Recent approaches to probe functional groups in ribonuclease P RNA by modification interference

Mol Biol Rep. 1995;22(2-3):161-9. doi: 10.1007/BF00988723.

Abstract

Modification interference is a powerful method to identify important functional groups in RNA molecules. We review here recent developments of techniques to screen for chemical modifications that interfere with (i) binding of (pre-)tRNA to bacterial RNase P RNA or (ii) pre-tRNA cleavage by this ribozyme. For example, two studies have analyzed positions at which a substitution of sulfur for the pro-Rp oxygen affects tRNA binding [1] or catalysis [2]. The results emphasize the functional key role of a central core element present in all known RNase P RNA subunits. The four sulfur substitutions identified in one study [2] to inhibit the catalytic step also interfered with binding of tRNA to E. coli RNase P RNA [1]. This suggests that losses in binding energy due to the modification at these positions affect the enzyme-substrate and the enzyme-transition state complex. In addition, the two studies have revealed, for the first time, sites of direct metal ion coordination in RNase P RNA. The potentials, limitations and interpretational ambiguities of modification interference experiments as well as factors influencing their outcome are discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Base Sequence
  • Binding Sites
  • Endoribonucleases / chemistry*
  • Endoribonucleases / metabolism*
  • Escherichia coli / enzymology
  • Escherichia coli Proteins*
  • Kinetics
  • Molecular Sequence Data
  • Nucleic Acid Conformation*
  • RNA Precursors / metabolism
  • RNA, Bacterial / chemistry*
  • RNA, Bacterial / metabolism
  • RNA, Catalytic / chemistry*
  • RNA, Catalytic / metabolism*
  • RNA, Transfer / biosynthesis
  • Ribonuclease P
  • Substrate Specificity

Substances

  • Escherichia coli Proteins
  • RNA Precursors
  • RNA, Bacterial
  • RNA, Catalytic
  • RNA, Transfer
  • Endoribonucleases
  • Ribonuclease P
  • ribonuclease P, E coli