Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli

Agustín Vioque, John Arnez, Sidney Altman

Research output: Contribution to journalArticle

142 Scopus citations

Abstract

The genes for the protein (C5 protein) and RNA (M1 RNA) subunits of Escherichia coli RNase P have been subcloned and their products prepared in milligram quantities by rapid procedures. The interactions between the two subunits of the enzyme have been studied in vitro by a filter-binding technique. The stoichiometry of the subunits in the holoenzyme is 1:1. The dissociation constant for the specific interactions of the subunits in the holoenzyme complex is ~4 × 10-10 m. C5 protein also interacts with various RNA molecules in a non-specific manner with a dissociation constant of 2 × 10-8 to 6 × 10-8 m. Regions of M1 RNA required for interaction with C5 protein have been defined by deletion analysis and footprinting techniques. These interactions are localized primarily between nucleotides 82 to 96 and 170 to 270 of M1 RNA.

Original languageEnglish (US)
Pages (from-to)835-848
Number of pages14
JournalJournal of molecular biology
Volume202
Issue number4
DOIs
StatePublished - Aug 20 1988
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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