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Published online before print April 25, 2008
RNA, DOI: 10.1261/rna.833408
 Copyright © 2008 RNA Society
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RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis

Elias Seif1 and Sidney Altman

Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA

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.

Keywords: transient structures; RNA enzyme; RNA processing; purines

Received September 20, 2007 ; accepted March 13, 2008.

1 Present address: Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.

Reprint requests to: Sidney Altman, Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven CT 06520, USA; e-mail: sidney.altman{at}yale.edu; fax: (203) 432-5713.

Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.833408.


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