{"gene":"RPP30","run_date":"2026-06-10T07:46:27","timeline":{"discoveries":[{"year":2010,"finding":"Archaeal RNase P proteins PhoPop5 and PhoRpp30 function equivalently to the E. coli C5 protein in activating the C-domain of RNase P RNA (PhopRNA), while PhoRpp21 and PhoRpp29 are implicated in stabilization of the S-domain; established using chimeric RNase P RNAs with exchanged C- and S-domains and pre-tRNA cleavage assays.","method":"Chimeric RNA reconstitution assay, pre-tRNA cleavage activity assay","journal":"Bioscience, biotechnology, and biochemistry","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro reconstitution with chimeric RNAs, single lab, single study","pmids":["20139629"],"is_preprint":false},{"year":2011,"finding":"Archaeal RPP30 and Pop5 (from Pyrococcus furiosus) interact in a 1:1 stoichiometry forming a 78 kDa heterotetramer (two copies each of Pop5 and RPP30); the binding surface on RPP30 was mapped by NMR chemical shift perturbations, and complex formation confirmed by ITC, light scattering, and size exclusion chromatography.","method":"NMR spectroscopy (backbone assignments and chemical shift perturbations), isothermal titration calorimetry (ITC), size exclusion chromatography, light scattering","journal":"Archaea (Vancouver, B.C.)","confidence":"High","confidence_rationale":"Tier 1 / Moderate — multiple orthogonal biophysical methods (NMR, ITC, SEC, light scattering) in a single rigorous study characterizing the interaction","pmids":["22162665"],"is_preprint":false},{"year":2015,"finding":"The PhoPop5-PhoRpp30 heterotetramer [PhoRpp30-(PhoPop5)2-PhoRpp30] strongly interacts with the stem-loop SL3 of RNase P RNA (PhopRNA); PhoRpp30 alone has little affinity for SL3, but assists PhoPop5 in attaining a functionally active conformation by shielding hydrophobic surfaces; the C-terminal helix (α4) of PhoPop5 acts as the molecular recognition element for SL3.","method":"Surface plasmon resonance (SPR), site-directed mutagenesis of PhoPop5, gel filtration chromatography","journal":"Journal of biochemistry","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — SPR with mutagenesis and gel filtration, single lab, multiple orthogonal methods","pmids":["26152732"],"is_preprint":false},{"year":2015,"finding":"Crystal structures of Thermococcus kodakarensis TkoRpp30 alone and in complex with TkoPop5 revealed that TkoRpp30 adopts a TIM barrel fold and TkoPop5 adopts an RRM-like fold, consistent with Pyrococcus horikoshii counterparts; reconstitution showed that TkoPop5 and TkoRpp30 are functionally interchangeable with their P. horikoshii homologs in pre-tRNA cleavage.","method":"X-ray crystallography, in vitro RNase P reconstitution and pre-tRNA cleavage assay","journal":"Bioscience, biotechnology, and biochemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure plus functional reconstitution assay, single lab but two orthogonal methods","pmids":["25704799"],"is_preprint":false},{"year":2006,"finding":"Dictyostelium discoideum DRpp30 (a Rpp30/Rpp1 homolog with predicted TIM-barrel fold) is a protein subunit of the D. discoideum RNase P holoenzyme; it co-purifies with RNase P active fractions and can bind D. discoideum RNase P RNA and tRNA transcripts in vitro.","method":"Heterologous expression, immunochemical co-purification with RNase P active fractions, in vitro RNA binding assay, homology modeling","journal":"Biochimie","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — co-purification and in vitro RNA binding, single lab, two orthogonal methods","pmids":["17207566"],"is_preprint":false}],"current_model":"RPP30 (and its archaeal/protist orthologs) is a protein subunit of the RNase P ribonucleoprotein complex that forms a tight heterotetramer with Pop5 (two copies each) via a mapped binding surface adopting a TIM-barrel fold; within this tetramer Pop5 mediates RNA recognition of the C-domain stem-loop of RNase P RNA while RPP30 stabilizes Pop5 in a catalytically active conformation, together activating pre-tRNA 5′ cleavage activity."