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The crystal structure of a long form tRNase Z from S. cerevisiae and study of its interactome

Abstract : Yeast Trz1 is responsible for the endonucleolytic cleavage at the 3’-end during the maturation process of tRNAs. Trz1 belongs to the family of β-lactamase type RNases characterized by the presence of a HxHxDH sequence motif that is involved in the ligand formation of the catalytical required Zn-ions. The family consists of two subfamilies: the short forms with sequence lengths between and the long forms. A few crystal structures of short form RNase Z enzymes showed that they are active as homodimers. One subunit embraces the substrate tRNA using a protruding arm and the other provides the catalytic site. We here present the crystal structure of Trz1, the first of a long form RNase Z. Trz1 is organized in two domains connected by a large linker. Each domain is composed of a beta-lactamase type fold. The N-terminal domain has lost its catalytic residues, but contains the long arm that is important for tRNA binding; while it is the other way around of the C-terminal domain. From proteomics studies it is known that Trz1 forms a ternary complex with NUC1, a mitochondrial nuclease involved in apoptosis, and with a mutarotase (encoded by YMR099C). We purified the ternary Trz1/Nuc1/mutarotase complex and characterized its biochemical properties. Trz1/Nuc1/mutarotase forms in vitro a very stable heterohexamer in solution. From our SAXS and MALLS data we propose that the Nuc1 homodimer is at the centre of the complex and that each subunit interacts with one copy of Trz1 and mutarotase.
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Submitted on : Friday, November 30, 2018 - 1:14:28 PM
Last modification on : Saturday, June 25, 2022 - 8:28:25 PM
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  • HAL Id : tel-01940586, version 1


Miao Ma. The crystal structure of a long form tRNase Z from S. cerevisiae and study of its interactome. Structural Biology [q-bio.BM]. Université Paris-Saclay, 2016. English. ⟨NNT : 2016SACLS353⟩. ⟨tel-01940586⟩



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