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Article Dans Une Revue Nature Structural and Molecular Biology Année : 2006

Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA

Résumé

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

Dates et versions

hal-03347756 , version 1 (17-09-2021)

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Inès Li de La Sierra-Gallay, Nathalie Mathy, Olivier Pellegrini, Ciarán Condon. Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA. Nature Structural and Molecular Biology, 2006, 13 (4), pp.376-377. ⟨10.1038/nsmb1066⟩. ⟨hal-03347756⟩
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