RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis

Elias Seif, Sidney Altman

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


RNase P from Bacillus subtilis cleaves in vitro the adenine riboswitch upstream of pbuE, which codes for an adenine efflux pump. The guanine riboswitch, encoded upstream of xpt-pbuX operon, is not cleaved. The cleavage sites do not occur at any predicted structures that should be recognized by RNase P in the theoretical model of the adenine riboswitch. However, it is possible to draw alternative secondary structure models that match the apparent requirements for RNase P substrates at these cleavage sites. Support for these models is provided by appropriate mutagenesis experiments. Adenine showed no effect on the cleavage in vitro of the pbuE adenine riboswitch by RNase P holoenzyme from B. subtilis. The results of genetic experiments performed in B. subtilis support the cleavage of adenine riboswitch by RNase P in vivo and suggest that it induces the stabilization of pbuE mRNA under normal conditions. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1237-1243
Number of pages7
Issue number6
StatePublished - Jun 2008
Externally publishedYes


  • Purines
  • RNA enzyme
  • RNA processing
  • Transient structures

ASJC Scopus subject areas

  • Molecular Biology


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