ArticleNature communications2026
A role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Plasmodium falciparum possesses one of the most AT-rich genomes in nature (80.6%). A consequence is an asparagine-rich proteome. A quarter of P. falciparum proteins possess poly-asparagine repeats that can extend more than 100 residues. The role of these repeats has remained a mystery in the biology of this parasite. Here, we report that the poly-asparagine repeat-containing Nterminus of the histone acetyltransferase PfGCN5 associates with the C-terminal catalytic domain after cleavage in the nucleus. Deletion of the repeat destabilizes the N-terminal polypeptide, leading to impaired parasite development and growth, particularly under stress conditions. Using high-resolution mass spectrometry and western blotting analysis, we uncovered a profound effect of the poly-asparagine repeat on acetylation of histones H3, H3.3, and H4. These findings suggest that the poly-asparagine repeat contributes to PfGCN5 acetyltransferase activity, a role previously attributed solely to its C-terminal domain. This report of a function for a poly-asparagine repeat in P. falciparum expands our understanding of a pervasive characteristic of its proteome.
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