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

研究成果: Article査読

5 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)2294-2296
ページ数3
ジャーナルBioscience, Biotechnology and Biochemistry
67
10
DOI
出版ステータスPublished - 2003 10
外部発表はい

ASJC Scopus subject areas

  • 食品科学
  • 応用微生物学とバイオテクノロジー
  • 化学(その他)
  • 生化学、遺伝学、分子生物学(全般)
  • 生化学
  • バイオテクノロジー
  • バイオエンジニアリング

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