TITLE

tRNase Z: the end is not in sight

AUTHOR(S)
Späth, B.; Canino, G.; Marchfelder, A.
PUB. DATE
September 2007
SOURCE
Cellular & Molecular Life Sciences;Sep2007, Vol. 64 Issue 18, p2404
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
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.
ACCESSION #
26530281

 

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