SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination

Dorothy Yanling Zhao, Gerald Gish, Ulrich Braunschweig, Yue Li, Zuyao Ni, Frank W. Schmitges, Guoqing Zhong, Ke Liu, Weiguo Li, Jason Moffat, Masoud Vedadi, Jinrong Min, Tony J. Pawson, Benjamin J. Blencowe and Jack F. Greenblatt ()
Additional contact information
Dorothy Yanling Zhao: Donnelly Centre, University of Toronto
Gerald Gish: Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Ulrich Braunschweig: Donnelly Centre, University of Toronto
Yue Li: Donnelly Centre, University of Toronto
Zuyao Ni: Donnelly Centre, University of Toronto
Frank W. Schmitges: Donnelly Centre, University of Toronto
Guoqing Zhong: Donnelly Centre, University of Toronto
Ke Liu: Structural Genomics Consortium, University of Toronto
Weiguo Li: Structural Genomics Consortium, University of Toronto
Jason Moffat: Donnelly Centre, University of Toronto
Masoud Vedadi: Structural Genomics Consortium, University of Toronto
Jinrong Min: Structural Genomics Consortium, University of Toronto
Tony J. Pawson: Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue
Benjamin J. Blencowe: Donnelly Centre, University of Toronto
Jack F. Greenblatt: Donnelly Centre, University of Toronto

Nature, 2016, vol. 529, issue 7584, 48-53

Abstract: Abstract The carboxy-terminal domain (CTD) of the RNA polymerase II (RNAP II) subunit POLR2A is a platform for modifications specifying the recruitment of factors that regulate transcription, mRNA processing, and chromatin remodelling. Here we show that a CTD arginine residue (R1810 in human) that is conserved across vertebrates is symmetrically dimethylated (me2s). This R1810me2s modification requires protein arginine methyltransferase 5 (PRMT5) and recruits the Tudor domain of the survival of motor neuron (SMN, also known as GEMIN1) protein, which is mutated in spinal muscular atrophy. SMN interacts with senataxin, which is sometimes mutated in ataxia oculomotor apraxia type 2 and amyotrophic lateral sclerosis. Because POLR2A R1810me2s and SMN, like senataxin, are required for resolving RNA–DNA hybrids created by RNA polymerase II that form R-loops in transcription termination regions, we propose that R1810me2s, SMN, and senataxin are components of an R-loop resolution pathway. Defects in this pathway can influence transcription termination and may contribute to neurodegenerative disorders.

Date: 2016
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DOI: 10.1038/nature16469

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