TRNase Z (EC 3.1.26.11, 3 tRNase, tRNA 3 endonuclease, RNase Z, 3' tRNase) is an enzyme [1] [2] [3] [4] [5] [6] [7] that, among other things, catalyses the reactions involved in the maturation of tRNAs. Here, it endonucleolytically cleaves the RNA and removes extra 3' nucleotides from the tRNA precursor, generating the 3' termini of tRNAs.

RNase Z is a widely distributed and often essential endoribonuclease that is responsible for the maturation of the 3′-end of a large family of transfer RNAs (tRNAs).

Sep 11, 2014 · Here we find that mutation of thermosensitive genic male sterile 5 (tms5) in rice causes the TGMS trait through a loss of RNase Z S1 function. We show that RNase Z S1 processes the mRNAs of...

Apr 18, 2024 · In humans, there are two isoforms of RNase Z, often referred to as ELAC1/2 or RNase Z S/L. ELAC1 forms a functional homodimer in a head-to-head orientation and it is believed that ELAC2 arose from an ELAC1 gene duplication event.

Mar 5, 2006 · RNase Z (tRNase Z or 3′ tRNase) is found in most if not all eukaryotes and archaea and in about half of the sequenced bacterial genomes 1. Two forms of RNase Z exist in eukaryotes, one long...

RNase Z is an endonuclease responsible for the removal of 3′ extensions from tRNA precursors, an essential step in tRNA biogenesis. Human cells contain a long form (RNase ZL) encoded by ELAC2, and a short form (RNase ZS; ELAC1). We studied their ...

RNase Z is a widely distributed and often essential endoribonuclease that is responsible for the maturation of the 3'-end of a large family of transfer RNAs (tRNAs). Although it has been the subject of study for more than 25 years, interest in this enzyme intensified dramatically with the …

Jun 6, 2017 · RNase Z is the enzyme responsible for the 3΄ endonucleolytic cleavage of tRNA precursors in all three domains of life, as shown in Methanococcus janaschii (6), Bacillus subtilis (7), Drosophila melanogaster (8), Arabidopsis thaliana (9), human mitochondria (10) and Schizosaccharomyces pombe (11).

Jan 4, 2006 · 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.