{"gene":"TG_232150","gene_symbol":"IMC32","run_date":"2026-09-08T15:31:29+00:00","timeline":{"discoveries":[{"year":2021,"finding":"IMC32 is a novel Toxoplasma gondii IMC protein that localizes to the body portion of the IMC and is recruited to developing daughter buds early during endodyogeny; conditional depletion causes complete collapse of the IMC and is lethal to the parasite, establishing IMC32 as essential for parasite replication.","method":"Conditional knockdown (auxin-inducible or analogous degron system), fluorescence microscopy localization","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Moderate — conditional depletion with defined lethal cellular phenotype (IMC collapse), direct localization imaging, single lab with multiple orthogonal methods","pmids":["33593973"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Localization of IMC32 to the IMC is dependent on an N-terminal palmitoylation site; mutation of this site disrupts membrane association.","method":"Deletion/mutagenesis analyses and functional complementation","journal":"mBio","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — site-directed mutagenesis with functional complementation, single lab","pmids":["33593973"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Localization of IMC32 also requires C-terminal coiled-coil domains; two conserved regions within these domains play critical roles in protein function during replication, as shown by deletion analyses and functional complementation.","method":"Deletion analyses, functional complementation assays","journal":"mBio","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — deletion mapping and functional complementation, single lab with multiple constructs","pmids":["33593973"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2023,"finding":"IMC43 regulates the localization of IMC32 at specific stages of endodyogeny; depletion of IMC43 mislocalizes IMC32, demonstrating that IMC43 acts upstream of IMC32 in daughter bud assembly.","method":"Auxin-inducible degron depletion of IMC43, fluorescence microscopy of IMC32 localization","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Moderate — conditional depletion epistasis with direct localization readout, single lab, two orthogonal methods (degron + imaging)","pmids":["37782662"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2023,"finding":"IMC43 physically interacts with IMC32; this interaction is mediated by the essential C-terminal domain of IMC43 and is sufficient for binding to IMC32 as shown by pairwise yeast two-hybrid assays. Together, IMC43 and IMC32 form an essential daughter bud assembly complex.","method":"TurboID proximity labeling, yeast two-hybrid screen, pairwise yeast two-hybrid assays","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal proximity labeling plus yeast two-hybrid with domain mapping, single lab, multiple orthogonal methods","pmids":["37782662"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"BCC0 is identified as a third member of the IMC32-IMC43 essential daughter bud assembly complex; BCC0's localization to daughter buds depends on both IMC32 and IMC43, and its essential domain (residues 701–877) directly binds the coiled-coil region of IMC32, as shown by pairwise yeast two-hybrid assays.","method":"Proximity labeling (IMC32 as bait), yeast two-hybrid screen, pairwise yeast two-hybrid, deletion analyses and functional complementation, fluorescence microscopy","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Moderate — proximity labeling plus yeast two-hybrid domain mapping plus functional complementation, single lab, multiple orthogonal methods","pmids":["39024411"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"A model for complex assembly was supported experimentally in which an IMC32-BCC0 subcomplex initially recruits to nascent buds via palmitoylation of IMC32, and is subsequently locked into the scaffold by IMC32 binding to IMC43 once bud elongation begins; BCC0 and IMC43 do not directly interact with each other.","method":"Epistasis via sequential depletion/localization experiments, pairwise yeast two-hybrid (negative result for BCC0-IMC43 direct interaction), deletion and complementation analyses","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — pathway order inferred from localization epistasis and negative yeast two-hybrid, single lab, model supported but not fully reconstituted in vitro","pmids":["39024411"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"IMC32 is an essential Toxoplasma gondii IMC protein that anchors to the nascent daughter bud membrane via N-terminal palmitoylation and uses its C-terminal coiled-coil domains to physically interact with IMC43 and BCC0, forming a tripartite essential daughter bud assembly complex that lays the structural foundation of the daughter IMC scaffold during endodyogeny; loss of IMC32 causes complete IMC collapse and parasite death."