmed.ncbi.nlm.nih.gov/10409744","citation_count":29,"is_preprint":false},{"pmid":"27587401","id":"PMC_27587401","title":"The C Terminus of the RNA Polymerase II Transcription Factor IID (TFIID) Subunit Taf2 Mediates Stable Association of Subunit Taf14 into the Yeast TFIID Complex.","date":"2016","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/27587401","citation_count":15,"is_preprint":false},{"pmid":"20026583","id":"PMC_20026583","title":"Genome-wide localization analysis of a complete set of Tafs reveals a specific effect of the taf1 mutation on Taf2 occupancy and provides indirect evidence for different TFIID conformations at different promoters.","date":"2009","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/20026583","citation_count":12,"is_preprint":false},{"pmid":"35676274","id":"PMC_35676274","title":"Taf2 mediates DNA binding of Taf14.","date":"2022","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/35676274","citation_count":9,"is_preprint":false},{"pmid":"34634302","id":"PMC_34634302","title":"TAF8 regions important for TFIID lobe B assembly or for TAF2 interactions are required for embryonic stem cell survival.","date":"2021","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/34634302","citation_count":6,"is_preprint":false},{"pmid":"38773077","id":"PMC_38773077","title":"TAF2, within the TFIID complex, regulates the expression of a subset of protein-coding genes.","date":"2024","source":"Cell death discovery","url":"https://pubmed.ncbi.nlm.nih.gov/38773077","citation_count":5,"is_preprint":false},{"pmid":"34474177","id":"PMC_34474177","title":"Phenotype associated with TAF2 biallelic mutations: A clinical description of four individuals and review of the literature.","date":"2021","source":"European journal of medical genetics","url":"https://pubmed.ncbi.nlm.nih.gov/34474177","citation_count":5,"is_preprint":false},{"pmid":"40287942","id":"PMC_40287942","title":"TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing factors.","date":"2025","source":"Cell reports","url":"https://pubmed.ncbi.nlm.nih.gov/40287942","citation_count":3,"is_preprint":false},{"pmid":"40392063","id":"PMC_40392063","title":"TATA-box binding protein-associated factor 2 (TAF2) in hepatocyte survival and tumorigenesis.","date":"2025","source":"Hepatology (Baltimore, Md.)","url":"https://pubmed.ncbi.nlm.nih.gov/40392063","citation_count":1,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8976,"output_tokens":3187,"usd":0.037366,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10615,"output_tokens":3732,"usd":0.073188,"stage2_stop_reason":"end_turn"},"total_usd":0.110554,"stage1_batch_id":"msgbatch_017qqVz33Ga63SCDwzb35XPb","stage2_batch_id":"msgbatch_01Scr2Ei9x4HJMiRGxwrmvLK","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1994,\n      \"finding\": \"Drosophila TAFII150 (TAF2 ortholog) directly binds TBP and dTAFII250, and binds specifically to DNA sequences overlapping the transcription start site, demonstrating that TAFII150 together with TBP are responsible for TFIID interactions with an extended region of the core promoter including the initiator.\",\n      \"method\": \"Biochemical co-purification, direct DNA binding studies with purified recombinant protein, in vivo association assays\",\n      \"journal\": \"Science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Strong — direct binding demonstrated with purified recombinant protein, multiple orthogonal methods (protein-protein binding, DNA binding), replicated across Drosophila and yeast systems\",\n      \"pmids\": [\"8178153\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1998,\n      \"finding\": \"Human TAFII150/CIF150 (TAF2) mediates TFIID-dependent initiator (Inr) activity; it directly interacts with hTAFII135, stabilizes TFIID binding to core promoters containing Inr elements, and can complement TFIID fractions lacking Inr activity.\",\n      \"method\": \"In vitro complementation assay, in vitro binding assays (direct protein-protein interaction), biochemical fractionation\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — complementation assay plus direct in vitro binding assays, two orthogonal methods in single study\",\n      \"pmids\": [\"9418870\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1998,\n      \"finding\": \"Human TAFII150-containing TFIID complex is not sufficient alone for initiator-directed transcription; novel cofactors TIC-1, TIC-2, and TIC-3 and TFIIA are additionally required for TAFII-mediated core promoter-selective transcription synergism.