tRNase Z: the end is not in sight

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. Anoth...

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Veröffentlicht in:	Cellular and molecular life sciences : CMLS 2007-09, Vol.64 (18), p.2404-2412
Hauptverfasser:	Späth, B, Canino, G, Marchfelder, A
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteria - enzymology Bacteria - metabolism bpNPP Endoribonucleases - chemistry Endoribonucleases - metabolism Enzymes Eukaryotes metallo-β-lactamases Molecular biology Prokaryotes Review ribonuclease RNA Processing, Post-Transcriptional RNA, Transfer - metabolism Substrates tRNA processing tRNase Z
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Zusammenfassung:	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.
ISSN:	1420-682X 1420-9071
DOI:	10.1007/s00018-007-7160-5