1. Pentatricopeptide Repeat Proteins with the DYW Motif Have Distinct Molecular Functions in RNA Editing and RNA Cleavage in Arabidopsis Chloroplasts
- Author
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Mamoru Sugita, Takahiro Nakamura, Kenji Okuda, Toshiharu Shikanai, Anne Laure Chateigner-Boutin, Kazuo Shinozaki, Etienne Delannoy, Reiko Motohashi, Fumiyoshi Myouga, Ian Small, Kyoto University [Kyoto], Australian Research Council Centre of Excellence in Plant Energy Biology, University of Canberra, Kyushu University, PRESTO, Japan Science and Technology Agency, Nagoya University, Riken, RIKEN - Institute of Physical and Chemical Research [Japon] (RIKEN), Shizuoka University, and Australian Research Council CE0561495
- Subjects
0106 biological sciences ,Chloroplasts ,Molecular Sequence Data ,Arabidopsis ,Plant Science ,Cleavage (embryo) ,01 natural sciences ,03 medical and health sciences ,Gene Expression Regulation, Plant ,Organelle ,[SDV.BV]Life Sciences [q-bio]/Vegetal Biology ,Amino Acid Sequence ,Plastid ,Research Articles ,030304 developmental biology ,Genetics ,0303 health sciences ,biology ,Arabidopsis Proteins ,RNA ,RNA Probes ,Cell Biology ,Plants, Genetically Modified ,biology.organism_classification ,Recombinant Proteins ,Protein Structure, Tertiary ,Cell biology ,Mutagenesis, Insertional ,RNA, Plant ,RNA editing ,Mutation ,Pentatricopeptide repeat ,RNA Editing ,RNA Cleavage ,010606 plant biology & botany - Abstract
Scientific Research on Priority Areas16085206 Ministry of Education, Culture, Sports, Science, and Technology of Japan 17GS0316 Ministry of Agriculture, Forestry, and Fisheries of Japan GPN0008 Australian Research Council CE0561495; International audience; The plant-specific DYW subclass of pentatricopeptide repeat proteins has been postulated to be involved in RNA editing of organelle transcripts. We discovered that the DYW proteins CHLORORESPIRATORY REDUCTION22 (CRR22) and CRR28 are required for editing of multiple plastid transcripts but that their DYW motifs are dispensable for editing activity in vivo. Replacement of the DYW motifs of CRR22 and CRR28 by that of CRR2, which has been shown to be capable of endonucleolytic cleavage, blocks the editing activity of both proteins. In return, the DYW motifs of neither CRR22 nor CRR28 can functionally replace that of CRR2. We propose that different DYW family members have acquired distinct functions in the divergent processes of RNA maturation, including RNA cleavage and RNA editing.
- Published
- 2009