A survey of PPR proteins identifies DYW domains like those of land plant RNA editing factors in diverse eukaryotes.

ABSTRACT: The pentatricopeptide repeat modules of PPR proteins are key to their sequence-specific binding to RNAs. Gene families encoding PPR proteins are greatly expanded in land plants where hundreds of them participate in RNA maturation, mainly in mitochondria and chloroplasts. Many plant PPR proteins contain additional carboxyterminal domains and have been identified as essential factors for specific events of C-to-U RNA editing, which is abundant in the two endosymbiotic plant organelles. Among those carboxyterminal domain additions to plant PPR proteins, the so-called DYW domain is particularly interesting given its similarity to cytidine deaminases. The frequency of organelle C-to-U RNA editing and the diversity of DYW-type PPR proteins correlate well in plants and both were recently identifi

SUBMITTER: Schallenberg-Rudinger M 

PROVIDER: S-EPMC3858438 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature