Examining the bases of the J3/4 domain of Escherichia coli ribonuclease P

Terumichi Tanaka, Tomoaki Ando, Shinnosuke Haga, Yo Kikuchi

Research output: Contribution to journalArticle

7 Citations (Scopus)


We prepared several mutants of the J3/4 and P4 domains of Escherichia coli ribonuclease P (RNase P): A62G, A62U, G63C/G64C, A65G, A67G, U69A, U69G, U69C, U69Δ, and U69UU. Comparison of the ribozyme and holo enzyme reactions at various concentrations of magnesium ions showed that the presence of a bulge at U69 in the P4 domain was important in the holo enzyme. The results also showed that the conserved bases G63 and G64 in the J3/4 domain were important for efficient ribozyme reactions but were replaceable in the presence of the protein component. Our data showed that the bases in the J3/4 and P4 domains displayed different responses to the metal ions that were affected by the presence of the protein component.

Original languageEnglish
Pages (from-to)1388-1392
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Issue number6
Publication statusPublished - 2004 Jun
Externally publishedYes



  • C5 protein
  • Escherichia coli
  • M1 RNA
  • Ribonuclease P (RNase P)
  • Ribozyme

ASJC Scopus subject areas

  • Food Science
  • Applied Microbiology and Biotechnology
  • Chemistry (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology

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