Comparative Monomethylarginine Proteomics Suggests that Protein Arginine Methyltransferase 1 (PRMT1) is a Significant Contributor to Arginine Monomethylation in Toxoplasma gondii.

摘要: Arginine methylation is a common posttranslational modification found on nuclear and cytoplasmic proteins that has roles in transcriptional regulation, RNA metabolism DNA repair. The protozoan parasite Toxoplasma gondii complex life cycle requiring plasticity unique regulatory pathways. may play an important part regulation splicing biology this organism. T. genome contains five putative protein arginine methyltransferases (PRMTs), of which PRMT1 for cell division growth. In order to better understand the function(s) monomethyl (MMA) gondii, we performed proteomic analysis MMA using affinity purification employing anti-MMA specific antibodies followed by mass spectrometry. monomethylome large number binding multiple ApiAP2 transcription factors, suggesting role regulation. Surprisingly, 90% are monomethylated were detected as being phosphorylated previous phosphoproteomics study raises possibility interplay between phosphorylation Supporting this, kinases also methylated. Because thought be major PRMT organism lacks MMA-specific PRMT, applied comparative proteomics how might contribute proteome gondii. We identified numerous substrates, include proteins, regulators (e.g. AP2 factors), kinases. Together, these data highlight importance potential regulator processes including transcription.