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Journal articles

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

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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https://hal-cnrs.archives-ouvertes.fr/hal-03347756
Contributor : Nathalie Mathy-Franchet Connect in order to contact the contributor
Submitted on : Friday, September 17, 2021 - 2:39:47 PM
Last modification on : Wednesday, February 9, 2022 - 3:46:11 AM

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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, Nature Publishing Group, 2006, 13 (4), pp.376-377. ⟨10.1038/nsmb1066⟩. ⟨hal-03347756⟩

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