Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes

Tomoaki Ando, Terumichi Tanaka, Yo Kikuchi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Previously, we reported that the substrate shape recognition of the Escherichia coli ribonuclease (RNase) P ribozyme depends on the concentration of magnesium ion in vitro. We additionally examined the Bacillus subtilis RNase P ribozyme and found that the B. subtilis enzyme also required high magnesium ion, above 10 mM, for cleavage of a hairpin substrate. The results of kinetic studies showed that the metal ion concentration affected both the catalysis and the affinity of the ribozymes toward a hairpin RNA substrate.

Original languageEnglish
Pages (from-to)1825-1827
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume67
Issue number8
Publication statusPublished - 2003 Aug
Externally publishedYes

Fingerprint

Ribonuclease P
Catalytic RNA
ribonucleases
Bacilli
Bacillus subtilis
Escherichia coli
magnesium
Ions
ions
Magnesium
Substrates
metal ions
catalytic activity
RNA
Catalysis
kinetics
Metal ions
Enzymes
enzymes
Metals

Keywords

  • Bacillus
  • Ribonuclease P
  • Ribozyme
  • Specificity
  • Transfer RNA

ASJC Scopus subject areas

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

Cite this

Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes. / Ando, Tomoaki; Tanaka, Terumichi; Kikuchi, Yo.

In: Bioscience, Biotechnology and Biochemistry, Vol. 67, No. 8, 08.2003, p. 1825-1827.

Research output: Contribution to journalArticle

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