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

Authors :
Li de la Sierra-Gallay I
Mathy N
Pellegrini O
Condon C
Source :
Nature structural & molecular biology [Nat Struct Mol Biol] 2006 Apr; Vol. 13 (4), pp. 376-7. Date of Electronic Publication: 2006 Mar 05.
Publication Year :
2006

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.

Subjects

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

Details

Language :
English
ISSN :
1545-9993
Volume :
13
Issue :
4
Database :
MEDLINE
Journal :
Nature structural & molecular biology
Publication Type :
Academic Journal
Accession number :
16518398
Full Text :
https://doi.org/10.1038/nsmb1066
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