Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA.
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.
Li de la Sierra-Gallay
Inés
I
Centre National de la Recherche (CNRS) FRC550, Institut de Biologie Physico-Chimique, Paris, France.
Mathy
Nathalie
N
Pellegrini
Olivier
O
Condon
Ciarán
C
D001412:Bacillus subtilis / Q000378:metabolism; D020134:Catalytic Domain; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism; D046911:Macromolecular Substances; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012323:RNA Processing, Post-Transcriptional; D012329:RNA, Bacterial / Q000737:chemistry* / Q000378:metabolism; D012363:RNA, Transfer, Thr / Q000737:chemistry* / Q000378:metabolism
D046911:Macromolecular Substances; D012329:RNA, Bacterial; D012363:RNA, Transfer, Thr; D004722:Endoribonucleases; C110250:RNase Z