title: RNA editing in plants: Machinery and flexibility of site recognition.
abstract: In plants, RNA editing is a process that deaminates specific cytidines (C) to uridines (U). PLS subfamily members of PPR proteins function in site recognition of the target C. In silico analysis has predicted the code used for PPR motif-nucleotide interaction, and the crystal structure of a protein-RNA complex supports this model. Despite progress in understanding the RNA-binding mechanism of PPR proteins, some of the flexibility of RNA recognition observed in trans-factors of RNA editing has not been fully explained. It is probably necessary to consider another unknown mechanism, and this consideration is related to the question of how PPR proteins have managed the creation of RNA editing sites during evolution. This question may be related to the mystery of the biological function of RNA editing in plants. MORF/RIP family members are required for RNA editing at multiple editing sites and are components of the RNA editosome in plants. The DYW domain has been a strong candidate for the C deaminase activity required for C-to-U conversion in RNA editing. So far, the activity of this enzyme has not been detected in recombinant DYW proteins, and several puzzling experimental results need to be explained to support the model. It is still difficult to resolve the entire image of the editosome in RNA editing in plants. This article is part of a Special Issue entitled: Chloroplast Biogenesis.
authors.affiliation: Department of Botany, Graduate School of Science, Kyoto University, Kyoto 606-8502 Japan; CREST, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 102-0076, Japan. Electronic address: shikanai@pmg.bot.kyoto-u.ac.jp.
authors.forename: Toshiharu
authors.initials: T
authors.lastname: Shikanai
mesh_terms: D010940:Plant Proteins / Q000502:physiology; D010944:Plants / Q000235:genetics*; D017393:RNA Editing
chemical_list: D010940:Plant Proteins
keywords: Chloroplast; DYW domain; NDH; PPR protein; RNA editing; Translation