MEF46 and MEF47 are novel specificity factors for RNA editing sites in mitochondrial nad transcripts
| Autor: | Franziska Glass, Anja Jörg, Nadja Brehme, Mizuki Takenaka |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Cytidine deaminase activity RNA Mitochondrial Mutant Arabidopsis Biology Subclass 03 medical and health sciences 0302 clinical medicine Protein Domains Gene Expression Regulation Plant RNA Messenger Plastid Tyrosine Molecular Biology Genetics Arabidopsis Proteins Cell Biology Mitochondria 030104 developmental biology RNA editing RNA Plant Mutation Molecular Medicine Pentatricopeptide repeat NAD+ kinase RNA Editing 030217 neurology & neurosurgery |
| Zdroj: | Mitochondrion. 53 |
| ISSN: | 1872-8278 |
| Popis: | Terrestrial plants have C-to-U RNA editing in the transcripts of plastids and mitochondria. Target specificity for more than several hundred editing sites are governed by PLS (PPR, Long and Short) class Pentatricopeptide repeat (PPR) proteins with additional C-terminal domains. Half of these PPR proteins have DYW (Aspartate (D), Tyrosine (Y) and Tryptophan (W)) domains, which most likely harbour cytidine deaminase activity. The other half of them, E subclass and E+ subclass proteins, contain no or only a part of the DYW domain. Missing DYW domains in the E and E+ subclass PPR proteins are likely to be complemented by other DYW containing proteins. All target sites of so far characterized E+ subclass PPR proteins show defects in dyw2 mutants, suggesting that the DYW2 protein complements the missing DYW domains in the E+ subclass PPR proteins. Here we report two novel RNA editing factors, MEF46 and MEF47, which belong to E+ and E subclass, respectively. The defective editing site in mef46, nad5-1958, overlaps with the affected sites in dyw2 mutants, while that in mef47, nad3-64 and ccmC-614 do not, further supporting the specific functional connection between E+ subclass PPR proteins and DYW2. |
| Databáze: | OpenAIRE |
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