The protein component of bacterial ribonuclease P flickers the metal ion response to the substrate shape preference of the ribozyme

Tomoaki Ando, Terumichi Tanaka, Yo Kikuchi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The substrate shape specificity of the Escherichia coli ribonuclease P (RNase P) ribozyme depends on the concentration of magnesium ion. At 10 mM or more, it can cleave a hairpin substrate as well as a cloverleaf pre-transfer RNA (tRNA). The results showed, however, that the holo enzyme cleaved the hairpin substrate at low concentrations of magnesium ion. Considering that the homologous E. coli tRNAs are resistant to internal cleavage by the RNase P, the phenomena suggest that this catalytic activity might take part in the removing the mis-folded RNAs in the cell.

Original languageEnglish
Pages (from-to)2294-2296
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume67
Issue number10
DOIs
Publication statusPublished - 2003 Oct
Externally publishedYes

Fingerprint

Ribonuclease P
Catalytic RNA
Bacterial Proteins
ribonucleases
Transfer RNA
metal ions
Magnesium
Metal ions
magnesium
Metals
Ions
ions
Escherichia coli
Proteins
transfer RNA
Substrates
Substrate Specificity
catalytic activity
proteins
RNA

Keywords

  • Escherichia coli
  • Holo enzyme
  • Ribonuclease P
  • Ribozyme
  • Specificity

ASJC Scopus subject areas

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

Cite this

The protein component of bacterial ribonuclease P flickers the metal ion response to the substrate shape preference of the ribozyme. / Ando, Tomoaki; Tanaka, Terumichi; Kikuchi, Yo.

In: Bioscience, Biotechnology and Biochemistry, Vol. 67, No. 10, 10.2003, p. 2294-2296.

Research output: Contribution to journalArticle

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