Identification of Nucleotide Residues Essential for RNase P Activity from the Hyperthermophilic Archaeon<i>Pyrococcus horikoshii</i>OT3

DOI Web Site Web Site 被引用文献3件 参考文献25件
  • TERADA Atsushi
    Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University
  • YOSHIDA Takeshi
    Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University
  • KIMURA Makoto
    Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University

書誌事項

タイトル別名
  • Identification of Nucleotide Residues Essential for RNase P Activity from the Hyperthermophilic Archaeon Pyrococcus horikoshii OT3
  • Identification of nucleotide residues essential for RNase P activity from the hyperthermophilic archaeaon Pyrococcus horikoshii OT3

この論文をさがす

抄録

Ribonuclease P (RNase P) is involved in the processing of the 5′ leader sequence of precursor tRNA (pre-tRNA). We have found that RNase P RNA (PhopRNA) and five proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) reconstitute RNase P activity with enzymatic properties similar to those of the authentic ribozyme from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. We report here that nucleotides A40, A41, and U44 at helix P4, and G269 and G270 located at L15/16 in PhopRNA, are, like the corresponding residues in Esherichia coli RNase P RNA (M1RNA), involved in hydrolysis by coordinating catalytic Mg2+ ions, and in the recognition of the acceptor end (CCA) of pre-tRNA by base-pairing, respectively. The information reported here strongly suggests that PhopRNA catalyzes the hydrolysis of pre-tRNA in approximately the same manner as eubacterial RNase P RNAs, even though it has no enzymatic activity in the absence of the proteins.

収録刊行物

被引用文献 (3)*注記

もっと見る

参考文献 (25)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