\",\n      \"method\": \"In vitro transcription reconstitution with purified GTFs, RNA polymerase II, and partially purified cofactor fractions\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — biochemical reconstitution with purified components, multiple cofactor fractions tested, clear functional readout\",\n      \"pmids\": [\"9774672\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1999,\n      \"finding\": \"Functional knockout of CIF150/hTAFII150 (TAF2) causes G2/M cell cycle arrest and selectively reduces transcription of cyclin B1 and cyclin A; a CIF150-responsive cis-element was identified in the cyclin B1 core promoter.\",\n      \"method\": \"Transient functional knockout, gel filtration, PCR display analysis, cotransfection assays, in vitro transcription assays\",\n      \"journal\": \"Molecular and cellular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function with specific phenotypic readout (G2/M arrest), supported by in vitro transcription and promoter element mapping\",\n      \"pmids\": [\"10409744\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"Yeast Taf2p is positioned within the TFIID complex in the vicinity of Taf1p and TBP, as determined by cryo-EM structural mapping using a Taf2p-depleted TFIID preparation and immunolabeling with a subunit-specific antibody.\",\n      \"method\": \"Electron tomography, cryo-electron microscopy, immunolabeling with subunit-specific antibody, comparison of Taf2p-containing vs Taf2p-depleted TFIID\",\n      \"journal\": \"Structure\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — structural determination by cryo-EM with immunolabeling confirmation, multiple orthogonal approaches\",\n      \"pmids\": [\"19278651\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"In yeast, a taf1 mutation specifically reduces Taf2 occupancy at promoters genome-wide, and sequential ChIP suggests different TFIID conformations exist at different promoters (RPGs vs non-RPGs), with SAGA and TFIID co-localizing on RPG promoters.\",\n      \"method\": \"ChIP-chip genome-wide localization, conventional and sequential ChIP\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — genome-wide ChIP-chip in single lab, clear specific effect of taf1 mutation on Taf2 occupancy, but single study\",\n      \"pmids\": [\"20026583\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"TAF2 assembles with TAF8 and TAF10 into a heterotrimeric cytoplasmic subcomplex; TAF8 nucleates the complex; TAF2 binds multiple motifs within the TAF8 C-terminal region; this cytoplasmic assembly dictates TAF2 incorporation into nuclear core-TFIID, providing evidence for stepwise holo-TFIID assembly via nuclear import of preformed cytoplasmic submodules.\",\n      \"method\": \"Native mass spectrometry, X-ray crystallography of TAF8-TAF10 histone fold domains, co-immunoprecipitation, biochemical fractionation\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structure plus native MS plus Co-IP, multiple orthogonal methods, defines precise interaction domains\",\n      \"pmids\": [\"25586196\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"The C-terminal region of yeast Taf2 directly interacts with Taf14 and mediates stable incorporation of Taf14 into the TFIID complex; a Taf2-ΔC separation-of-function variant incorporates into TFIID but lacks Taf14, demonstrating the Taf2 C-terminus specifically mediates Taf14 recruitment.\",\n      \"method\": \"Site-directed mutagenesis (systematic), temperature-sensitive allele screen, in vitro and in vivo co-immunoprecipitation, overexpression suppression genetics\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Strong — systematic mutagenesis, genetic suppression, in vitro and in vivo binding assays, separation-of-function allele, multiple orthogonal methods\",\n      \"pmids\": [\"27587401\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Four distinct regions in the TAF8 C-terminal proline-rich domain are each individually required for interaction with TAF2 in TFIID lobe C; CRISPR/Cas9 deletion of the TAF8 proline-rich domain that interacts with TAF2 abolishes mouse embryonic stem cell survival.