ArticleThe Journal of biological chemistry2015
A conserved glutamate residue in the C-terminal deaminase domain of pentatricopeptide repeat proteins is required for RNA editing activity.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 74 citations in OpenAlex.
- Natural Variation of a PPR Coding Gene SST1 Confers Salt Tolerance During Soybean Domestication.Plant biotechnology journal · 2026Article
- Genome-wide identification and dynamic transcriptome profiling of the DYW-type PPR family across greening of chlorotic leaves in pear (Frontiers in plant science · 2026Article
- Synthetic Pentatricopeptide Repeat Proteins: Building a Toolkit for Precise RNA Control.International journal of molecular sciences · 2025Review
- Deciphering the role of accessory proteins in Arabidopsis chloroplast editosomes via interaction with a synthetic PPR-PLS factor in E. coli.Nucleic acids research · 2025Article
- Genome-wide analysis ofFrontiers in plant science · 2025Article
- Article
- The dicot homolog of maize PPR103 carries a C-terminal DYW domain and may have a role in C-to-U editing of some chloroplast RNA transcripts.Plant molecular biology · 2024Article
- Conservation of the moss RNA editing factor PPR78 despite the loss of its known cytidine-to-uridine editing sites is explained by a hidden extra target.The Plant cell · 2024Article
- A ribonuclease activity linked to DYW1 in vitro is inhibited by RIP/MORF proteins.Scientific reports · 2023Article
- Structural insight into the activation of an Arabidopsis organellar C-to-U RNA editing enzyme by active site complementation.The Plant cell · 2023Article
- Plant organellar RNA maturation.The Plant cell · 2023Review
- Characterization of theGenes · 2023Article
- Article
- Functions of PPR Proteins in Plant Growth and Development.International journal of molecular sciences · 2021Review
- DYW domain structures imply an unusual regulation principle in plant organellar RNA editing catalysis.Nature catalysis · 2021Article
- A synthetic RNA editing factor edits its target site in chloroplasts and bacteria.Communications biology · 2021Article
- Research Progress of PPR Proteins in RNA Editing, Stress Response, Plant Growth and Development.Frontiers in genetics · 2021Review
- Article
- PPR-DYW Protein EMP17 Is Required for Mitochondrial RNA Editing, Complex III Biogenesis, and Seed Development in Maize.Frontiers in plant science · 2021Article
- Accumulation of the RNA polymerase subunit RpoB depends on RNA editing by OsPPR16 and affects chloroplast development during early leaf development in rice.The New phytologist · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many transcripts expressed from plant organelle genomes are modified by C-to-U RNA editing. Nuclear encoded pentatricopeptide repeat (PPR) proteins include an RNA binding domain that provides site specificity. In addition, many PPR proteins include a C-terminal DYW deaminase domain with characteristic zinc binding motifs (CXXC, HXE) and has recently been shown to bind zinc ions. The glutamate residue of the HXE motif is catalytically required in the reaction catalyzed by cytidine deaminase. In this work, we examine the activity of the DYW deaminase domain through truncation or mutagenesis of the HXE motif. OTP84 is required for editing three chloroplast sites, and transgenes expressing OTP84 with C-terminal truncations were capable of editing only one of the three cognate sites at high efficiency. These results suggest that the deaminase domain of OTP84 is required for editing two of the sites, but another deaminase is able to supply the deamination activity for the third site. OTP84 and CREF7 transgenes were mutagenized to replace the glutamate residue of the HXE motif, and transgenic plants expressing OTP84-E824A and CREF7-E554A were unable to efficiently edit the cognate editing sites for these genes. In addition, plants expressing CREF7-E554A exhibited substantially reduced capacity to edit a non-cognate site, rpoA C200. These results indicate that the DYW deaminase domains of PPR proteins are involved in editing their cognate editing sites, and in some cases may participate in editing additional sites in the chloroplast.
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