抄録
We showed previously that the bacterial ribonuclease P (RNase P) ribozyme has substrate shape preference depending on the concentrations of catalytically important magnesium ions. The ribozyme discriminates a canonical cloverleaf precursor tRNA from a hairpin RNA with a CCA-tag sequence at low concentrations of magnesium ions. By detailed analysis of the shape preference using the bottom-half part-shifting variants of a tRNA precursor, we showed that the RNAs in a T-shape structure can be substrates for the ribozyme reactions even at low concentrations of magnesium ions, and that the RNA in a natural L-shape is the best substrate for both the ribozyme and the holo enzyme. The results also showed that the position of the bottom-half part did not affect the cleavage site selection of a substrate by the enzyme. Our results are the first kinetic evidence to show the importance of the bottom-half part of tRNA molecule, and our result also showed that the holo enzyme can discriminate substrate shape as well as the ribozyme at low concentrations of metal ions.
本文言語 | English |
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ページ(範囲) | 1992-1994 |
ページ数 | 3 |
ジャーナル | Bioscience, Biotechnology and Biochemistry |
巻 | 69 |
号 | 10 |
DOI | |
出版ステータス | Published - 2005 10月 23 |
外部発表 | はい |
ASJC Scopus subject areas
- バイオエンジニアリング
- バイオテクノロジー
- 生化学
- 生化学、遺伝学、分子生物学(全般)
- 化学(その他)
- 応用微生物学とバイオテクノロジー
- 食品科学