Protein arginine methylation, an evolutionarily conserved post-translational modification, serves critical cellular functions by transferring a methyl group to a variety of substrates, including histones and some transcription factors. In budding yeast, HSL7 (histone synthetic lethal 7) displays type II PRMT (protein arginine methyltransferase) activity by generating symmetric dimethylarginine residues on histone H2A in vitro. However, identification of the in vivo substrate of HSL7 and how it contributes to important cellular processes remain largely unexplored. In the present study, we show that HSL7 has a repressive role in transcription. We found that HSL7 is responsible for in vivo symmetric dimethylation of histone H4 arginine 3 (H4R3me2s) in a transcriptionally repressed state. Tandem affinity purification further demonstrated that HSL7 physically interacts with histone deacetylase RPD3, and both similarly repress transcription. Our results suggest that H4R3me2s generation by the type II PRMT HSL7 is required for transcriptional repression, possibly in cooperation with histone deacetylation by RPD3.

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Journal Article

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Ryu HY, Duan R, Ahn SH

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