Mammalian Y RNAs are modified at discrete guanosine residues with N-glycans
Ryan A. Flynn,
Benjamin A. H. Smith,
Alex G. Johnson,
Benson M. George,
Stacy A. Malaker,
Jan E. Carette,
Carolyn R. Bertozzi
Posted 30 Sep 2019
bioRxiv DOI: 10.1101/787614
Posted 30 Sep 2019
Glycans modify lipids and proteins to mediate inter- and intramolecular interactions across all domains of life. RNA, another multifaceted biopolymer, is not thought to be a major target of glycosylation. Here, we challenge this view with evidence that mammalian cells use RNA as a third scaffold for glycosylation in the secretory pathway. Using a battery of chemical and biochemical approaches, we find that a select group of small noncoding RNAs including Y RNAs are modified with complex, sialylated N-glycans (glycoRNAs). These glycoRNA are present in multiple cell types and mammalian species, both in cultured cells and in vivo. Finally, we find that RNA glycosylation depends on the canonical N-glycan biosynthetic machinery within the ER/Golgi luminal spaces. Collectively, these findings suggest the existence of a ubiquitous interface of RNA biology and glycobiology suggesting an expanded role for glycosylation beyond canonical lipid and protein scaffolds.
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