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

Terumichi Tanaka*, Tomoaki Ando, Shinnosuke Haga, Yo Kikuchi

*この研究の対応する著者

研究成果: Article査読

7 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)1388-1392
ページ数5
ジャーナルBioscience, Biotechnology and Biochemistry
68
6
DOI
出版ステータスPublished - 2004 6月
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

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