},"narrative":{"mechanistic_narrative":"RPP30 is a protein subunit of the RNase P ribonucleoprotein complex that activates the catalytic RNA responsible for 5′ maturation of pre-tRNA [PMID:20139629, PMID:17207566]. Across archaeal and protist orthologs, RPP30 assembles with Pop5 into a tight heterotetramer with 1:1 stoichiometry (two copies each of RPP30 and Pop5), with the RPP30 binding surface mapped directly to Pop5 [PMID:22162665]. RPP30 adopts a TIM-barrel fold while Pop5 adopts an RRM-like fold [PMID:25704799]. Functionally, RPP30 and Pop5 act on the C-domain of RNase P RNA, equivalent to the bacterial C5 protein, to activate pre-tRNA cleavage [PMID:20139629]; within the heterotetramer Pop5 recognizes the SL3 stem-loop of RNase P RNA through its C-terminal α4 helix, while RPP30 itself has little affinity for SL3 and instead assists Pop5 in attaining a catalytically active conformation by shielding hydrophobic surfaces [PMID:26152732]. Beyond this RNase P assembly role, no additional cellular functions of RPP30 have been characterized in the available corpus.","teleology":[{"year":2006,"claim":"Establishing that a Rpp30/Rpp1 homolog is a genuine subunit of the eukaryotic-type RNase P holoenzyme rather than a peripheral factor was needed to extend the RNase P protein model beyond bacteria.","evidence":"Immunochemical co-purification of Dictyostelium DRpp30 with RNase P active fractions plus in vitro RNA binding and homology modeling","pmids":["17207566"],"confidence":"Medium","gaps":["Does not define stoichiometry or the precise RNA target","RNA binding shown in vitro without functional cleavage requirement","No structural data"]},{"year":2010,"claim":"Resolved which RNase P proteins act on which RNA domain, showing RPP30 and Pop5 functionally substitute for the bacterial C5 protein in activating the catalytic C-domain.","evidence":"Chimeric RNase P RNA reconstitution with exchanged C-/S-domains and pre-tRNA cleavage assays in an archaeal system","pmids":["20139629"],"confidence":"Medium","gaps":["Does not resolve the physical RPP30–Pop5 architecture","Mechanism of conformational activation not addressed","Single lab, single study"]},{"year":2011,"claim":"Defined the physical architecture of the RPP30–Pop5 module, fixing its stoichiometry as a heterotetramer and mapping the RPP30 binding surface.","evidence":"NMR chemical shift perturbation mapping with orthogonal ITC, SEC, and light scattering on Pyrococcus furiosus proteins","pmids":["22162665"],"confidence":"High","gaps":["Does not show how the tetramer engages RNase P RNA","No catalytic readout linking the interface to activity"]},{"year":2015,"claim":"Established the division of labor within the heterotetramer: Pop5 recognizes RNase P RNA stem-loop SL3 via its α4 helix while RPP30 acts as a conformational chaperone for Pop5.","evidence":"SPR binding, site-directed mutagenesis of Pop5, and gel filtration in the Pyrococcus horikoshii system","pmids":["26152732"],"confidence":"Medium","gaps":["RPP30's direct contribution to RNA contact remains minimal/undefined","Conformational shielding inferred rather than structurally captured","Single lab"]},{"year":2015,"claim":"Provided atomic-resolution confirmation of the folds, defining RPP30 as a TIM-barrel and Pop5 as RRM-like, and demonstrated cross-species functional interchangeability.","evidence":"X-ray crystallography of TkoRpp30 alone and with TkoPop5 plus in vitro RNase P reconstitution and pre-tRNA cleavage","pmids":["25704799"],"confidence":"High","gaps":["No structure of the full RNase P holoenzyme with RNA","Catalytic mechanism of cleavage not resolved at this interface"]},{"year":null,"claim":"How the RPP30–Pop5 module is integrated into the complete human RNase P holoenzyme and any roles of RPP30 outside tRNA processing remain uncharacterized in this corpus.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No human holoenzyme structure in the corpus","No cellular or physiological phenotype data","No disease association established"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[4]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,2]}],"localization":[],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[0,3]}],"complexes":["RNase P"],"partners":["POP5"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P78346","full_name":"Ribonuclease P protein subunit p30","aliases":["RNase P subunit 2"],"length_aa":268,"mass_kda":29.3,"function":"Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:9037013, PubMed:9630247). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465)","subcellular_location":"Nucleus, nucleolus","url":"https://www.uniprot.org/uniprotkb/P78346/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/RPP30","classification":"Common Essential","n_dependent_lines":1112,"n_total_lines":1208,"dependency_fraction":0.9205298013245033},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000148688","cell_line_id":"CID001934","localizations":[{"compartment":"nucleolus_gc","grade":3},{"compartment":"nuclear_punctae","grade":1},{"compartment":"nucleoplasm","grade":1}],"interactors":[{"gene":"RPP40","stoichiometry":10.0},{"gene":"POP7","stoichiometry":10.0},{"gene":"TRIM39-RPP21;RPP21","stoichiometry":10.0},{"gene":"POP1","stoichiometry":10.0},{"gene":"RPP14","stoichiometry":4.0},{"gene":"POP4","stoichiometry":4.0},{"gene":"VWA8","stoichiometry":4.0},{"gene":"RPP25L","stoichiometry":4.0},{"gene":"NPM1","stoichiometry":0.2},{"gene":"WDR44","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID001934","total_profiled":1310},"omim":[{"mim_id":"606117","title":"RIBONUCLEASE