Polymerase-Mediated Site-Specific Incorporation of a Synthetic Fluorescent Isomorphic G Surrogate into RNA

Angew Chem Int Ed Engl. 2017 Jan 24;56(5):1303-1307. doi: 10.1002/anie.201609327. Epub 2016 Dec 21.

Abstract

An enzyme-mediated approach for the assembly of singly modified RNA constructs in which specific G residues are replaced with th G, an emissive isomorphic G surrogate, is reported. Transcription in the presence of th G and native nucleoside triphosphates enforces initiation with the unnatural analogue, yielding 5'-end modified transcripts that can be mono-phosphorylated and ligated to provide longer site-specifically modified RNA constructs. The scope of this unprecedented enzymatic approach to non-canonical purine-containing RNAs is explored via the assembly of several altered hammerhead (HH) ribozymes and a singly modified HH substrate. By strategically modifying key positions, a mechanistic insight into the ribozyme-mediated cleavage is gained. Additionally, the emissive features of the modified nucleoside and its responsiveness to environmental changes can be used to monitor cleavage in real time by steady state fluorescence spectroscopy.

Keywords: RNA; fluorescence; hammerhead ribozyme; nucleosides; transcription initiation.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Base Sequence
  • DNA-Directed RNA Polymerases / metabolism*
  • Fluorescent Dyes / chemistry*
  • Guanosine / chemistry
  • Guanosine / metabolism*
  • Nucleic Acid Conformation
  • RNA / metabolism*
  • RNA, Catalytic / metabolism
  • Substrate Specificity
  • Viral Proteins / metabolism*

Substances

  • Fluorescent Dyes
  • RNA, Catalytic
  • Viral Proteins
  • hammerhead ribozyme
  • Guanosine
  • RNA
  • bacteriophage T7 RNA polymerase
  • DNA-Directed RNA Polymerases