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Mol. Cell. Biol. doi:10.1128/MCB.02064-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Degradation of a polyadenylated rRNA maturation by-product involves one of the three RRP6-like proteins in Arabidopsis thaliana

Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique, Unité Propre de Recherche 2357, Conventionné avec l'Université Louis Pasteur, 67000 Strasbourg, France

^* To whom correspondence should be addressed. Email: dominique.gagliardi{at}ibmp-ulp.u-strasbg.fr.

	Abstract

Yeast Rrp6p and its human counterpart PM/Scl100 are exosome-associated proteins involved in degradation of aberrant transcripts and processing of precursors to stable RNAs such as the 5.8S rRNA, snRNAs and snoRNAs. Activity of yeast Rrp6p is stimulated by the polyadenylation of its RNA substrates. We identified three RRP6-like proteins in Arabidopsis thaliana: At-RRP6L3 is restricted to the cytoplasm, whereas At-RRP6L1 and 2 have different intra-nuclear localizations. Both nuclear RRP6L proteins are functional since At-RRP6L1 complements the temperature sensitive phenotype of a yeast rrp6 strain and mutation of At-RRP6L2 leads to accumulation of an rRNA maturation by-product. This by-product corresponds to the excised 5' part of the 18S-5.8S-25S rRNA precursor and accumulates as a polyadenylated transcript, suggesting that RRP6L2 is involved in poly(A)-mediated RNA degradation in plant nuclei. Interestingly, the rRNA maturation by-product is a substrate of At-RRP6L2 but not of AtRRP6L1. This result and the distinctive subcellular distribution of AtRRP6L1 to 3 indicate a specialization of RRP6-like proteins in Arabidopsis.

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