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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)2798-2801
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Issue number12
Publication statusPublished - 2001 Dec
Externally publishedYes


  • Escherichia coli
  • Hyperprocessing
  • RNase P
  • tRNA
  • Tyrosine

ASJC Scopus subject areas

  • Food Science
  • General Biochemistry,Genetics and Molecular Biology
  • Biochemistry
  • Biotechnology
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Bioengineering


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