RNase P cleaves transient structures in some riboswitches

Sidney Altman, Donna Wesolowski, Cecilia Guerrier-Takada, Yong Li

Research output: Contribution to journalArticlepeer-review

70 Scopus citations

Abstract

RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. The cleavage sites do not occur in any recognizable structure, as judged from theoretical schemes that have been drawn for these 5′ UTRs. However, it is possible to draw a scheme that is a good representation of the E. coli cleavage site for RNase P and for the cleavage site in B. subtilis. These data indicate that transient structures are important in RNase P cleavage and in riboswitch function. Coenzyme B12 has a small inhibitory effect on E. coli RNase P cleavage of the E. coli riboswitch. Both E. coli RNase P and a partially purified RNase P from Aspergillus nidulans mycelia succeeded in cleaving a putative arginine riboswitch from A. nidulans. The cleavage site may be a representative of another model substrate for eukaryotic RNase P. This 5′ UTR controls splicing of the arginase mRNA in A. nidulans. Four other riboswitches in E. coli were not cleaved by RNase P under the conditions tested.

Original languageEnglish (US)
Pages (from-to)11284-11289
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number32
DOIs
StatePublished - Aug 9 2005
Externally publishedYes

Keywords

  • Arginase
  • Aspergillus nidulans
  • Bacillus subtilis
  • Coenzyme B12
  • Escherichia coli

ASJC Scopus subject areas

  • General

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