Skip to main content
Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2007 Jun 29;64(18):2404–2412. doi: 10.1007/s00018-007-7160-5

tRNase Z: the end is not in sight

B Späth 1, G Canino 1, A Marchfelder 1,
PMCID: PMC11138456  PMID: 17599240

Abstract.

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.

Keywords. tRNase Z, metallo-β-lactamases, bpNPP, tRNA processing, ribonuclease

Footnotes

Received 29 March 2007; received after revision 15 May 2007; accepted 21 May 2007


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

RESOURCES