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Updated: Aug 11, 2026

Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
Published on: May 3, 2014
Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA
Inés Li de la Sierra-Gallay1, Nathalie Mathy, Olivier Pellegrini
1Centre National de la Recherche (CNRS) FRC550, Institut de Biologie Physico-Chimique, Paris, France.
Abstract:
The highly conserved ribonuclease RNase Z catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Here we present the structure of the complex between Bacillus subtilis RNase Z and tRNA(Thr), the first structure of a ribonucleolytic processing enzyme bound to tRNA. Binding of tRNA to RNase Z causes conformational changes in both partners to promote reorganization of the catalytic site and tRNA cleavage.
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