Structural highlights
Function
[RNZ_YEAST] Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Publication Abstract from PubMed
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 beta-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 beta-lactamase domains within a single polypeptide. Only structures of short form RNase Z enzymes are known. Here we present the 3.1 A crystal structure of the long-form Trz1 from Saccharomyces cerevisiae. Trz1 is organized into two beta-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.
The crystal structure of Trz1, the long form RNase Z from yeast.,Ma M, Li de la Sierra-Gallay I, Lazar N, Pellegrini O, Durand D, Marchfelder A, Condon C, van Tilbeurgh H Nucleic Acids Res. 2017 Jun 2;45(10):6209-6216. doi: 10.1093/nar/gkx216. PMID:28379452[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ma M, Li de la Sierra-Gallay I, Lazar N, Pellegrini O, Durand D, Marchfelder A, Condon C, van Tilbeurgh H. The crystal structure of Trz1, the long form RNase Z from yeast. Nucleic Acids Res. 2017 Jun 2;45(10):6209-6216. doi: 10.1093/nar/gkx216. PMID:28379452 doi:https://dx.doi.org/10.1093/nar/gkx216
