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Acta Crystallogr F Struct Biol Commun. 2015 Nov;71(Pt 11):1372-7. doi: 10.1107/S2053230X15017033. Epub 2015 Oct 23.

Crystallization and crystallographic analysis of an Arabidopsis nuclear proteinaceous RNase P.

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UPR 9002 du CNRS, IBMC, Centre National de la Recherche Scientifique, University of Strasbourg, 15 Rue René Descartes, 67084 Strasbourg, France.
UPR 2357 du CNRS, IBMP, Centre National de la Recherche Scientifique, University of Strasbourg, 12 Rue du Général Zimmer, 67084 Strasbourg, France.


RNase P activity is ubiquitous and involves the 5' maturation of precursor tRNAs. For a long time, it was thought that all RNases P were ribonucleoproteic enzymes. However, the characterization of RNase P in human mitochondria and in plants revealed a novel kind of RNase P composed of protein only, called PRORP for `proteinaceous RNase P'. Whereas in human mitochondria PRORP has two partners that are required for RNase P activity, PRORP proteins are active as single-subunit enzymes in plants. Three paralogues of PRORP are found in Arabidopsis thaliana. PRORP1 is responsible for RNase P in mitochondria and chloroplasts, while PRORP2 and PRORP3 are nuclear enzymes. Here, the purification and crystallization of the Arabidopsis PRORP2 protein are reported. Optimization of the initial crystallization conditions led to crystals that diffracted to 3 Å resolution.


PPR; RNase P; nuclear PRORP; tRNA maturation enzyme

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