P/MRP SUBUNIT p40; RPP40","url":"https://www.omim.org/entry/606117"},{"mim_id":"606116","title":"RIBONUCLEASE P/MRP SUBUNIT p38; RPP38","url":"https://www.omim.org/entry/606116"},{"mim_id":"606115","title":"RIBONUCLEASE P/MRP SUBUNIT p30; RPP30","url":"https://www.omim.org/entry/606115"},{"mim_id":"606114","title":"POP4 HOMOLOG, RIBONUCLEASE P/MRP SUBUNIT; POP4","url":"https://www.omim.org/entry/606114"},{"mim_id":"606113","title":"POP7 HOMOLOG, RIBONUCLEASE P/MRP SUBUNIT; POP7","url":"https://www.omim.org/entry/606113"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Nucleoli","reliability":"Approved"},{"location":"Microtubule ends","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/RPP30"},"hgnc":{"alias_symbol":["TSG15"],"prev_symbol":[]},"alphafold":{"accession":"P78346","domains":[{"cath_id":"3.20.20.140","chopping":"6-237","consensus_level":"medium","plddt":90.3406,"start":6,"end":237}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P78346","model_url":"https://alphafold.ebi.ac.uk/files/AF-P78346-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P78346-F1-predicted_aligned_error_v6.png","plddt_mean":84.81},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=RPP30","jax_strain_url":"https://www.jax.org/strain/search?query=RPP30"},"sequence":{"accession":"P78346","fasta_url":"https://rest.uniprot.org/uniprotkb/P78346.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P78346/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P78346"}},"corpus_meta":[{"pmid":"33932077","id":"PMC_33932077","title":"The rice RNase P protein subunit Rpp30 confers broad-spectrum resistance to fungal and bacterial pathogens.","date":"2021","source":"Plant biotechnology journal","url":"https://pubmed.ncbi.nlm.nih.gov/33932077","citation_count":24,"is_preprint":false},{"pmid":"29483619","id":"PMC_29483619","title":"Normalization of cell associated antiretroviral drug concentrations with a novel RPP30 droplet digital PCR assay.","date":"2018","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/29483619","citation_count":24,"is_preprint":false},{"pmid":"20139629","id":"PMC_20139629","title":"Archaeal homologs of human RNase P protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 work on distinct functional domains of the RNA subunit.","date":"2010","source":"Bioscience, biotechnology, and biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/20139629","citation_count":18,"is_preprint":false},{"pmid":"32702667","id":"PMC_32702667","title":"RPP30, a transcriptional regulator, is a potential pathogenic factor in glioblastoma.","date":"2020","source":"Aging","url":"https://pubmed.ncbi.nlm.nih.gov/32702667","citation_count":9,"is_preprint":false},{"pmid":"22162665","id":"PMC_22162665","title":"Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5.","date":"2011","source":"Archaea (Vancouver, B.C.)","url":"https://pubmed.ncbi.nlm.nih.gov/22162665","citation_count":7,"is_preprint":false},{"pmid":"26152732","id":"PMC_26152732","title":"Functional implication of archaeal homologues of human RNase P protein pair Pop5 and Rpp30.","date":"2015","source":"Journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/26152732","citation_count":5,"is_preprint":false},{"pmid":"17207566","id":"PMC_17207566","title":"A 40.7 kDa Rpp30/Rpp1 homologue is a protein subunit of Dictyostelium discoideum RNase P holoenzyme.","date":"2006","source":"Biochimie","url":"https://pubmed.ncbi.nlm.nih.gov/17207566","citation_count":4,"is_preprint":false},{"pmid":"25704799","id":"PMC_25704799","title":"On archaeal homologs of the human RNase P proteins Pop5 and Rpp30 in the hyperthermophilic archaeon Thermococcus kodakarensis.","date":"2015","source":"Bioscience, biotechnology, and biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/25704799","citation_count":4,"is_preprint":false},{"pmid":"41133709","id":"PMC_41133709","title":"Validation on the First-Tier Fully Automated High-Throughput SMN1, SMN2, TREC, and RPP30 Quantification by Quadruplex Droplet Digital PCR for Newborn Screening for Spinal Muscular Atrophy and Severe Combined Immunodeficiency.","date":"2025","source":"International journal of neonatal screening","url":"https://pubmed.ncbi.nlm.nih.gov/41133709","citation_count":0,"is_preprint":false},{"pmid":"41873718","id":"PMC_41873718","title":"Dual regulation of RNase P subunit Rpp30 by an acetyltransferase and E3 ligase in rice immunity.","date":"2026","source":"Plant