Proceedings of the National Academy of Sciences · 2012 · 339 citations · 26 references
Life SciencesPlant BiologyPlant SciencesPlant BiochemistryPlant GeneticsPlant Molecular BiologyPlant EnzymesPlant Small Rna BiologyRna EditingRna Processing In PlantsCytidine-to-uridine EditingMitochondrial Rna EditingOrganelle Rna EditingPentatricopeptide Repeat ProteinsPull-down AssaysRna Editing ComplexesRna Editing EnzymesRna Editing In Plastids
RNA editing in flowering plant plastids and mitochondria converts many cytidines to uridines in coding regions, with site recognition thought to involve up to 200 PPR proteins. The study identifies the MORF protein family as additional components of the RNA editing machinery in plant mitochondria and plastids. Loss of MORF proteins disrupts editing at many sites, with two MORFs required for nearly all plastid editing and at least two for mitochondrial editing, and biochemical assays reveal that MORFs form hetero‑ and homodimers that selectively interact with PPR proteins, indicating a more complex editosome than previously thought.
RNA editing in plastids and mitochondria of flowering plants changes hundreds of selected cytidines to uridines, mostly in coding regions of mRNAs. Specific sequences around the editing sites are presumably recognized by up to 200 pentatricopeptide repeat (PPR) proteins. The here identified family of multiple organellar RNA editing factor (MORF) proteins provides additional components of the RNA editing machinery in both plant organelles. Two MORF proteins are required for editing in plastids; at least two are essential for editing in mitochondria. The loss of a MORF protein abolishes or lowers editing at multiple sites, many of which are addressed individually by PPR proteins. In plastids, both MORF proteins are required for complete editing at almost all sites, suggesting a heterodimeric complex. In yeast two-hybrid and pull-down assays, MORF proteins can connect to form hetero- and homodimers. Furthermore, MORF proteins interact selectively with PPR proteins, establishing a more complex editosome in plant organelles than previously thought.
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Sorting Signals, N-Terminal Modifications and Abundance of the Chloroplast Proteome
Boris Zybailov, Heidi L. Rutschow, Giulia Friso et al. · PLoS ONE · 2008 · 638 citations · Full text
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RNA Editing in Plant Mitochondria
Rudolf Hiesel, Bernd Wissinger, Wolfgang Schuster et al. · Science · 1989 · 555 citations