{"gene":"TG_270690","gene_symbol":"DRPC","run_date":"2026-09-08T14:08:29","timeline":{"discoveries":[{"year":2018,"finding":"TgDrpC localizes to cytoplasmic puncta in non-dividing parasites but redistributes to the growing edge of daughter cells during parasite division, and this redistribution is dependent on post-Golgi trafficking.","method":"Conditional knockdown, live imaging/localization, pharmacological inhibition of post-Golgi trafficking","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiments with functional consequence (division-stage redistribution) and post-Golgi trafficking dependency, single lab with multiple orthogonal approaches","pmids":["30362624"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"finding":"Conditional knockdown of TgDrpC stalls parasite division and leads to rapid deterioration of multiple organelles and the inner membrane complex (IMC), establishing TgDrpC as essential for parasite division and organelle stability.","method":"Conditional knockdown with defined phenotypic readout (organelle morphology, IMC integrity, division arrest)","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — conditional knockdown with specific cellular phenotypes, single lab","pmids":["30362624"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"finding":"TgDrpC physically interacts with proteins homologous to vesicle transport factors, including a homolog of the adaptor protein 2 (AP-2) complex subunit alpha-1 and a homolog of ERM (ezrin-radixin-moesin) family proteins, both of which localize to puncta and associate with daughter cells.","method":"Co-immunoprecipitation / interaction proteomics, co-localization","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — interaction data from pulldown/Co-IP with co-localization support, single lab","pmids":["30362624"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"finding":"TgDrpC is unusual among dynamin-related proteins in that it lacks a conserved GTPase Effector Domain (GED), which is typically required for dynamin function.","method":"Sequence/domain analysis reported in the context of functional studies","journal":"Molecular microbiology","confidence":"Low","confidence_rationale":"Tier 4 / Weak — domain analysis only, no direct biochemical validation of GED absence impact","pmids":["30362624"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"TgDrpC localizes adjacent to the mitochondrion, both at its periphery and at its basal part where fission is expected to occur. Depletion or dominant-negative expression of TgDrpC results in interconnected mitochondria, drastic changes in mitochondrial morphology, and parasite death, establishing TgDrpC as essential for mitochondrial fission and biogenesis.","method":"Conditional knockdown, dominant-negative expression, fluorescence microscopy of mitochondrial morphology, viability assays","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal loss-of-function approaches (knockdown and dominant negative) with specific mitochondrial morphology readouts, replicated within one rigorous study with multiple orthogonal methods","pmids":["30947298"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"The canonical mitochondrial fission adaptor TgFis1 is NOT required for mitochondrial fission in Toxoplasma gondii, indicating that TgDrpC operates through a non-canonical fission mechanism lacking the typical Fis1 adaptor.","method":"Genetic loss-of-function of TgFis1 with mitochondrial morphology readout","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct genetic test of TgFis1 requirement, negative result mechanistically informative, single lab","pmids":["30947298"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"finding":"Conditional knockdown of drpC using DiCre-mediated U1 snRNP-based gene silencing demonstrates that drpC can be efficiently depleted in T. gondii, validating it as an endogenous gene amenable to conditional mutagenesis; the knockdown was used as a proof-of-concept for the silencing technology.","method":"DiCre-mediated conditional U1 snRNP-based knockdown, rapamycin induction","journal":"PloS one","confidence":"Low","confidence_rationale":"Tier 3 / Weak — drpC used as a proof-of-concept target; no mechanistic characterization of TgDrpC function reported in this paper","pmids":["26090798"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgDrpC is an Apicomplexa-specific dynamin-related protein that localizes adjacent to and at the basal part of the single Toxoplasma mitochondrion, where it is essential for mitochondrial fission and biogenesis; it also redistributes to the growing edge of daughter cells during division in a post-Golgi trafficking-dependent manner and interacts with AP-2 complex and ERM-family vesicle transport proteins, with its depletion or dominant-negative expression causing interconnected mitochondria, organelle deterioration, and parasite death, while the canonical fission adaptor TgFis1 is dispensable for this process."