Eukaryotic transcription regulation is crucial for establishing how cells respond to various signals and maintain proper gene expression patterns. Post-translational modifications (PTMs) play an essential role in modulating the activity of the transcriptional machinery and chromatin structure. To fully understand cell functioning and the molecular basis of pathological conditions, it is necessary to understand the molecular principles that enable PTMs to modulate transcriptional regulation. Protein citrullination (deimination) is the PTM of arginine to the non-coded amino acid citrulline, catalyzed by the peptidyl arginine deiminases (PADIs) enzyme family. We previously showed that PADI2 specifically citrullinates the RNAPII to dictate the active transcription required to maintain cell proliferation. Functionally, Cit1810 enhances the association of active RNAP2 with the positive transcription elongation factor-b kinase complex. In this way, Cit1810 promotes the transcription regulation of essential genes contributing to cell identity.
Our finding provides a new spectrum to the functional implication of citrullination to the transcription machinery.
I will discuss our unpublished data on the potential role of PADI2-mediated citrullination on transcriptional events.