\",\n      \"method\": \"In vitro assembly assays, co-immunoprecipitation, CRISPR/Cas9 gene editing with cell viability readout\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — domain mapping by in vitro assembly, CRISPR validation with functional readout (ESC survival), two orthogonal methods\",\n      \"pmids\": [\"34634302\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"The YEATS and ET domains of yeast Taf14 bind the C-terminal tail of Taf2; Taf2 binding promotes a conformational rearrangement in Taf14 that releases an autoinhibited linker region, enabling Taf14 to bind DNA and nucleosomes; in vivo, Taf14 association with both Taf2 and DNA is essential for transcriptional regulation.\",\n      \"method\": \"X-ray crystallography/structural determination, in vitro binding assays, mutagenesis, in vivo genetic assays\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — structural determination of complex, mutagenesis, in vitro binding, in vivo genetic validation, multiple orthogonal methods\",\n      \"pmids\": [\"35676274\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"TAF2 is sub-stoichiometrically associated with TFIID and regulates TBP/TFIID binding and transcription of only a small subset of protein-coding genes, including ribosomal protein genes RPL30 and RPL39; TAF2 depletion reduces ribosome assembly and global protein translation.\",\n      \"method\": \"Co-immunoprecipitation, inducible TAF2 degradation system, genome-wide ChIP-seq, ribosome assembly assay, protein translation assay\",\n      \"journal\": \"Cell death discovery\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — inducible degradation with genome-wide binding profiles, multiple orthogonal readouts (ChIP-seq, ribosome assembly, translation), single lab\",\n      \"pmids\": [\"38773077\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TAF2 contains a conserved intrinsically disordered region (IDR) that drives TAF2 condensation into nuclear speckles independently of other TFIID subunits; the TAF2 IDR directly interacts with the RNA splicing factor SRRM2 in nuclear speckles; IDR deletion does not majorly affect global gene expression but alters alternative splicing events and increases TAF2 promoter association.\",\n      \"method\": \"Live-cell imaging, quantitative proximity mass spectrometry, genome-wide ChIP-seq, alternative splicing analysis, IDR deletion mutant\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (imaging, MS, genomics, splicing analysis), IDR deletion mutant with functional consequences, single lab\",\n      \"pmids\": [\"40287942\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Hepatocyte-specific conditional knockout of Taf2 causes hepatocyte death and compensatory proliferation leading to an inflammatory/fibrotic environment; TAF2 binds promoters of tumor-promoting genes and non-coding RNAs to regulate their transcription.\",\n      \"method\": \"Hepatocyte-specific conditional knockout mouse, ChIP (promoter binding), TAF2 knockdown and overexpression in human HCC cells\",\n      \"journal\": \"Hepatology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — conditional knockout with specific phenotype, ChIP for promoter binding, but abstract-level detail on mechanism is limited\",\n      \"pmids\": [\"40392063\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TAF2 is a sub-stoichiometric subunit of the TFIID complex that directly binds TBP, TAF1/TAFII250, and—via multiple motifs in the TAF8 C-terminal region—is recruited into TFIID through a cytoplasmic TAF2-TAF8-TAF10 preassembly module; within TFIID it contacts DNA at the initiator/transcription start site, selectively regulates TBP/TFIID binding to a small subset of promoters (including ribosomal protein genes required for translation), controls cell cycle progression (G2/M) through cyclin B1/A transcription, and an intrinsically disordered region drives TAF2 into nuclear speckle condensates where it interacts with splicing factor SRRM2 to influence alternative splicing, while in yeast its C-terminal tail recruits Taf14 and allosterically activates Taf14's DNA/nucleosome-binding activity.