},"narrative":{"mechanistic_narrative":"TgDrpC is an Apicomplexa-specific dynamin-related protein essential for mitochondrial fission, organelle biogenesis, and parasite division in Toxoplasma gondii [PMID:30947298, PMID:30362624]. It localizes adjacent to the single mitochondrion, both at its periphery and at the basal region where fission occurs, and depletion or dominant-negative expression yields interconnected mitochondria, drastic morphological defects, and parasite death [PMID:30947298]. During parasite division TgDrpC redistributes from cytoplasmic puncta to the growing edge of daughter cells in a post-Golgi trafficking-dependent manner, and its conditional knockdown stalls division while causing deterioration of multiple organelles and the inner membrane complex [PMID:30362624]. TgDrpC physically interacts with vesicle transport factors, including a homolog of the AP-2 complex alpha-1 subunit and an ERM-family homolog that co-localize to puncta and daughter cells [PMID:30362624]. It operates through a non-canonical fission mechanism, as the conventional adaptor TgFis1 is dispensable for mitochondrial fission [PMID:30947298]. Beyond these findings, the biochemical basis of its activity has not been characterized in the available corpus.","teleology":[{"year":2015,"claim":"Establishing that drpC is an endogenous, silenceable gene provided the genetic entry point for interrogating its function.","evidence":"DiCre-mediated U1 snRNP-based conditional knockdown with rapamycin induction in T. gondii, used as proof-of-concept","pmids":["26090798"],"confidence":"Low","gaps":["No mechanistic characterization of TgDrpC function in this study","Used only as a technical demonstration of the silencing platform"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"claim":"Whether TgDrpC has a division-stage role was answered by showing its dynamic redistribution to daughter cell growing edges and its essentiality for division and organelle integrity.","evidence":"Conditional knockdown, live imaging, and pharmacological inhibition of post-Golgi trafficking in T. gondii","pmids":["30362624"],"confidence":"Medium","gaps":["The molecular cargo/function of TgDrpC at the daughter cell edge is undefined","Whether organelle deterioration is a direct or downstream consequence of division arrest is unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"claim":"The trafficking context of TgDrpC was addressed by identifying interactions with AP-2 and ERM-family vesicle transport homologs, linking it to a membrane-trafficking machinery.","evidence":"Co-immunoprecipitation/interaction proteomics with co-localization in T. gondii","pmids":["30362624"],"confidence":"Medium","gaps":["Interactions not validated reciprocally","Functional consequence of the AP-2 and ERM associations for fission or division not tested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"claim":"The primary organellar target of TgDrpC was defined as the mitochondrion, establishing it as essential for mitochondrial fission and biogenesis.","evidence":"Conditional knockdown, dominant-negative expression, mitochondrial morphology imaging, and viability assays in T. gondii","pmids":["30947298"],"confidence":"High","gaps":["Direct demonstration of GTP-dependent membrane scission activity is absent","The mechanism recruiting TgDrpC to the fission site is unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"claim":"Whether TgDrpC uses the canonical fission adaptor was answered by showing TgFis1 is dispensable, revealing a non-canonical fission mechanism.","evidence":"Genetic loss-of-function of TgFis1 with mitochondrial morphology readout in T. gondii","pmids":["30947298"],"confidence":"Medium","gaps":["The actual adaptor recruiting TgDrpC to the mitochondrion is unidentified","Negative result from a single lab"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The biochemical basis of TgDrpC action, including whether its atypical domain architecture supports GTPase-driven membrane scission and how it is recruited absent Fis1, remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct biochemical validation of the functional consequence of the missing GTPase Effector Domain","No identified mitochondrial recruitment adaptor","No reconstitution of fission activity in vitro"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["AP-2 COMPLEX ALPHA-1 SUBUNIT HOMOLOG [#2]","ERM (EZRIN-RADIXIN-MOESIN) FAMILY PROTEIN HOMOLOG [#2]"],"other_free_text":["Apicomplexa-specific dynamin-related protein that lacks the conserved GTPase Effector Domain (GED) typical of dynamins [#3]","Operates through a non-canonical fission mechanism independent of the canonical adaptor TgFis1 [#5]","Redistribution to daughter cell growing edge during division depends on post-Golgi trafficking [#0]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"26090798","id":"PMC_26090798","title":"Conditional U1 Gene Silencing in Toxoplasma gondii.","date":"2015","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26090798","citation_count":51,"is_preprint":false},{"pmid":"30947298","id":"PMC_30947298","title":"A unique dynamin-related protein is essential for mitochondrial fission in Toxoplasma gondii.","date":"2019","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/30947298","citation_count":33,"is_preprint":false},{"pmid":"30362624","id":"PMC_30362624","title":"TgDrpC, an atypical dynamin-related protein in Toxoplasma gondii, is associated with vesicular transport factors and parasite division.","date":"2018","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/30362624","citation_count":24,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3813,"output_tokens":1731,"usd":0.018702,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6975,"output_tokens":2466,"usd":0.048262,"stage2_stop_reason":"end_turn"},"total_usd":0.066964,"stage1_batch_id":"msgbatch_015xmQKDRqnTh9anE4m7LiD6","stage2_batch_id":"msgbatch_01JLpkFTVhoQBNgqHCKFrVVU","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2018,\n      \"finding\": \"TgDrpC localizes to cytoplasmic puncta in non-dividing parasites but redistributes to the growing edge of daughter cells during parasite division, and this redistribution is dependent on post-Golgi trafficking.