{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T02:48:50Z","timestamp":1787021330191,"version":"build-2736575974"},"reference-count":53,"publisher":"The Company of Biologists","issue":"6","license":[{"start":{"date-parts":[[2023,3,6]],"date-time":"2023-03-06T00:00:00Z","timestamp":1678060800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000968","name":"American Heart Association","doi-asserted-by":"crossref","award":["18PRE33960417"],"award-info":[{"award-number":["18PRE33960417"]}],"id":[{"id":"10.13039\/100000968","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"crossref","award":["RO1 AI047798"],"award-info":[{"award-number":["RO1 AI047798"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"crossref","award":["R21 AI171062"],"award-info":[{"award-number":["R21 AI171062"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100007268","name":"Washington University in St. Louis","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100007268","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,3,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>N-terminal acetylation is a common eukaryotic protein modification that involves the addition of an acetyl group to the N-terminus of a polypeptide. This modification is largely performed by cytosolic N-terminal acetyltransferases (NATs). Most associate with the ribosome, acetylating nascent polypeptides co-translationally. In the malaria parasite Plasmodium falciparum, exported effectors are thought to be translated into the endoplasmic reticulum (ER), processed by the aspartic protease plasmepsin V and then N-acetylated, despite having no clear access to cytosolic NATs. Here, we used inducible gene deletion and post-transcriptional knockdown to investigate the primary ER-resident NAT candidate, Pf3D7_1437000. We found that it localizes to the ER and is required for parasite growth. However, depletion of Pf3D7_1437000 had no effect on protein export or acetylation of the exported proteins HRP2 and HRP3. Despite this, Pf3D7_1437000 depletion impedes parasite development within the host red blood cell and prevents parasites from completing genome replication. Thus, this work provides further proof of N-terminal acetylation of secretory system proteins, a process unique to apicomplexan parasites, but strongly discounts a promising candidate for this post-translational modification.<\/jats:p>","DOI":"10.1242\/jcs.260551","type":"journal-article","created":{"date-parts":[[2023,2,6]],"date-time":"2023-02-06T04:06:06Z","timestamp":1675656366000},"source":"Crossref","is-referenced-by-count":9,"title":["An essential endoplasmic reticulum-resident N-acetyltransferase ortholog in\n                    <i>Plasmodium falciparum<\/i>"],"prefix":"10.1242","volume":"136","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2601-3638","authenticated-orcid":false,"given":"Alexander J.","family":"Polino","sequence":"first","affiliation":[{"name":"Washington University School of Medicine Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology , , St Louis, MO 63110 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muhammad M.","family":"Hasan","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology , , St Louis, MO 63110 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5242-090X","authenticated-orcid":false,"given":"Katherine","family":"Floyd","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology , , St Louis, MO 63110 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yolotzin","family":"Avila-Cruz","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology , , St Louis, MO 63110 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5428-8180","authenticated-orcid":false,"given":"Yujuan","family":"Yang","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology , , St Louis, MO 63110 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3529-8399","authenticated-orcid":false,"given":"Daniel E.","family":"Goldberg","sequence":"additional","affiliation":[{"name":"Washington University School of Medicine Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology , , St Louis, MO 63110 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2023,3,6]]},"reference":[{"key":"2023030612410976600_","doi-asserted-by":"publisher","first-page":"D898","DOI":"10.1093\/nar\/gkab929","article-title":"VEuPathDB: the eukaryotic pathogen, vector and host bioinformatics resource center","volume":"50","author":"Amos","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"2023030612410976600_","doi-asserted-by":"publisher","first-page":"990","DOI":"10.1073\/pnas.022630099","article-title":"Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine","volume":"99","author":"Banerjee","year":"2002","journal-title":"Proc. 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