physiology","url":"https://pubmed.ncbi.nlm.nih.gov/41873718","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.06.11.659223","title":"Digital PCR detection of  <i>Mycobacterium tuberculosis</i>  and HIV-1 co-localization in spinal tuberculosis biopsies","date":"2025-06-13","source":"bioRxiv","url":"https://doi.org/10.1101/2025.06.11.659223","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7825,"output_tokens":1406,"usd":0.022283,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8057,"output_tokens":2034,"usd":0.045567,"stage2_stop_reason":"end_turn"},"total_usd":0.06785,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"Archaeal RNase P proteins PhoPop5 and PhoRpp30 function equivalently to the E. coli C5 protein in activating the C-domain of RNase P RNA (PhopRNA), while PhoRpp21 and PhoRpp29 are implicated in stabilization of the S-domain; established using chimeric RNase P RNAs with exchanged C- and S-domains and pre-tRNA cleavage assays.\",\n      \"method\": \"Chimeric RNA reconstitution assay, pre-tRNA cleavage activity assay\",\n      \"journal\": \"Bioscience, biotechnology, and biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro reconstitution with chimeric RNAs, single lab, single study\",\n      \"pmids\": [\"20139629\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"Archaeal RPP30 and Pop5 (from Pyrococcus furiosus) interact in a 1:1 stoichiometry forming a 78 kDa heterotetramer (two copies each of Pop5 and RPP30); the binding surface on RPP30 was mapped by NMR chemical shift perturbations, and complex formation confirmed by ITC, light scattering, and size exclusion chromatography.\",\n      \"method\": \"NMR spectroscopy (backbone assignments and chemical shift perturbations), isothermal titration calorimetry (ITC), size exclusion chromatography, light scattering\",\n      \"journal\": \"Archaea (Vancouver, B.C.)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — multiple orthogonal biophysical methods (NMR, ITC, SEC, light scattering) in a single rigorous study characterizing the interaction\",\n      \"pmids\": [\"22162665\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"The PhoPop5-PhoRpp30 heterotetramer [PhoRpp30-(PhoPop5)2-PhoRpp30] strongly interacts with the stem-loop SL3 of RNase P RNA (PhopRNA); PhoRpp30 alone has little affinity for SL3, but assists PhoPop5 in attaining a functionally active conformation by shielding hydrophobic surfaces; the C-terminal helix (α4) of PhoPop5 acts as the molecular recognition element for SL3.\",\n      \"method\": \"Surface plasmon resonance (SPR), site-directed mutagenesis of PhoPop5, gel filtration chromatography\",\n      \"journal\": \"Journal of biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — SPR with mutagenesis and gel filtration, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"26152732\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Crystal structures of Thermococcus kodakarensis TkoRpp30 alone and in complex with TkoPop5 revealed that TkoRpp30 adopts a TIM barrel fold and TkoPop5 adopts an RRM-like fold, consistent with Pyrococcus horikoshii counterparts; reconstitution showed that TkoPop5 and TkoRpp30 are functionally interchangeable with their P. horikoshii homologs in pre-tRNA cleavage.\",\n      \"method\": \"X-ray crystallography, in vitro RNase P reconstitution and pre-tRNA cleavage assay\",\n      \"journal\": \"Bioscience, biotechnology, and biochemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure plus functional reconstitution assay, single lab but two orthogonal methods\",\n      \"pmids\": [\"25704799\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"Dictyostelium discoideum DRpp30 (a Rpp30/Rpp1 homolog with predicted TIM-barrel fold) is a protein subunit of the D. discoideum RNase P holoenzyme; it co-purifies with RNase P active fractions and can bind D. discoideum RNase P RNA and tRNA transcripts in vitro.\",\n      \"method\": \"Heterologous expression, immunochemical co-purification with RNase P active fractions, in vitro RNA binding assay, homology modeling\",\n      \"journal\": \"Biochimie\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — co-purification and in vitro RNA binding, single lab, two orthogonal methods\",\n      \"pmids\": [\"17207566\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"RPP30 (and its archaeal/protist orthologs) is a protein subunit of the RNase P ribonucleoprotein complex that forms a tight heterotetramer with Pop5 (two copies each) via a mapped binding surface adopting a TIM-barrel fold; within this tetramer Pop5 mediates RNA recognition of the C-domain stem-loop of RNase P RNA while RPP30 stabilizes Pop5 in a catalytically active conformation, together activating pre-tRNA 5′ cleavage activity.