Improving CMC-derivatization of pseudouridine in RNA for mass spectrometric detection

Anal Chim Acta. 2008 Apr 7;612(2):173-81. doi: 10.1016/j.aca.2008.02.026. Epub 2008 Feb 17.

Abstract

A protocol that utilizes matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and N-cyclohexyl-N'-beta-(4-methylmorpholinium)ethylcarbodiimide (CMC) derivatization to detect the post-transcriptionally modified nucleoside, pseudouridine, in RNA has been optimized for RNase digests. Because pseudouridine is mass-silent (i.e., the mass of pseudouridine is the same as the mass of uridine), after CMC-derivatization and alkaline treatment, all pseudouridine residues exhibit a mass shift of 252 Da that allows its presence to be easily detected by mass spectrometry. This protocol is illustrated by the direct MALDI-MS identification of pseudouridines within Escherichia coli tRNA(TyrII) starting from microgram amounts of sample. During this optimization study, it was discovered that the post-transcriptionally modified nucleoside 2-methylthio-N(6)-isopentenyladenosine, which is present in bacterial tRNAs, also retains a CMC unit after derivatization and incubation with base. Thus, care must be exercised when applying this MALDI-based CMC-derivatization approach for pseudouridine detection to samples containing transfer RNAs to minimize the misidentification of pseudouridine.

Publication types

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

MeSH terms

  • Escherichia coli / genetics
  • Exonucleases / metabolism
  • Imides / chemistry*
  • Morpholines / chemistry*
  • Oligonucleotides / analysis
  • Oligonucleotides / chemistry
  • Pseudouridine / chemistry*
  • RNA / analysis*
  • RNA / chemistry*
  • RNA / metabolism
  • Ribonuclease T1 / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*

Substances

  • Imides
  • Morpholines
  • N-cyclohexyl-N'-beta-(4-methylmorpholinium)ethylcarbodiimide
  • Oligonucleotides
  • Pseudouridine
  • RNA
  • Exonucleases
  • Ribonuclease T1