{"gene":"TG_239760","gene_symbol":"RPL22","run_date":"2026-09-08T12:58:24","timeline":{"discoveries":[{"year":2010,"finding":"RPL22 protein levels decline more slowly than RPS13 upon conditional knockdown of rps13, indicating that ribosomal protein abundance is differentially regulated and that RPL22 expression is partially buffered from depletion of the small subunit protein RPS13.","method":"Conditional tetracycline-repressor-based knockdown of rps13 combined with Myc-tagged RPL22 protein quantitation in Toxoplasma gondii","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — clean conditional KO system with protein-level readout for RPL22, but single lab, single method, and RPL22 is a secondary observation in a paper focused on RPS13","pmids":["21124925"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"In Toxoplasma gondii, RPL22 is a ribosomal large subunit protein whose abundance decreases more slowly than the small subunit protein RPS13 upon ribosomal stress, suggesting differential buffering of large versus small subunit protein levels; no direct enzymatic, structural, or binding-partner mechanism has been established for RPL22 itself."},"narrative":{"mechanistic_narrative":"In Toxoplasma gondii, RPL22 is a large ribosomal subunit protein whose abundance is differentially regulated relative to the small subunit protein RPS13: upon conditional knockdown of rps13, RPL22 protein levels decline more slowly than RPS13, indicating that RPL22 expression is partially buffered from small-subunit depletion [PMID:21124925]. Beyond this differential-stability observation [PMID:21124925], no direct enzymatic, structural, or binding-partner mechanism for RPL22 has been characterized in the available corpus.","teleology":[{"year":2010,"claim":"It was unknown whether large- and small-subunit ribosomal protein levels are co-regulated; measuring RPL22 during RPS13 depletion showed that RPL22 decays more slowly, establishing that ribosomal protein abundance is differentially buffered across subunits.","evidence":"Conditional tetracycline-repressor knockdown of rps13 with Myc-tagged RPL22 protein quantitation in Toxoplasma gondii","pmids":["21124925"],"confidence":"Medium","gaps":["No mechanism for the differential stability of RPL22 versus RPS13 is defined","No direct enzymatic, structural, or binding-partner activity for RPL22 established","RPL22 was a secondary observation in a study focused on RPS13"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The molecular function, ribosome incorporation, and any regulatory or extra-ribosomal role of Toxoplasma RPL22 remain uncharacterized.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural or biochemical characterization of RPL22 within the ribosome","No binding partners or substrates identified","Mechanism underlying differential buffering versus RPS13 unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["large ribosomal subunit"],"partners":[],"other_free_text":["RPL22 protein abundance declines more slowly than the small subunit protein RPS13 upon rps13 knockdown, indicating differential buffering of large versus small subunit protein levels [#0]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"21124925","id":"PMC_21124925","title":"T. gondii RP promoters & knockdown reveal molecular pathways associated with proliferation and cell-cycle arrest.","date":"2010","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/21124925","citation_count":22,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3138,"output_tokens":364,"usd":0.007437,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":4957,"output_tokens":999,"usd":0.02488,"stage2_stop_reason":"end_turn"},"total_usd":0.032317,"stage1_batch_id":"msgbatch_01TEPNZ4MCzJ7xtsNwosiDRk","stage2_batch_id":"msgbatch_01FQShM7n1sfCr4pWTDShmki","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"RPL22 protein levels decline more slowly than RPS13 upon conditional knockdown of rps13, indicating that ribosomal protein abundance is differentially regulated and that RPL22 expression is partially buffered from depletion of the small subunit protein RPS13.\",\n      \"method\": \"Conditional tetracycline-repressor-based knockdown of rps13 combined with Myc-tagged RPL22 protein quantitation in Toxoplasma gondii\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean conditional KO system with protein-level readout for RPL22, but single lab, single method, and RPL22 is a secondary observation in a paper focused on RPS13\",\n      \"pmids\": [\"21124925\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"In Toxoplasma gondii, RPL22 is a ribosomal large subunit protein whose abundance decreases more slowly than the small subunit protein RPS13 upon ribosomal stress, suggesting differential buffering of large versus small subunit protein levels; no direct enzymatic, structural, or binding-partner mechanism has been established for RPL22 itself.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"In Toxoplasma gondii, RPL22 is a large ribosomal subunit protein whose abundance is differentially regulated relative to the small subunit protein RPS13: upon conditional knockdown of rps13, RPL22 protein levels decline more slowly than RPS13, indicating that RPL22 expression is partially buffered from small-subunit depletion [#0]. Beyond this differential-stability observation [#0], no direct enzymatic, structural, or binding-partner mechanism for RPL22 has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"It was unknown whether large- and small-subunit ribosomal protein levels are co-regulated; measuring RPL22 during RPS13 depletion showed that RPL22 decays more slowly, establishing that ribosomal protein abundance is differentially buffered across subunits.\",\n      \"evidence\": \"Conditional tetracycline-repressor knockdown of rps13 with Myc-tagged RPL22 protein quantitation in Toxoplasma gondii\",\n      \"pmids\": [\"21124925\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No mechanism for the differential stability of RPL22 versus RPS13 is defined\",\n        \"No direct enzymatic, structural, or binding-partner activity for RPL22 established\",\n        \"RPL22 was a secondary observation in a study focused on RPS13\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The molecular function, ribosome incorporation, and any regulatory or extra-ribosomal role of Toxoplasma RPL22 remain uncharacterized.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural or biochemical characterization of RPL22 within the ribosome\",\n        \"No binding partners or substrates identified\",\n        \"Mechanism underlying differential buffering versus RPS13 unknown\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003735\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [],\n    \"pathway\": [],\n    \"complexes\": [\"large ribosomal subunit\"],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"RPL22 protein abundance declines more slowly than the small subunit protein RPS13 upon rps13 knockdown, indicating differential buffering of large versus small subunit protein levels [#0]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_239760","name":"RPL22","product":"ribosomal protein RPL22","uniprot_acc":"A0A125YT46","chromosome":"TGME49_chrVI","start_pos":901019},{"strain":"GT1","gene_id":"TGGT1_239760","name":null,"product":"ribosomal protein RPL22","uniprot_acc":null,"chromosome":"TGGT1_chrVI","start_pos":893982},{"strain":"RH88","gene_id":"TGRH88_031200","name":null,"product":"ribosomal protein RPL22","uniprot_acc":null,"chromosome":"CM023087","start_pos":2800659},{"strain":"VEG","gene_id":"TGVEG_239760","name":null,"product":"ribosomal protein RPL22","uniprot_acc":"B9PNF3","chromosome":"TGVEG_chrVI","start_pos":914252}]}