{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T20:01:07Z","timestamp":1791230467084,"version":"4.1.0"},"reference-count":32,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2025,8,4]],"date-time":"2025-08-04T00:00:00Z","timestamp":1754265600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005046","name":"Natural Science Foundation of Heilongjiang Province","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005046","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell. Infect. Microbiol."],"abstract":"<jats:p><jats:italic>Toxoplasma gondii<\/jats:italic> is an obligate intracellular apicomplexan parasite. Most apicomplexan parasites contain an endosymbiont-derived organelle called the apicoplast. This organelle is critical for the survival of parasites because it plays a role in several essential metabolic pathways. However, the molecular mechanisms involved in maintaining the apicoplast have not been well understood. In this study, we investigated the function of an apicoplast-residing protein called <jats:italic>Tg<\/jats:italic>YCAP in the inheritance of the apicoplast. Our results showed that conditional knockdown of <jats:italic>Tg<\/jats:italic>YCAP severely inhibited the growth of the parasite and disrupted the inheritance of the apicoplast. In addition, the YGGT domain is essential for its function in the apicoplast.<\/jats:p>","DOI":"10.3389\/fcimb.2025.1642716","type":"journal-article","created":{"date-parts":[[2025,8,4]],"date-time":"2025-08-04T05:27:02Z","timestamp":1754285222000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":1,"title":["A novel YGGT family protein is localized in the apicoplast and is essential for the organelle inheritance"],"prefix":"10.3389","volume":"15","author":[{"given":"Wenqiang","family":"Su","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haorong","family":"Gu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Honglin","family":"Jia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2025,8,4]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1003426","article-title":"An apicoplast localized ubiquitylation system is required for the import of nuclear-encoded plastid proteins","volume":"9","author":"Agrawal","year":"2013","journal-title":"PloS Pathog."},{"key":"B2","doi-asserted-by":"publisher","first-page":"33683","DOI":"10.1074\/jbc.M109.044024","article-title":"Genetic evidence that an endosymbiont-derived endoplasmic reticulum-associated protein degradation (ERAD) system functions in import of apicoplast proteins","volume":"284","author":"Agrawal","year":"2009","journal-title":"J. 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