\",\n      \"method\": \"Conditional knockdown, live imaging/localization, pharmacological inhibition of post-Golgi trafficking\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiments with functional consequence (division-stage redistribution) and post-Golgi trafficking dependency, single lab with multiple orthogonal approaches\",\n      \"pmids\": [\"30362624\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Conditional knockdown of TgDrpC stalls parasite division and leads to rapid deterioration of multiple organelles and the inner membrane complex (IMC), establishing TgDrpC as essential for parasite division and organelle stability.\",\n      \"method\": \"Conditional knockdown with defined phenotypic readout (organelle morphology, IMC integrity, division arrest)\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — conditional knockdown with specific cellular phenotypes, single lab\",\n      \"pmids\": [\"30362624\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"TgDrpC physically interacts with proteins homologous to vesicle transport factors, including a homolog of the adaptor protein 2 (AP-2) complex subunit alpha-1 and a homolog of ERM (ezrin-radixin-moesin) family proteins, both of which localize to puncta and associate with daughter cells.\",\n      \"method\": \"Co-immunoprecipitation / interaction proteomics, co-localization\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — interaction data from pulldown/Co-IP with co-localization support, single lab\",\n      \"pmids\": [\"30362624\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"TgDrpC is unusual among dynamin-related proteins in that it lacks a conserved GTPase Effector Domain (GED), which is typically required for dynamin function.\",\n      \"method\": \"Sequence/domain analysis reported in the context of functional studies\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — domain analysis only, no direct biochemical validation of GED absence impact\",\n      \"pmids\": [\"30362624\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TgDrpC localizes adjacent to the mitochondrion, both at its periphery and at its basal part where fission is expected to occur. Depletion or dominant-negative expression of TgDrpC results in interconnected mitochondria, drastic changes in mitochondrial morphology, and parasite death, establishing TgDrpC as essential for mitochondrial fission and biogenesis.\",\n      \"method\": \"Conditional knockdown, dominant-negative expression, fluorescence microscopy of mitochondrial morphology, viability assays\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal loss-of-function approaches (knockdown and dominant negative) with specific mitochondrial morphology readouts, replicated within one rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"30947298\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"The canonical mitochondrial fission adaptor TgFis1 is NOT required for mitochondrial fission in Toxoplasma gondii, indicating that TgDrpC operates through a non-canonical fission mechanism lacking the typical Fis1 adaptor.\",\n      \"method\": \"Genetic loss-of-function of TgFis1 with mitochondrial morphology readout\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct genetic test of TgFis1 requirement, negative result mechanistically informative, single lab\",\n      \"pmids\": [\"30947298\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Conditional knockdown of drpC using DiCre-mediated U1 snRNP-based gene silencing demonstrates that drpC can be efficiently depleted in T. gondii, validating it as an endogenous gene amenable to conditional mutagenesis; the knockdown was used as a proof-of-concept for the silencing technology.\",\n      \"method\": \"DiCre-mediated conditional U1 snRNP-based knockdown, rapamycin induction\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — drpC used as a proof-of-concept target; no mechanistic characterization of TgDrpC function reported in this paper\",\n      \"pmids\": [\"26090798\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgDrpC is an Apicomplexa-specific dynamin-related protein that localizes adjacent to and at the basal part of the single Toxoplasma mitochondrion, where it is essential for mitochondrial fission and biogenesis; it also redistributes to the growing edge of daughter cells during division in a post-Golgi trafficking-dependent manner and interacts with AP-2 complex and ERM-family vesicle transport proteins, with its depletion or dominant-negative expression causing interconnected mitochondria, organelle deterioration, and parasite death, while the canonical fission adaptor TgFis1 is dispensable for this process.