| Autor: |
Späth, Bettina, Schubert, Sylvia, Lieberoth, Annika, Settele, Florian, Schütz, Stefanie, Fischer, Susan, Marchfelder, Anita |
| Předmět: |
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| Zdroj: |
Archives of Microbiology; Sep2008, Vol. 190 Issue 3, p301-308, 8p, 1 Black and White Photograph, 4 Diagrams, 3 Charts |
| Abstrakt: |
The endoribonuclease tRNase Z plays an essential role in tRNA metabolism by removal of the 3′ trailer element of precursor RNAs. To investigate tRNA processing in archaea, we identified and expressed the tRNase Z from Haloferax volcanii, a halophilic archaeon. The recombinant enzyme is a homodimer and efficiently processes precursor tRNAs. Although the protein is active in vivo at 2–4 M KCl, it is inhibited by high KCl concentrations in vitro, whereas 2–3 M (NH4)2SO4 do not inhibit tRNA processing. Analysis of the metal content of the metal depleted tRNase Z revealed that it still contains 0.4 Zn2+ ions per dimer. In addition tRNase Z requires Mn2+ ions for processing activity. We compared the halophilic tRNase Z to the homologous one from Pyrococcus furiosus, a thermophilic archaeon. Although both enzymes have 46% sequence similarity, they differ in their optimal reaction conditions. Both archaeal tRNase Z proteins process mitochondrial pre-tRNAs. Only the thermophilic tRNase Z shows in addition activity toward intron containing pre-tRNAs, 5′ extended precursors, the phosphodiester bis( p-nitrophenyl)phosphate (bpNPP) and the glyoxalase II substrate S- d-lactoylglutathion (SLG). [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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