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Interactome of PRMT5 in malaria parasite Plasmodium falciparum

ABSTRACT: Protein arginine methyltransferases (PRMTs) modify proteins that cause their functional change by modulating their localization and interactions with their partners, which controls their functions on cellular processes, such as transcription and signal transduction, DNA repair, and RNA processing. The majority of studies on PRMTs are focused on yeast and mammals. We characterize PfPRMT5, a type II PRMT, from the early eukaryote Plasmodium falciparum. PfPRMT5 contains the conserved domain structures of type II enzyme with a diverse long N-terminus. This study revealed that PfPRMT5 associated with other invasion related transcriptional regulators such as AP2-I and BDP1. Furthermore, PfPRMT5 was associated with RNA splicing machinery, indicating that PfPRMT5 plays a critical role in regulating invasion and harbors conserved function in RNA metabolism.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Plasmodium Falciparum (isolate 3d7)

TISSUE(S): Single Nucleate Cell

DISEASE(S): Plasmodium Falciparum Malaria

SUBMITTER: JUN MIAO

LAB HEAD: Jun Miao

PROVIDER: PXD032834 | Pride | 2023-06-28

REPOSITORIES: Pride

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DNA methyltransferase (DNMT) associated proteins in human malaria parasite Plasmodium falciparum

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mRNAs associated with EIF4E1 and EIF4E6 in Trypanosoma brucei

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