Detection of 3'-end RNA uridylation with a protein nanopore

ACS Nano. 2014 Feb 25;8(2):1364-74. doi: 10.1021/nn4050479. Epub 2013 Dec 31.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3' Untranslated Regions*
  • Binding Sites
  • Nanopores*
  • Proteins / chemistry*
  • RNA / chemistry*
  • RNA Processing, Post-Transcriptional
  • Uridine / chemistry*

Substances

  • 3' Untranslated Regions
  • Proteins
  • RNA
  • Uridine