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TAF2 is a subunit of the general transcription factor TFIID that confers core-promoter selectivity by recognizing the initiator element at the transcription start site, where it acts together with TBP to extend TFIID's contacts across the core promoter [#0, #1]. It is positioned within TFIID adjacent to TAF1 and TBP and stabilizes TFIID binding to initiator-containing promoters [#1, #4]. TAF2 reaches TFIID through an ordered assembly route: it first forms a cytoplasmic heterotrimer with TAF8 and TAF10, binding multiple motifs in the TAF8 C-terminal proline-rich region, and this preassembled submodule is imported and incorporated into nuclear core-TFIID—an interaction so central that loss of the TAF8 region engaging TAF2 abolishes embryonic stem cell survival [#6, #8]. Although associated only sub-stoichiometrically with TFIID, TAF2 governs TBP/TFIID occupancy and transcription at a restricted subset of genes: it selectively drives cyclin B1 and cyclin A transcription to permit G2/M progression, and it controls ribosomal protein genes such as RPL30 and RPL39, so that its loss impairs ribosome assembly and global translation [#3, #10]. Beyond its TFIID role, a conserved intrinsically disordered region partitions TAF2 into nuclear speckle condensates where it engages the splicing factor SRRM2 and modulates alternative splicing [#11]. In yeast, the Taf2 C-terminal tail recruits Taf14 into TFIID and allosterically relieves Taf14 autoinhibition to license its DNA/nucleosome binding [#7, #9]. Hepatocyte-specific loss of Taf2 in mice triggers cell death, compensatory proliferation, and an inflammatory/fibrotic state, with TAF2 binding promoters of tumor-promoting genes [#12].\",\n  \"teleology\": [\n    {\n      \"year\": 1994,\n      \"claim\": \"Established that the TAF2 ortholog is the TFIID component responsible for core-promoter recognition beyond TBP, answering how TFIID engages the initiator region.\",\n      \"evidence\": \"Biochemical co-purification and direct DNA/protein binding with purified recombinant Drosophila TAFII150\",\n      \"pmids\": [\"8178153\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not define the human ortholog's behavior\", \"Initiator binding determinants within TAF2 not mapped at residue level\"]\n    },\n    {\n      \"year\": 1998,\n      \"claim\": \"Showed the human protein mediates TFIID-dependent initiator activity and stabilizes TFIID on Inr promoters, but is insufficient alone—additional cofactors and TFIIA are required for promoter-selective synergism.\",\n      \"evidence\": \"In vitro complementation, direct binding assays, and reconstitution with purified GTFs and cofactor fractions\",\n      \"pmids\": [\"9418870\", \"9774672\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular identities/mechanism of TIC-1/2/3 cofactors unresolved\", \"Promoter scope of Inr selectivity not defined genome-wide\"]\n    },\n    {\n      \"year\": 1999,\n      \"claim\": \"Linked TAF2 function to cell cycle control by identifying selective transcriptional targets, demonstrating that loss causes G2/M arrest via reduced cyclin B1/A expression.\",\n      \"evidence\": \"Transient functional knockout, in vitro transcription, and cyclin B1 promoter element mapping\",\n      \"pmids\": [\"10409744\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism of target selectivity not explained\", \"Direct vs indirect promoter effects not fully separated\"]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Placed Taf2 spatially within TFIID near Taf1 and TBP and showed taf1-dependence of Taf2 promoter occupancy, providing structural and genome-wide context for its function.\",\n      \"evidence\": \"Cryo-EM/electron tomography with immunolabeling and ChIP-chip in yeast\",\n      \"pmids\": [\"19278651\", \"20026583\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"High-resolution atomic placement of Taf2 not achieved\", \"Conformational differences across promoter classes only inferred\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Defined the assembly pathway by showing TAF2 enters TFIID via a cytoplasmic TAF8-nucleated TAF2-TAF8-TAF10 submodule, establishing stepwise holo-TFIID formation through nuclear import.\",\n      \"evidence\": \"Native mass spectrometry, X-ray crystallography of TAF8-TAF10 histone folds, and Co-IP\",\n      \"pmids\": [\"25586196\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Nuclear import machinery for the submodule not identified\", \"Kinetics of submodule integration into core-TFIID unknown\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Mapped four discrete TAF8 proline-rich regions each required for TAF2 binding and demonstrated this interface is essential for cell viability.