ArticleNucleic acids research2017
The crystal structure of Trz1, the long form RNase Z from yeast.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of human nuclear and mitochondrial tRNA 3' processing.Nature structural & molecular biology · 2025Article
- Structural insights into human ELAC2 as a tRNA 3' processing enzyme.Nucleic acids research · 2024Article
- Structural basis for human mitochondrial tRNA maturation.Nature communications · 2024Article
- The making and breaking of tRNAs by ribonucleases.Trends in genetics : TIG · 2024Review
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- A tRNA processing enzyme is a key regulator of the mitochondrial unfolded protein response.eLife · 2022Article
- ELAC2/RNaseZ-linked cardiac hypertrophy in Drosophila melanogaster.Disease models & mechanisms · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Visualizing the superfamily of metallo-β-lactamases through sequence similarity network neighborhood connectivity analysis.Heliyon · 2021Article
- A protein of the metallo-hydrolase/oxidoreductase superfamily with both beta-lactamase and ribonuclease activity is linked with translation in giant viruses.Scientific reports · 2020Article
- Mutations in ELAC2 associated with hypertrophic cardiomyopathy impair mitochondrial tRNA 3'-end processing.Human mutation · 2019Article
- TheRNA (New York, N.Y.) · 2018Article
- Article
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Authors and funding
8 authors at 6 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
tRNAs are synthesized as precursor RNAs that have to undergo processing steps to become functional. Yeast Trz1 is a key endoribonuclease involved in the 3΄ maturation of tRNAs in all domains of life. It is a member of the β-lactamase family of RNases, characterized by an HxHxDH sequence motif involved in coordination of catalytic Zn-ions. The RNase Z family consists of two subfamilies: the short (250-400 residues) and the long forms (about double in size). Short form RNase Z enzymes act as homodimers: one subunit embraces tRNA with a protruding arm, while the other provides the catalytic site. The long form is thought to contain two fused β-lactamase domains within a single polypeptide. Only structures of short form RNase Z enzymes are known. Here we present the 3.1 Å crystal structure of the long-form Trz1 from Saccharomyces cerevisiae. Trz1 is organized into two β-lactamase domains connected by a long linker. The N-terminal domain has lost its catalytic residues, but retains the long flexible arm that is important for tRNA binding, while it is the other way around in the C-terminal domain. Trz1 likely evolved from a duplication and fusion of the gene encoding the monomeric short form RNase Z.
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