The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i>
<p><b>(A–F)</b> Western blots of proteins extracted from <b>(A)</b> <i>Tg</i>Tah18-HA, <b>(B)</b> <i>Tg</i>Dre2-HA, <b>(C)</b> HA-mAID-<i>Tg</i>Nar1, <b>(D)</b> <i>Tg</i>CIA1-HA, <b&g...
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2025
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| _version_ | 1849927626957783040 |
|---|---|
| author | Evie R. Hodgson (21866946) |
| author2 | Jenni A. Hayward (10063377) Rachel A. Leonard (5195411) F. Victor Makota (16625292) Giel G. van Dooren (10063383) |
| author2_role | author author author author |
| author_facet | Evie R. Hodgson (21866946) Jenni A. Hayward (10063377) Rachel A. Leonard (5195411) F. Victor Makota (16625292) Giel G. van Dooren (10063383) |
| author_role | author |
| dc.creator.none.fl_str_mv | Evie R. Hodgson (21866946) Jenni A. Hayward (10063377) Rachel A. Leonard (5195411) F. Victor Makota (16625292) Giel G. van Dooren (10063383) |
| dc.date.none.fl_str_mv | 2025-11-25T18:38:20Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003520.g001 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/The_CIA_pathway_localizes_to_the_mitochondrion_of_i_Toxoplasma_gondii_i_/30714631 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biochemistry Medicine Microbiology Cell Biology Immunology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified iron – sulfur eukaryotic cell biology elucidates pivotal differences div >< p exhibit dual localization nuclear client proteins toxoplasma gondii </ cia targeting complex toxoplasma </ nuclear proteins gondii </ mitochondrial targeting three proteins study provides showed previously scaffold protein remained unclear present evidence otherwise ancient may reflect living relatives important group functionally conserved comprehensive analysis closest free cia1 protein |
| dc.title.none.fl_str_mv | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p><b>(A–F)</b> Western blots of proteins extracted from <b>(A)</b> <i>Tg</i>Tah18-HA, <b>(B)</b> <i>Tg</i>Dre2-HA, <b>(C)</b> HA-mAID-<i>Tg</i>Nar1, <b>(D)</b> <i>Tg</i>CIA1-HA, <b>(E)</b> <i>Tg</i>CIA2-HA, or <b>(F)</b> <i>Tg</i>MMS19-HA expressing parasites, separated by SDS-PAGE and probed with anti-HA antibodies. <i>Tg</i>MMS19-HA appears as two separate bands, the lower of which may represent a degradation product. <b>(G–L)</b> Immunofluorescence assays of <b>(G)</b> <i>Tg</i>Tah18-HA, <b>(H)</b> <i>Tg</i>Dre2-HA, <b>(I)</b> HA-mAID-<i>Tg</i>Nar1, <b>(J)</b> <i>Tg</i>CIA1-HA, <b>(K)</b> <i>Tg</i>CIA2-HA, or <b>(L)</b> <i>Tg</i>MMS19-HA expressing parasites, probed with anti-HA antibodies (green) to label the proteins-of-interest and anti-<i>Tg</i>Tom40 antibodies (magenta) to label the mitochondrion. Scale bars are 2 µm. DIC, differential interference contrast transmission image. Right, corresponding fluorescence profiles depicting the intensity of anti-HA (green) and anti-<i>Tg</i>Tom40 (magenta) labeling along the yellow line on merged images. The numerical data underlying this Figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003520#pbio.3003520.s016" target="_blank">S1 Data</a>. <b>(M)</b> Model for the CIA pathway in <i>T. gondii</i> parasites, with Tah18, NBP35 and Nar1 positioned on the outer face of the mitochondrion, Dre2 in the cytosol, and the CIA Targeting Complex (CTC; consisting of CIA1, CIA2 and MMS19), exhibiting dual cytosolic and mitochondrial localization. Electrons (e<sup>−</sup>) are sourced from NADPH via an electron transfer chain consisting of Tah18 and Dre2. Sulfur (yellow) and possibly iron (red) are sourced from the iron–sulfur cluster (ISC) synthesis pathway in the mitochondrion, assembled as [4Fe-4S] clusters on the NBP35 scaffold, then trafficked via Nar1 to the CTC. The CTC donates FeS clusters to client FeS proteins.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_c0324c9da750019d007953252316825f |
