Human tyrosine tRNA is also internally cleavable by E. coli ribonuclease P RNA ribozyme in vitro

Tomoaki Ando, Terumichi Tanaka*, Yoshiaki Hori, Etsuko Sakai, Yo Kikuchi

*この研究の対応する著者

研究成果: Article査読

10 被引用数 (Scopus)

抄録

Transfer RNA is an essential molecule for biological system, and each (RNA molecule commonly has a cloverleaf structure. Previously, we experimentally showed that some Drosophila tRNA (tRNAAla, tRNAHis, and tRNAMet 1) molecules fit to form another, non-cloverleaf, structure in which the 3′-half of the tRNA molecules forms an alternative hairpin, and that the tRNA molecules are internally cleaved by the catalytic RNA of bacterial ribonuclease P (RNase P). Until now, the hyperprocessing reaction of tRNA has only been reported with Drosophila tRNAs. This time, we applied the hyperprocessing reaction to one of human tRNAs, human tyrosine tRNA, and we showed that this tRNA was also hyperprocessed by E. coli RNase P RNA. This tRNA is the first example for hyperprocessed non-Drosophila tRNAs. The results suggest that the hyperprocessing reaction can be a useful tool to detect destablized tRNA molecules from any species.

本文言語English
ページ(範囲)2798-2801
ページ数4
ジャーナルBioscience, Biotechnology and Biochemistry
65
12
DOI
出版ステータスPublished - 2001 12
外部発表はい

ASJC Scopus subject areas

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

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