Abstract:
:E2F is a family of master transcription regulators involved in mediating diverse cell fates. Here, we show that residue-specific arginine methylation (meR) by PRMT5 enables E2F1 to regulate many genes at the level of alternative RNA splicing, rather than through its classical transcription-based mechanism. The p100/TSN tudor domain protein reads the meR mark on chromatin-bound E2F1, allowing snRNA components of the splicing machinery to assemble with E2F1. A large set of RNAs including spliced variants associate with E2F1 by virtue of the methyl mark. By focusing on the deSUMOylase SENP7 gene, which we identified as an E2F target gene, we establish that alternative splicing is functionally important for E2F1 activity. Our results reveal an unexpected consequence of arginine methylation, where reader-writer interplay widens the mechanism of control by E2F1, from transcription factor to regulator of alternative RNA splicing, thereby extending the genomic landscape under E2F1 control.
journal_name
Sci Advjournal_title
Science advancesauthors
Roworth AP,Carr SM,Liu G,Barczak W,Miller RL,Munro S,Kanapin A,Samsonova A,La Thangue NBdoi
10.1126/sciadv.aaw4640subject
Has Abstractpub_date
2019-06-26 00:00:00pages
eaaw4640issue
6issn
2375-2548pii
aaw4640journal_volume
5pub_type
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