},"narrative":{"mechanistic_narrative":"IMC32 is an essential Toxoplasma gondii inner membrane complex (IMC) protein that lays the structural foundation of the daughter bud scaffold during endodyogeny [PMID:33593973]. It localizes to the body portion of the IMC and is recruited to developing daughter buds early in replication; conditional depletion causes complete collapse of the IMC and is lethal [PMID:33593973]. IMC32 anchors to the nascent bud membrane through an N-terminal palmitoylation site, whose mutation disrupts membrane association [PMID:33593973], while its C-terminal coiled-coil domains — containing two conserved functionally critical regions — are required both for correct localization and for its role in replication [PMID:33593973]. Through these coiled-coil domains IMC32 physically binds IMC43 and BCC0, forming a tripartite essential daughter bud assembly complex [PMID:37782662, PMID:39024411]. IMC43 acts upstream, controlling IMC32 localization at specific stages of endodyogeny [PMID:37782662], and BCC0's own recruitment depends on both IMC32 and IMC43, with its essential domain (residues 701–877) directly binding the IMC32 coiled-coil [PMID:39024411]. Assembly proceeds by an IMC32–BCC0 subcomplex recruiting to nascent buds via IMC32 palmitoylation, which is subsequently locked into the scaffold by IMC32–IMC43 binding as bud elongation begins; BCC0 and IMC43 do not directly interact [PMID:39024411].","teleology":[{"year":2021,"claim":"Establishing whether IMC32 is a functionally important IMC component addressed whether it contributes structurally to daughter bud formation, and showed it is essential for the integrity of the IMC scaffold.","evidence":"Conditional degron depletion with fluorescence localization in T. gondii, revealing early daughter bud recruitment and lethal IMC collapse upon loss","pmids":["33593973"],"confidence":"High","gaps":["Molecular partners not yet identified","Mechanism by which IMC collapse leads to death not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Dissecting which sequence features drive IMC32 membrane targeting versus function distinguished a lipid-anchoring role from a protein-interaction role, defining a bipartite domain architecture.","evidence":"Site-directed mutagenesis of the N-terminal palmitoylation site and deletion mapping of C-terminal coiled-coil regions with functional complementation in T. gondii","pmids":["33593973"],"confidence":"High","gaps":["Identity of binding partners engaged by the coiled-coil domains unknown at this stage","Palmitoylating enzyme not identified"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2023,"claim":"Determining what governs IMC32 stage-specific localization and what it binds revealed IMC43 as an upstream regulator and direct partner, defining a two-component essential complex.","evidence":"Auxin-inducible degron depletion of IMC43 showing IMC32 mislocalization, plus TurboID and pairwise yeast two-hybrid domain mapping of a direct IMC43–IMC32 interaction in T. gondii","pmids":["37782662"],"confidence":"High","gaps":["Interaction not reconstituted with purified proteins","Whether additional components complete the complex unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"Identifying a third complex member and mapping the order of assembly addressed how the daughter bud scaffold nucleates, establishing a tripartite complex and a stepwise recruitment logic.","evidence":"Proximity labeling and yeast two-hybrid identifying BCC0 binding the IMC32 coiled-coil (residues 701–877), plus sequential depletion/localization epistasis and a negative BCC0–IMC43 yeast two-hybrid in T. gondii","pmids":["39024411"],"confidence":"High","gaps":["Assembly order inferred from localization epistasis, not fully reconstituted in vitro","Downstream scaffold components recruited after this complex not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"How the IMC32-anchored complex is connected to downstream IMC alveolar/cytoskeletal architecture and what enzymes control IMC32 palmitoylation dynamics remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["Palmitoyltransferase acting on IMC32 not identified","Structural basis of coiled-coil-mediated binding not resolved","Link to mature IMC scaffold assembly uncharacterized"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["IMC32-IMC43-BCC0 essential daughter bud assembly complex"],"partners":["IMC43","BCC0"],"other_free_text":["N-terminal palmitoylation anchors IMC32 to the nascent daughter bud membrane [#1]","C-terminal coiled-coil domains mediate binding to both IMC43 and BCC0 [#2, #4, #5]","IMC43 acts upstream of IMC32 in daughter bud assembly [#3]","BCC0-IMC43 do not directly interact; IMC32 bridges the complex [#6]","Conditional depletion causes complete IMC collapse and parasite death [#0]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"33593973","id":"PMC_33593973","title":"Identification and Molecular Dissection of IMC32, a Conserved Toxoplasma Inner Membrane Complex Protein That Is Essential for Parasite Replication.","date":"2021","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/33593973","citation_count":25,"is_preprint":false},{"pmid":"37782662","id":"PMC_37782662","title":"Identification of IMC43, a novel IMC protein that collaborates with IMC32 to form an essential daughter bud assembly complex in Toxoplasma gondii.","date":"2023","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/37782662","citation_count":11,"is_preprint":false},{"pmid":"39024411","id":"PMC_39024411","title":"BCC0 collaborates with IMC32 and IMC43 to form the Toxoplasma gondii essential daughter bud assembly complex.","date":"2024","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/39024411","citation_count":7,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3988,"output_tokens":1725,"usd":0.018919,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6972,"output_tokens":2373,"usd":0.047093,"stage2_stop_reason":"end_turn"},"total_usd":0.0,"stage1_batch_id":"msgbatch_01WgHz6kceqm573AGLyz57at","stage2_batch_id":"msgbatch_01LK4wDYj5zYquahv7gi9893","note":"batch pricing = 50% of standard","skipped":true},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"IMC32 is a novel Toxoplasma gondii IMC protein that localizes to the body portion of the IMC and is recruited to developing daughter buds early during endodyogeny; conditional depletion causes complete collapse of the IMC and is lethal to the parasite, establishing IMC32 as essential for parasite replication.