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Published on May 1, 2009; 10.1104/pp.109.137950

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Received March 2, 2009
Accepted April 26, 2009

Arabidopsis encodes four tRNase Z enzymes

Giusy Canino , Edyta Bocian , Nicolas Barbezier , Manuel Echeverria , Joachim Forner , Stefan Binder , and Anita Marchfelder *

Molekulare Botanik, Universitat Ulm, Albert-Einstein-Allee 11, 89069 Ulm, Germany; Laboratoire Genome et Developpement des Plantes, UMR CNRS 5096, Universite de Perpignan, 66860 Perpignan Cedex, France

* Corresponding author; email: anita.marchfelder{at}uni-ulm.de.

Functional tRNA molecules are a prerequisite for protein biosynthesis. Several processing steps are required to generate the mature functional tRNA from precursor molecules. Two of the early processing steps involve cleavage at the tRNA 5' end and the tRNA 3' end. While processing at the tRNA 5' end is performed by RNase P, cleavage at the 3' end is catalysed by the endonuclease tRNase Z. In eukaryotes tRNase Z enzymes are found in two versions: a short form of about 250–300 amino acids and a long form of about 700–900 amino acids. All eukaryotic genomes analysed to date encode at least one long tRNase Z protein. Of those, Arabidopsis thaliana is the only organism that encodes four tRNase Z proteins, two short forms and two long forms. We show here that the four proteins are distributed to different subcellular compartments in the plant cell: the nucleus, the cytoplasm the mitochondrion and the chloroplast. One tRNase Z is present only in the cytoplasm, one protein is found exclusively in mitochondria while the third one has dual locations: nucleus and mitochondria. None of these three tRNase Z proteins are essential. The fourth tRNase Z protein is present in chloroplasts and deletion of its gene results in an embryo-lethal phenotype. In vitro analysis with the recombinant proteins showed that all four tRNase Z enzymes have tRNA 3' processing activity. In addition, the mitochondrial tRNase Z proteins cleave tRNA-like elements that serve as processing signals in mitochondrial mRNA maturation.




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N. Barbezier, G. Canino, J. Rodor, E. Jobet, J. Saez-Vasquez, A. Marchfelder, and M. Echeverria
Processing of a Dicistronic tRNA-snoRNA Precursor: Combined Analysis in Vitro and in Vivo Reveals Alternate Pathways and Coupling to Assembly of snoRNP
Plant Physiology, July 1, 2009; 150(3): 1598 - 1610.
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