Molecular and Cellular Biology, April 2006, p. 2869-2876, Vol. 26, No. 7
0270-7306/06/$08.00+0 doi:10.1128/MCB.26.7.2869-2876.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Heike Lange,1,
Kristina Kühn,2
Malek Alioua,1
Thomas Börner,2 and
Dominique Gagliardi1*
Institut de Biologie Moléculaire des Plantes, CNRS UPR2357, 12 Rue du Général Zimmer, 67084 Strasbourg Cedex, France,1 Institut für Biologie/Genetik, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany2
Received 26 September 2005/ Returned for modification 30 November 2005/ Accepted 9 January 2006
Plant mitochondrial genomes are extraordinarily large and complex compared to their animal counterparts, due to the presence of large noncoding regions. Multiple promoters are common for plant mitochondrial genes, and transcription exhibits little or no modulation. Mature functional RNAs are produced through various posttranscriptional processes, and control of RNA stability has a major impact on RNA abundance. This control involves polyadenylation which targets RNA for degradation by polynucleotide phosphorylase (PNPase). Here, we have analyzed polyadenylated RNA fragments from Arabidopsis plants down-regulated for PNPase (PNP plants). Because of their polyadenylated status and the accumulation of the corresponding RNA in PNP versus wild-type plants, these sequences represent mitochondrial RNA degradation tags. Analysis of these tags revealed that PNPase is involved in degrading rRNA and tRNA maturation by-products but also RNA transcribed from regions that are in some cases highly expressed although lacking known functional genes. Some of these transcripts, such as RNA containing chimeric open reading frames created by recombination or antisense RNA transcribed on the opposite strand of a known gene, may present potential detrimental effects to mitochondrial function. Taken together, our data show that the relaxed transcription in Arabidopsis mitochondria is counterbalanced by RNA stability control mediated by polyadenylation and PNPase.
Supplemental material for this article may be found at http://mcb.asm.org/.
These authors contributed equally to this work.
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