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RPP30 is a protein subunit of the RNase P ribonucleoprotein complex that activates the catalytic RNA responsible for 5′ maturation of pre-tRNA [#0, #4]. Across archaeal and protist orthologs, RPP30 assembles with Pop5 into a tight heterotetramer with 1:1 stoichiometry (two copies each of RPP30 and Pop5), with the RPP30 binding surface mapped directly to Pop5 [#1]. RPP30 adopts a TIM-barrel fold while Pop5 adopts an RRM-like fold [#3]. Functionally, RPP30 and Pop5 act on the C-domain of RNase P RNA, equivalent to the bacterial C5 protein, to activate pre-tRNA cleavage [#0]; within the heterotetramer Pop5 recognizes the SL3 stem-loop of RNase P RNA through its C-terminal α4 helix, while RPP30 itself has little affinity for SL3 and instead assists Pop5 in attaining a catalytically active conformation by shielding hydrophobic surfaces [#2]. Beyond this RNase P assembly role, no additional cellular functions of RPP30 have been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Establishing that a Rpp30/Rpp1 homolog is a genuine subunit of the eukaryotic-type RNase P holoenzyme rather than a peripheral factor was needed to extend the RNase P protein model beyond bacteria.\",\n      \"evidence\": \"Immunochemical co-purification of Dictyostelium DRpp30 with RNase P active fractions plus in vitro RNA binding and homology modeling\",\n      \"pmids\": [\"17207566\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Does not define stoichiometry or the precise RNA target\", \"RNA binding shown in vitro without functional cleavage requirement\", \"No structural data\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Resolved which RNase P proteins act on which RNA domain, showing RPP30 and Pop5 functionally substitute for the bacterial C5 protein in activating the catalytic C-domain.\",\n      \"evidence\": \"Chimeric RNase P RNA reconstitution with exchanged C-/S-domains and pre-tRNA cleavage assays in an archaeal system\",\n      \"pmids\": [\"20139629\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Does not resolve the physical RPP30–Pop5 architecture\", \"Mechanism of conformational activation not addressed\", \"Single lab, single study\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Defined the physical architecture of the RPP30–Pop5 module, fixing its stoichiometry as a heterotetramer and mapping the RPP30 binding surface.\",\n      \"evidence\": \"NMR chemical shift perturbation mapping with orthogonal ITC, SEC, and light scattering on Pyrococcus furiosus proteins\",\n      \"pmids\": [\"22162665\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"Does not show how the tetramer engages RNase P RNA\", \"No catalytic readout linking the interface to activity\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Established the division of labor within the heterotetramer: Pop5 recognizes RNase P RNA stem-loop SL3 via its α4 helix while RPP30 acts as a conformational chaperone for Pop5.\",\n      \"evidence\": \"SPR binding, site-directed mutagenesis of Pop5, and gel filtration in the Pyrococcus horikoshii system\",\n      \"pmids\": [\"26152732\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"RPP30's direct contribution to RNA contact remains minimal/undefined\", \"Conformational shielding inferred rather than structurally captured\", \"Single lab\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Provided atomic-resolution confirmation of the folds, defining RPP30 as a TIM-barrel and Pop5 as RRM-like, and demonstrated cross-species functional interchangeability.\",\n      \"evidence\": \"X-ray crystallography of TkoRpp30 alone and with TkoPop5 plus in vitro RNase P reconstitution and pre-tRNA cleavage\",\n      \"pmids\": [\"25704799\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"No structure of the full RNase P holoenzyme with RNA\", \"Catalytic mechanism of cleavage not resolved at this interface\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How the RPP30–Pop5 module is integrated into the complete human RNase P holoenzyme and any roles of RPP30 outside tRNA processing remain uncharacterized in this corpus.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\"No human holoenzyme structure in the corpus\", \"No cellular or physiological phenotype data\", \"No disease association established\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [4]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"complexes\": [\"RNase P\"],\n    \"partners\": [\"POP5\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"tie","faith_supported":4,"faith_total":4,"faith_pct":100.0}}