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Peer-Reviewed Publication
bioRxiv2024August 12, 2024Journal Article

Productive mRNA Chromatin Escape is Promoted by PRMT5 Methylation of SNRPB.

Joseph D DeAngelo1,2, Maxim I Maron1,2,3, Jacob S Roth1, Aliza M Silverstein1, Varun Gupta4, Stephanie Stransky1, Joel Basken5,6, Joey Azofeifa5, Simone Sidoli1, Matthew J Gamble7,5, David Shechter1
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461.
2Contributed equally.
3Current address: Department of Medicine, Weill Cornell Medical College, 1300 York Ave, New York, NY 10065.
4Department of Oncology, Albert Einstein College of Medicine, Bronx, NY 10461.
5Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461.
6Current address: Enveda Biosciences, Boulder, Colorado, 80301, United States.
7Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461.
PubMed PMC DOI PDF

Abstract

Protein Arginine Methyltransferase 5 (PRMT5) regulates RNA splicing and transcription by symmetric dimethylation of arginine residues (Rme2s/SDMA) in many RNA binding proteins. However, the mechanism by which PRMT5 couples splicing to transcriptional output is unknown. Here, we demonstrate that a major function of PRMT5 activity is to promote chromatin escape of a novel, large class of mRNAs that…

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