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TgDrpC is an Apicomplexa-specific dynamin-related protein essential for mitochondrial fission, organelle biogenesis, and parasite division in Toxoplasma gondii [#4, #1]. It localizes adjacent to the single mitochondrion, both at its periphery and at the basal region where fission occurs, and depletion or dominant-negative expression yields interconnected mitochondria, drastic morphological defects, and parasite death [#4]. During parasite division TgDrpC redistributes from cytoplasmic puncta to the growing edge of daughter cells in a post-Golgi trafficking-dependent manner, and its conditional knockdown stalls division while causing deterioration of multiple organelles and the inner membrane complex [#0, #1]. TgDrpC physically interacts with vesicle transport factors, including a homolog of the AP-2 complex alpha-1 subunit and an ERM-family homolog that co-localize to puncta and daughter cells [#2]. It operates through a non-canonical fission mechanism, as the conventional adaptor TgFis1 is dispensable for mitochondrial fission [#5]. Beyond these findings, the biochemical basis of its activity has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2015,\n      \"claim\": \"Establishing that drpC is an endogenous, silenceable gene provided the genetic entry point for interrogating its function.\",\n      \"evidence\": \"DiCre-mediated U1 snRNP-based conditional knockdown with rapamycin induction in T. gondii, used as proof-of-concept\",\n      \"pmids\": [\"26090798\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No mechanistic characterization of TgDrpC function in this study\", \"Used only as a technical demonstration of the silencing platform\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Whether TgDrpC has a division-stage role was answered by showing its dynamic redistribution to daughter cell growing edges and its essentiality for division and organelle integrity.\",\n      \"evidence\": \"Conditional knockdown, live imaging, and pharmacological inhibition of post-Golgi trafficking in T. gondii\",\n      \"pmids\": [\"30362624\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"The molecular cargo/function of TgDrpC at the daughter cell edge is undefined\", \"Whether organelle deterioration is a direct or downstream consequence of division arrest is unresolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"The trafficking context of TgDrpC was addressed by identifying interactions with AP-2 and ERM-family vesicle transport homologs, linking it to a membrane-trafficking machinery.\",\n      \"evidence\": \"Co-immunoprecipitation/interaction proteomics with co-localization in T. gondii\",\n      \"pmids\": [\"30362624\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Interactions not validated reciprocally\", \"Functional consequence of the AP-2 and ERM associations for fission or division not tested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"The primary organellar target of TgDrpC was defined as the mitochondrion, establishing it as essential for mitochondrial fission and biogenesis.\",\n      \"evidence\": \"Conditional knockdown, dominant-negative expression, mitochondrial morphology imaging, and viability assays in T. gondii\",\n      \"pmids\": [\"30947298\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct demonstration of GTP-dependent membrane scission activity is absent\", \"The mechanism recruiting TgDrpC to the fission site is unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether TgDrpC uses the canonical fission adaptor was answered by showing TgFis1 is dispensable, revealing a non-canonical fission mechanism.\",\n      \"evidence\": \"Genetic loss-of-function of TgFis1 with mitochondrial morphology readout in T. gondii\",\n      \"pmids\": [\"30947298\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"The actual adaptor recruiting TgDrpC to the mitochondrion is unidentified\", \"Negative result from a single lab\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The biochemical basis of TgDrpC action, including whether its atypical domain architecture supports GTPase-driven membrane scission and how it is recruited absent Fis1, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No direct biochemical validation of the functional consequence of the missing GTPase Effector Domain\", \"No identified mitochondrial recruitment adaptor\", \"No reconstitution of fission activity in vitro\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003924\", \"supporting_discovery_ids\": [4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005741\", \"supporting_discovery_ids\": [4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0000266\", \"supporting_discovery_ids\": [4, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0051301\", \"supporting_discovery_ids\": [1, 0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"AP-2 complex alpha-1 subunit homolog [#2]\",\n      \"ERM (ezrin-radixin-moesin) family protein homolog [#2]\"\n    ],\n    \"other_free_text\": [\n      \"Apicomplexa-specific dynamin-related protein that lacks the conserved GTPase Effector Domain (GED) typical of dynamins [#3]\",\n      \"Operates through a non-canonical fission mechanism independent of the canonical adaptor TgFis1 [#5]\",\n      \"Redistribution to daughter cell growing edge during division depends on post-Golgi trafficking [#0]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_270690","name":"DRPC","product":"dynamin-related protein DRPC","uniprot_acc":"S8GIW4","chromosome":"TGME49_chrVIII","start_pos":5070319},{"strain":"GT1","gene_id":"TGGT1_270690","name":null,"product":"arginyl-tRNA synthetase","uniprot_acc":null,"chromosome":"TGGT1_chrVIII","start_pos":5067864},{"strain":"RH88","gene_id":"TGRH88_080750","name":null,"product":"arginyl-tRNA synthetase","uniprot_acc":null,"chromosome":"CM023089","start_pos":10188461},{"strain":"VEG","gene_id":"TGVEG_270690","name":null,"product":"arginyl-tRNA synthetase","uniprot_acc":"B9Q624","chromosome":"TGVEG_chrVIII","start_pos":5083668}]}