tRNase Z: the end is not in sight

Cell Mol Life Sci. 2007 Sep;64(18):2404-12. doi: 10.1007/s00018-007-7160-5.


Although the enzyme tRNase Z has only recently been isolated, a plethora of data has already been acquired concerning the enzyme. tRNase Z is the endonuclease that catalyzes the removal of the tRNA 3' trailer, yielding the mature tRNA 3' end ready for CCA addition and aminoacylation. Another substrate cleaved by tRNase Z is the small chromogenic phosphodiester bis(p-nitrophenyl)phosphate (bpNPP), which is the smallest tRNase Z substrate known so far. Hitherto the biological function as tRNA 3'-end processing enzyme has been shown only in one prokaryotic and one eukaryotic organism, respectively. This review summarizes the present information concerning the two tRNase Z substrates pre-tRNA and bpNPP, as well as the metal requirements of tRNase Z enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacteria / enzymology*
  • Bacteria / metabolism
  • Endoribonucleases / chemistry*
  • Endoribonucleases / metabolism*
  • RNA Processing, Post-Transcriptional
  • RNA, Transfer / metabolism*


  • RNA, Transfer
  • Endoribonucleases