{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T02:33:42Z","timestamp":1787884422461,"version":"build-2784847793"},"update-to":[{"DOI":"10.1371\/journal.pbio.3003028","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2025,2,19]],"date-time":"2025-02-19T00:00:00Z","timestamp":1739923200000}}],"reference-count":87,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2025,2,6]],"date-time":"2025-02-06T00:00:00Z","timestamp":1738800000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-22-CE20-0026"],"award-info":[{"award-number":["ANR-22-CE20-0026"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-22-CE20-0026"],"award-info":[{"award-number":["ANR-22-CE20-0026"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosbiology.org"],"crossmark-restriction":false},"short-container-title":["PLoS Biol"],"abstract":"<jats:p>\n                    Several key cellular functions depend on proteins harboring an iron\u2013sulfur (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.\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    is a plastid-bearing parasitic protist responsible for a pathology affecting humans and other warm-blooded vertebrates. We have characterized the\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    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\n                    <jats:italic>Toxoplasma<\/jats:italic>\n                    . 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.\n                  <\/jats:p>","DOI":"10.1371\/journal.pbio.3003028","type":"journal-article","created":{"date-parts":[[2025,2,6]],"date-time":"2025-02-06T13:57:44Z","timestamp":1738850264000},"page":"e3003028","update-policy":"https:\/\/doi.org\/10.1371\/journal.pbio.corrections_policy","source":"Crossref","is-referenced-by-count":6,"title":["The HCF101 protein is an important component of the cytosolic iron\u2013sulfur synthesis pathway in Toxoplasma gondii"],"prefix":"10.1371","volume":"23","author":[{"given":"El\u00e9a A.","family":"Renaud","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ambre J. 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