The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii.
Several key cellular functions depend on proteins harboring an iron-sulfur (Fe-S) cofactor. As these Fe-S proteins localize to several subcellular compartments, they require a dedicated machinery for cofactor assembly. For instance, in plants and algae there are Fe-S cluster synthesis pathways local...
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| Format: | Article |
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Public Library of Science (PLoS)
2025-02-01
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| Series: | PLoS Biology |
| Online Access: | https://doi.org/10.1371/journal.pbio.3003028 |
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| author | Eléa A Renaud Ambre J M Maupin Laurence Berry Julie Bals Yann Bordat Vincent Demolombe Valérie Rofidal Florence Vignols Sébastien Besteiro |
| author_facet | Eléa A Renaud Ambre J M Maupin Laurence Berry Julie Bals Yann Bordat Vincent Demolombe Valérie Rofidal Florence Vignols Sébastien Besteiro |
| author_sort | Eléa A Renaud |
| collection | DOAJ |
| description | Several key cellular functions depend on proteins harboring an iron-sulfur (Fe-S) cofactor. As these Fe-S proteins localize to several subcellular compartments, they require a dedicated machinery for cofactor assembly. For instance, in plants and algae there are Fe-S cluster synthesis pathways localizing to the cytosol, but also present in the mitochondrion and in the chloroplast, 2 organelles of endosymbiotic origin. Toxoplasma gondii is a plastid-bearing parasitic protist responsible for a pathology affecting humans and other warm-blooded vertebrates. We have characterized the Toxoplasma homolog of HCF101, originally identified in plants as a protein transferring Fe-S clusters to photosystem I subunits in the chloroplast. Contrarily to plants, we have shown that HCF101 does not localize to the plastid in parasites, but instead is an important component of the cytosolic Fe-S assembly (CIA) pathway which is vital for Toxoplasma. While the CIA pathway is widely conserved in eukaryotes, it is the first time the involvement of HCF101 in this pan-eukaryotic machinery is established. Moreover, as this protein is essential for parasite viability and absent from its mammalian hosts, it constitutes a novel and promising potential drug target. |
| format | Article |
| id | doaj-art-1e20c3c59c824eaf9415b4922a41ea37 |
| institution | DOAJ |
| issn | 1544-9173 1545-7885 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj-art-1e20c3c59c824eaf9415b4922a41ea372025-08-20T02:57:16ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852025-02-01232e300302810.1371/journal.pbio.3003028The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii.Eléa A RenaudAmbre J M MaupinLaurence BerryJulie BalsYann BordatVincent DemolombeValérie RofidalFlorence VignolsSébastien BesteiroSeveral key cellular functions depend on proteins harboring an iron-sulfur (Fe-S) cofactor. As these Fe-S proteins localize to several subcellular compartments, they require a dedicated machinery for cofactor assembly. For instance, in plants and algae there are Fe-S cluster synthesis pathways localizing to the cytosol, but also present in the mitochondrion and in the chloroplast, 2 organelles of endosymbiotic origin. Toxoplasma gondii is a plastid-bearing parasitic protist responsible for a pathology affecting humans and other warm-blooded vertebrates. We have characterized the Toxoplasma homolog of HCF101, originally identified in plants as a protein transferring Fe-S clusters to photosystem I subunits in the chloroplast. Contrarily to plants, we have shown that HCF101 does not localize to the plastid in parasites, but instead is an important component of the cytosolic Fe-S assembly (CIA) pathway which is vital for Toxoplasma. While the CIA pathway is widely conserved in eukaryotes, it is the first time the involvement of HCF101 in this pan-eukaryotic machinery is established. Moreover, as this protein is essential for parasite viability and absent from its mammalian hosts, it constitutes a novel and promising potential drug target.https://doi.org/10.1371/journal.pbio.3003028 |
| spellingShingle | Eléa A Renaud Ambre J M Maupin Laurence Berry Julie Bals Yann Bordat Vincent Demolombe Valérie Rofidal Florence Vignols Sébastien Besteiro The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii. PLoS Biology |
| title | The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii. |
| title_full | The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii. |
| title_fullStr | The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii. |
| title_full_unstemmed | The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii. |
| title_short | The HCF101 protein is an important component of the cytosolic iron-sulfur synthesis pathway in Toxoplasma gondii. |
| title_sort | hcf101 protein is an important component of the cytosolic iron sulfur synthesis pathway in toxoplasma gondii |
| url | https://doi.org/10.1371/journal.pbio.3003028 |
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