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.
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Received 29 March 2007; received after revision 15 May 2007; accepted 21 May 2007
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Späth, B., Canino, G. & Marchfelder, A. tRNase Z: the end is not in sight. Cell. Mol. Life Sci. 64, 2404–2412 (2007). https://doi.org/10.1007/s00018-007-7160-5
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DOI: https://doi.org/10.1007/s00018-007-7160-5