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PXD068464-1

PXD068464 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleA role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5
DescriptionPlasmodium 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 find that the poly-asparagine repeat-containing N terminus 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.
HostingRepositoryMassIVE
AnnounceDate2026-06-04
AnnouncementXMLSubmission_2026-06-04_09:27:23.960.xml
DigitalObjectIdentifier
ReviewLevelNon peer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterDaniel Goldberg
SpeciesList scientific name: Plasmodium falciparum; common name: malaria parasite P. falciparum; NCBI TaxID: 5833;
ModificationListAcetyl; Methyl; Trimethyl; Dimethyl
InstrumentOrbitrap Exploris 240
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-09-17 13:52:54ID requested
12026-06-04 09:27:24announced
Publication List
no publication
Keyword List
submitter keyword: Plasmodium, histone, PfGCN5, DatasetType:Proteomics
Contact List
Daniel Goldberg
contact affiliationWashington University in St. Louis
contact emaildgoldberg@wustl.edu
lab head
Daniel Goldberg
contact affiliationWashington University in St. Louis
contact emaildgoldberg@wustl.edu
dataset submitter
Full Dataset Link List
MassIVE dataset URI
Dataset FTP location
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