\",\n      \"method\": \"Conditional knockdown (auxin-inducible or analogous degron system), fluorescence microscopy localization\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — conditional depletion with defined lethal cellular phenotype (IMC collapse), direct localization imaging, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"33593973\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Localization of IMC32 to the IMC is dependent on an N-terminal palmitoylation site; mutation of this site disrupts membrane association.\",\n      \"method\": \"Deletion/mutagenesis analyses and functional complementation\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — site-directed mutagenesis with functional complementation, single lab\",\n      \"pmids\": [\"33593973\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Localization of IMC32 also requires C-terminal coiled-coil domains; two conserved regions within these domains play critical roles in protein function during replication, as shown by deletion analyses and functional complementation.\",\n      \"method\": \"Deletion analyses, functional complementation assays\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — deletion mapping and functional complementation, single lab with multiple constructs\",\n      \"pmids\": [\"33593973\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"IMC43 regulates the localization of IMC32 at specific stages of endodyogeny; depletion of IMC43 mislocalizes IMC32, demonstrating that IMC43 acts upstream of IMC32 in daughter bud assembly.\",\n      \"method\": \"Auxin-inducible degron depletion of IMC43, fluorescence microscopy of IMC32 localization\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — conditional depletion epistasis with direct localization readout, single lab, two orthogonal methods (degron + imaging)\",\n      \"pmids\": [\"37782662\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"IMC43 physically interacts with IMC32; this interaction is mediated by the essential C-terminal domain of IMC43 and is sufficient for binding to IMC32 as shown by pairwise yeast two-hybrid assays. Together, IMC43 and IMC32 form an essential daughter bud assembly complex.\",\n      \"method\": \"TurboID proximity labeling, yeast two-hybrid screen, pairwise yeast two-hybrid assays\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal proximity labeling plus yeast two-hybrid with domain mapping, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"37782662\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"BCC0 is identified as a third member of the IMC32-IMC43 essential daughter bud assembly complex; BCC0's localization to daughter buds depends on both IMC32 and IMC43, and its essential domain (residues 701–877) directly binds the coiled-coil region of IMC32, as shown by pairwise yeast two-hybrid assays.\",\n      \"method\": \"Proximity labeling (IMC32 as bait), yeast two-hybrid screen, pairwise yeast two-hybrid, deletion analyses and functional complementation, fluorescence microscopy\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — proximity labeling plus yeast two-hybrid domain mapping plus functional complementation, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"39024411\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"A model for complex assembly was supported experimentally in which an IMC32-BCC0 subcomplex initially recruits to nascent buds via palmitoylation of IMC32, and is subsequently locked into the scaffold by IMC32 binding to IMC43 once bud elongation begins; BCC0 and IMC43 do not directly interact with each other.\",\n      \"method\": \"Epistasis via sequential depletion/localization experiments, pairwise yeast two-hybrid (negative result for BCC0-IMC43 direct interaction), deletion and complementation analyses\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — pathway order inferred from localization epistasis and negative yeast two-hybrid, single lab, model supported but not fully reconstituted in vitro\",\n      \"pmids\": [\"39024411\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"IMC32 is an essential Toxoplasma gondii IMC protein that anchors to the nascent daughter bud membrane via N-terminal palmitoylation and uses its C-terminal coiled-coil domains to physically interact with IMC43 and BCC0, forming a tripartite essential daughter bud assembly complex that lays the structural foundation of the daughter IMC scaffold during endodyogeny; loss of IMC32 causes complete IMC collapse and parasite death.