| identifier_str_mv | 10.1371/journal.pbio.3003520.g001 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30714631 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i>Evie R. Hodgson (21866946)Jenni A. Hayward (10063377)Rachel A. Leonard (5195411)F. Victor Makota (16625292)Giel G. van Dooren (10063383)BiochemistryMedicineMicrobiologyCell BiologyImmunologyInfectious DiseasesEnvironmental Sciences not elsewhere classifiedBiological Sciences not elsewhere classifiedPhysical Sciences not elsewhere classifiediron – sulfureukaryotic cell biologyelucidates pivotal differencesdiv >< pexhibit dual localizationnuclear client proteinstoxoplasma gondii </cia targeting complextoxoplasma </nuclear proteinsgondii </mitochondrial targetingthree proteinsstudy providesshowed previouslyscaffold proteinremained unclearpresent evidenceotherwise ancientmay reflectliving relativesimportant groupfunctionally conservedcomprehensive analysisclosest freecia1 protein<p><b>(A–F)</b> Western blots of proteins extracted from <b>(A)</b> <i>Tg</i>Tah18-HA, <b>(B)</b> <i>Tg</i>Dre2-HA, <b>(C)</b> HA-mAID-<i>Tg</i>Nar1, <b>(D)</b> <i>Tg</i>CIA1-HA, <b>(E)</b> <i>Tg</i>CIA2-HA, or <b>(F)</b> <i>Tg</i>MMS19-HA expressing parasites, separated by SDS-PAGE and probed with anti-HA antibodies. <i>Tg</i>MMS19-HA appears as two separate bands, the lower of which may represent a degradation product. <b>(G–L)</b> Immunofluorescence assays of <b>(G)</b> <i>Tg</i>Tah18-HA, <b>(H)</b> <i>Tg</i>Dre2-HA, <b>(I)</b> HA-mAID-<i>Tg</i>Nar1, <b>(J)</b> <i>Tg</i>CIA1-HA, <b>(K)</b> <i>Tg</i>CIA2-HA, or <b>(L)</b> <i>Tg</i>MMS19-HA expressing parasites, probed with anti-HA antibodies (green) to label the proteins-of-interest and anti-<i>Tg</i>Tom40 antibodies (magenta) to label the mitochondrion. Scale bars are 2 µm. DIC, differential interference contrast transmission image. Right, corresponding fluorescence profiles depicting the intensity of anti-HA (green) and anti-<i>Tg</i>Tom40 (magenta) labeling along the yellow line on merged images. The numerical data underlying this Figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003520#pbio.3003520.s016" target="_blank">S1 Data</a>. <b>(M)</b> Model for the CIA pathway in <i>T. gondii</i> parasites, with Tah18, NBP35 and Nar1 positioned on the outer face of the mitochondrion, Dre2 in the cytosol, and the CIA Targeting Complex (CTC; consisting of CIA1, CIA2 and MMS19), exhibiting dual cytosolic and mitochondrial localization. Electrons (e<sup>−</sup>) are sourced from NADPH via an electron transfer chain consisting of Tah18 and Dre2. Sulfur (yellow) and possibly iron (red) are sourced from the iron–sulfur cluster (ISC) synthesis pathway in the mitochondrion, assembled as [4Fe-4S] clusters on the NBP35 scaffold, then trafficked via Nar1 to the CTC. The CTC donates FeS clusters to client FeS proteins.</p>2025-11-25T18:38:20ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003520.g001https://figshare.com/articles/figure/The_CIA_pathway_localizes_to_the_mitochondrion_of_i_Toxoplasma_gondii_i_/30714631CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307146312025-11-25T18:38:20Z |
| spellingShingle | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> Evie R. Hodgson (21866946) Biochemistry Medicine Microbiology Cell Biology Immunology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified iron – sulfur eukaryotic cell biology elucidates pivotal differences div >< p exhibit dual localization nuclear client proteins toxoplasma gondii </ cia targeting complex toxoplasma </ nuclear proteins gondii </ mitochondrial targeting three proteins study provides showed previously scaffold protein remained unclear present evidence otherwise ancient may reflect living relatives important group functionally conserved comprehensive analysis closest free cia1 protein |
| status_str | publishedVersion |
| title | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| title_full | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| title_fullStr | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| title_full_unstemmed | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| title_short | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| title_sort | The CIA pathway localizes to the mitochondrion of <i>Toxoplasma gondii.</i> |
| topic | Biochemistry Medicine Microbiology Cell Biology Immunology Infectious Diseases Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified Physical Sciences not elsewhere classified iron – sulfur eukaryotic cell biology elucidates pivotal differences div >< p exhibit dual localization nuclear client proteins toxoplasma gondii </ cia targeting complex toxoplasma </ nuclear proteins gondii </ mitochondrial targeting three proteins study provides showed previously scaffold protein remained unclear present evidence otherwise ancient may reflect living relatives important group functionally conserved comprehensive analysis closest free cia1 protein |