Matrix-assisted laser desorption/ionization mass spectrometry (MALDI) of endonuclease digests of RNA

Nucleic Acids Res. 1997 May 15;25(10):1957-64. doi: 10.1093/nar/25.10.1957.

Abstract

The determination of RNA sequences using base- specific enzymatic cleavages is a well established method. Different synthetic RNA molecules were analyzed for uniformity of degradation by RNase T1, U2, A and PhyM under reaction conditions compatible with Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry (MALDI-MS), to identify the positions of G, A and pyrimidine residues. In order to get a complete set of fragments derived from cleavage at every phosphodiester bond, the samples were also subjected to a limited alkaline hydrolysis. Additionally, the 5'-terminus fragments of a 49mer RNA transcript were isolated by way of 5'-biotinylation and streptavidin-coated magnetic beads (Dynal), followed by a RNase U2digestion. MALDI-MS of the generated fragments is presented as an efficient technique for a direct read out of the nucleotide sequence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspergillus oryzae / enzymology
  • Base Sequence
  • Cattle
  • Chickens
  • Liver / enzymology
  • Molecular Sequence Data
  • Oligoribonucleotides / chemical synthesis
  • Oligoribonucleotides / chemistry*
  • Pancreas / enzymology
  • Physarum / enzymology
  • Plants
  • RNA / biosynthesis
  • RNA / chemistry*
  • Ribonuclease T1 / metabolism
  • Ribonucleases / metabolism*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*
  • Substrate Specificity
  • Transcription, Genetic
  • Ustilago / enzymology

Substances

  • Oligoribonucleotides
  • RNA
  • Ribonucleases
  • Ribonuclease T1