title: Detection of 3'-end RNA uridylation with a protein nanopore.
abstract: Post-transcriptional modifications of the 3'-ends of RNA molecules have a profound impact on their stability and processing in the cell. Uridylation, the addition of uridines to 3'-ends, has recently been found to be an important regulatory signal to stabilize the tagged molecules or to direct them toward degradation. Simple and cost-effective methods for the detection of this post-transcriptional modification are not yet available. Here, we demonstrate the selective and transient binding of 3'-uridylated ssRNAs inside the β barrel of the staphylococcal α-hemolysin (αHL) nanopore and investigate the molecular basis of uridine recognition by the pore. We show the discrimination of 3'-oligouridine tails on the basis of their lengths and propose the αHL nanopore as a useful sensor for this biologically relevant RNA modification.
authors.affiliation: Department of Chemistry, University of Oxford , 12 Mansfield Road, Oxford OX1 3TA, United Kingdom.
authors.forename: Massimiliano
authors.initials: M
authors.lastname: Clamer
authors.forename: Lajos
authors.initials: L
authors.lastname: Höfler
authors.forename: Ellina
authors.initials: E
authors.lastname: Mikhailova
authors.forename: Gabriella
authors.initials: G
authors.lastname: Viero
authors.forename: Hagan
authors.initials: H
authors.lastname: Bayley
mesh_terms: D020413:3' Untranslated Regions; D001665:Binding Sites; D058608:Nanopores; D011506:Proteins / Q000737:chemistry*; D012313:RNA / Q000737:chemistry*; D012323:RNA Processing, Post-Transcriptional; D014529:Uridine / Q000737:chemistry*
chemical_list: D020413:3' Untranslated Regions; D011506:Proteins; D012313:RNA; D014529:Uridine