An essential endoplasmic reticulum-resident N-acetyltransferase ortholog in Plasmodium falciparum.
In: Journal of Cell Science, Jg. 136 (2023-03-15), Heft 6, S. 1-13
academicJournal
Zugriff:
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. [ABSTRACT FROM AUTHOR]
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Titel: |
An essential endoplasmic reticulum-resident N-acetyltransferase ortholog in Plasmodium falciparum.
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Autor/in / Beteiligte Person: | Polino, Alexander J. ; Hasan, Muhammad M. ; Floyd, Katherine ; Avila-Cruz, Yolotzin ; Yang, Yujuan ; Goldberg, Daniel E. |
Zeitschrift: | Journal of Cell Science, Jg. 136 (2023-03-15), Heft 6, S. 1-13 |
Veröffentlichung: | 2023 |
Medientyp: | academicJournal |
ISSN: | 0021-9533 (print) |
DOI: | 10.1242/jcs.260551 |
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