Interaction of RNAse P from Escherichia coli with pseudoknotted structures in viral RNAs

Ruud M.W. Mans, Cecilia Guerrier-Takada, Sidney Altman, Cornelis W.A. Pieij

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

In a previous study it was shown that RNase P from E. coli cleaves the tRNA-like structure of turnip yellow mosaic virus (TYMV) RNA in vitro (Guerrier-Takada et al. (1988) Cell, 53, 267-272). Cleavage takes place at the 3' side of the loop that crosses the deep groove of the pseudoknot structure present in the aminoacyl acceptor domain. In the present study fragments of TYMV RNA with mutations in the pseudoknot, generated by transcription in vitro, were tested for susceptibility to cleavage by RNase P. Changes in the specificity with respect to the site of cleavage and decreases in the rate of cleavage were observed with most of these substrates. The behaviour of various mutants in the reaction catalyzed by RNase P is in agreement with the present model of the TYMV RNA pseudoknot (Dumas et al. (1987), J. Biomol. Struct Dyn. 263, 652 - 657). Base substitutions in the loop that crosses the shallow groove of the pseudoknot structure resulted, however, in an unexpected decrease in the rate of cleavage, probably due to conformational changes in the substrates. Studies on other tRNA-like structures revealed an important role in the reaction with RNase P for both the nucleotide at the 3' side of the loop that spans the deep groove and the nucleotide at position 4, which correspond to positions -1 and 73, respectively, in tRNA precursors.

Original languageEnglish (US)
Pages (from-to)3479-3487
Number of pages9
JournalNucleic acids research
Volume18
Issue number12
DOIs
StatePublished - Jun 25 1990
Externally publishedYes

ASJC Scopus subject areas

  • Genetics

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