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"IMC32 is an essential Toxoplasma gondii inner membrane complex (IMC) protein that lays the structural foundation of the daughter bud scaffold during endodyogeny [#0]. It localizes to the body portion of the IMC and is recruited to developing daughter buds early in replication; conditional depletion causes complete collapse of the IMC and is lethal [#0]. IMC32 anchors to the nascent bud membrane through an N-terminal palmitoylation site, whose mutation disrupts membrane association [#1], while its C-terminal coiled-coil domains — containing two conserved functionally critical regions — are required both for correct localization and for its role in replication [#2]. Through these coiled-coil domains IMC32 physically binds IMC43 and BCC0, forming a tripartite essential daughter bud assembly complex [#4, #5]. IMC43 acts upstream, controlling IMC32 localization at specific stages of endodyogeny [#3], and BCC0's own recruitment depends on both IMC32 and IMC43, with its essential domain (residues 701\\u2013877) directly binding the IMC32 coiled-coil [#5]. Assembly proceeds by an IMC32\\u2013BCC0 subcomplex recruiting to nascent buds via IMC32 palmitoylation, which is subsequently locked into the scaffold by IMC32\\u2013IMC43 binding as bud elongation begins; BCC0 and IMC43 do not directly interact [#6].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Establishing whether IMC32 is a functionally important IMC component addressed whether it contributes structurally to daughter bud formation, and showed it is essential for the integrity of the IMC scaffold.\",\n      \"evidence\": \"Conditional degron depletion with fluorescence localization in T. gondii, revealing early daughter bud recruitment and lethal IMC collapse upon loss\",\n      \"pmids\": [\"33593973\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular partners not yet identified\", \"Mechanism by which IMC collapse leads to death not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Dissecting which sequence features drive IMC32 membrane targeting versus function distinguished a lipid-anchoring role from a protein-interaction role, defining a bipartite domain architecture.\",\n      \"evidence\": \"Site-directed mutagenesis of the N-terminal palmitoylation site and deletion mapping of C-terminal coiled-coil regions with functional complementation in T. gondii\",\n      \"pmids\": [\"33593973\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Identity of binding partners engaged by the coiled-coil domains unknown at this stage\", \"Palmitoylating enzyme not identified\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Determining what governs IMC32 stage-specific localization and what it binds revealed IMC43 as an upstream regulator and direct partner, defining a two-component essential complex.\",\n      \"evidence\": \"Auxin-inducible degron depletion of IMC43 showing IMC32 mislocalization, plus TurboID and pairwise yeast two-hybrid domain mapping of a direct IMC43\\u2013IMC32 interaction in T. gondii\",\n      \"pmids\": [\"37782662\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Interaction not reconstituted with purified proteins\", \"Whether additional components complete the complex unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Identifying a third complex member and mapping the order of assembly addressed how the daughter bud scaffold nucleates, establishing a tripartite complex and a stepwise recruitment logic.\",\n      \"evidence\": \"Proximity labeling and yeast two-hybrid identifying BCC0 binding the IMC32 coiled-coil (residues 701\\u2013877), plus sequential depletion/localization epistasis and a negative BCC0\\u2013IMC43 yeast two-hybrid in T. gondii\",\n      \"pmids\": [\"39024411\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Assembly order inferred from localization epistasis, not fully reconstituted in vitro\", \"Downstream scaffold components recruited after this complex not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How the IMC32-anchored complex is connected to downstream IMC alveolar/cytoskeletal architecture and what enzymes control IMC32 palmitoylation dynamics remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Palmitoyltransferase acting on IMC32 not identified\", \"Structural basis of coiled-coil-mediated binding not resolved\", \"Link to mature IMC scaffold assembly uncharacterized\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [4, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0070258\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0051301\", \"supporting_discovery_ids\": [0, 3, 6], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"IMC32-IMC43-BCC0 essential daughter bud assembly complex\"\n    ],\n    \"partners\": [\n      \"IMC43\",\n      \"BCC0\"\n    ],\n    \"other_free_text\": [\n      \"N-terminal palmitoylation anchors IMC32 to the nascent daughter bud membrane [#1]\",\n      \"C-terminal coiled-coil domains mediate binding to both IMC43 and BCC0 [#2, #4, #5]\",\n      \"IMC43 acts upstream of IMC32 in daughter bud assembly [#3]\",\n      \"BCC0-IMC43 do not directly interact; IMC32 bridges the complex [#6]\",\n      \"Conditional depletion causes complete IMC collapse and parasite death [#0]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_232150","name":"IMC32","product":"inner membrane complex protein IMC32","uniprot_acc":"S8EZT1","chromosome":"TGME49_chrVIII","start_pos":1888716},{"strain":"GT1","gene_id":"TGGT1_232150","name":null,"product":"hypothetical protein","uniprot_acc":null,"chromosome":"TGGT1_chrVIII","start_pos":1884936},{"strain":"RH88","gene_id":"TGRH88_076280","name":null,"product":"unspecified product","uniprot_acc":null,"chromosome":"CM023089","start_pos":6995249},{"strain":"VEG","gene_id":"TGVEG_232150","name":null,"product":"hypothetical protein","uniprot_acc":"A0A0F7V0W3","chromosome":"TGVEG_chrVIII","start_pos":1895932}]}