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tRNase Z: the end is not in sight

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 64, Issue 18, Pages 2404-2412

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-007-7160-5

Keywords

tRNase Z; metallo-beta-lactamases; bpNPP; tRNA processing; ribonuclease

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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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