\",\n      \"evidence\": \"In vitro assembly assays, Co-IP, and CRISPR/Cas9 deletion with ESC survival readout\",\n      \"pmids\": [\"34634302\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether viability loss reflects TFIID disassembly specifically not isolated\", \"Structure of the TAF2-TAF8 interface unresolved\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Identified the yeast Taf2 C-terminus as the recruiter of Taf14 into TFIID using a separation-of-function allele, distinguishing TFIID incorporation from Taf14 recruitment.\",\n      \"evidence\": \"Systematic mutagenesis, ts allele screen, in vitro/in vivo Co-IP, and suppression genetics\",\n      \"pmids\": [\"27587401\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Conservation of this recruitment in human TAF2 not established\", \"Functional consequence of Taf14 loss from TFIID not fully detailed here\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Provided the mechanism for Taf2-Taf14 functional coupling: Taf2 binding to Taf14 YEATS/ET domains relieves an autoinhibitory linker, licensing Taf14 DNA/nucleosome binding required for transcription.\",\n      \"evidence\": \"X-ray crystallography, in vitro binding, mutagenesis, and in vivo genetics in yeast\",\n      \"pmids\": [\"35676274\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Human relevance of the allosteric mechanism unknown\", \"How this gates promoter-specific transcription not resolved\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Demonstrated that despite sub-stoichiometric TFIID association, TAF2 selectively controls a small gene subset including ribosomal protein genes, linking TAF2 loss to impaired ribosome assembly and translation.\",\n      \"evidence\": \"Inducible TAF2 degradation, genome-wide ChIP-seq, ribosome assembly and translation assays\",\n      \"pmids\": [\"38773077\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Basis for promoter selectivity at the sequence level unresolved\", \"Single-lab observation\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Revealed a TFIID-independent role: a conserved IDR drives TAF2 into nuclear speckles where it binds SRRM2 and influences alternative splicing, expanding TAF2 function beyond transcription initiation.\",\n      \"evidence\": \"Live-cell imaging, proximity mass spectrometry, ChIP-seq, splicing analysis, and IDR deletion mutant\",\n      \"pmids\": [\"40287942\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct vs scaffolding role in splicing not distinguished\", \"Relationship between condensate partitioning and TFIID occupancy unclear\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Established an in vivo physiological/pathological role by showing hepatocyte Taf2 loss causes cell death, fibrosis, and inflammation, with TAF2 binding tumor-promoting gene promoters.\",\n      \"evidence\": \"Hepatocyte-specific conditional knockout mouse, ChIP, and knockdown/overexpression in HCC cells\",\n      \"pmids\": [\"40392063\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanistic detail limited to abstract-level promoter binding\", \"Causal link between specific targets and phenotype not dissected\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TAF2 achieves selectivity for its restricted target gene set and how its TFIID-bound and condensate/splicing functions are mechanistically coordinated remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No sequence/structural determinant for promoter selectivity defined\", \"Interplay between IDR-driven condensation and core-promoter occupancy unknown\", \"Human conservation of yeast Taf2-Taf14 allostery untested\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003677\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [3, 10]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [6, 7]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [6]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [6]},\n      {\"term_id\": \"GO:0005654\", \"supporting_discovery_ids\": [11]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [0, 1, 10]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [11]}\n    ],\n    \"complexes\": [\"TFIID\", \"cytoplasmic TAF2-TAF8-TAF10 submodule\"],\n    \"partners\": [\"TBP\", \"TAF1\", \"TAF8\", \"TAF10\", \"TAF14\", \"SRRM2\"],\n    \"other_free_text\": []\n  }\n}\n```","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":7,"faith_total":7,"faith_pct":100.0}}