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

Inés Li de la Sierra-Gallay; Nathalie Mathy; Olivier Pellegrini; Ciarán Condon

doi:10.1038/nsmb1066

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

Nat Struct Mol Biol. 2006 Apr;13(4):376-7. doi: 10.1038/nsmb1066. Epub 2006 Mar 5.

Authors

Inés Li de la Sierra-Gallay¹, Nathalie Mathy, Olivier Pellegrini, Ciarán Condon

Affiliation

¹ Centre National de la Recherche (CNRS) FRC550, Institut de Biologie Physico-Chimique, Paris, France.

PMID: 16518398
DOI: 10.1038/nsmb1066

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillus subtilis / metabolism
Catalytic Domain
Endoribonucleases / chemistry*
Endoribonucleases / metabolism
Macromolecular Substances
Models, Molecular
Nucleic Acid Conformation
Protein Conformation
RNA Processing, Post-Transcriptional
RNA, Bacterial / chemistry*
RNA, Bacterial / metabolism
RNA, Transfer, Thr / chemistry*
RNA, Transfer, Thr / metabolism

Substances

Macromolecular Substances
RNA, Bacterial
RNA, Transfer, Thr
Endoribonucleases
RNase Z

Associated data

PDB/1EHZ
PDB/1Y44
PDB/2FK6