The cytidine deaminase signature HxE(x)nCxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1. Boussardon, C., Avon, A., Kindgren, P., Bond, C. S., Challenor, M., Lurin, C., & Small, I. New Phytologist, 203(4):1090–1095, 2014. _eprint: https://nph.onlinelibrary.wiley.com/doi/pdf/10.1111/nph.12928![The cytidine deaminase signature HxE(x)nCxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1 [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.
@article{boussardon_cytidine_2014,
title = {The cytidine deaminase signature {HxE}(x){nCxxC} of {DYW1} binds zinc and is necessary for {RNA} editing of {ndhD}-1},
volume = {203},
issn = {1469-8137},
url = {https://nph.onlinelibrary.wiley.com/doi/abs/10.1111/nph.12928},
doi = {10/f6cv49},
abstract = {In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.},
language = {en},
number = {4},
urldate = {2021-09-02},
journal = {New Phytologist},
author = {Boussardon, Clément and Avon, Alexandra and Kindgren, Peter and Bond, Charles S. and Challenor, Michael and Lurin, Claire and Small, Ian},
year = {2014},
note = {\_eprint: https://nph.onlinelibrary.wiley.com/doi/pdf/10.1111/nph.12928},
keywords = {DYW domain, RNA editing, cytidine deaminase, pentatricopeptide repeat (PPR) proteins, zinc-binding motif},
pages = {1090--1095},
}
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The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.","language":"en","number":"4","urldate":"2021-09-02","journal":"New Phytologist","author":[{"propositions":[],"lastnames":["Boussardon"],"firstnames":["Clément"],"suffixes":[]},{"propositions":[],"lastnames":["Avon"],"firstnames":["Alexandra"],"suffixes":[]},{"propositions":[],"lastnames":["Kindgren"],"firstnames":["Peter"],"suffixes":[]},{"propositions":[],"lastnames":["Bond"],"firstnames":["Charles","S."],"suffixes":[]},{"propositions":[],"lastnames":["Challenor"],"firstnames":["Michael"],"suffixes":[]},{"propositions":[],"lastnames":["Lurin"],"firstnames":["Claire"],"suffixes":[]},{"propositions":[],"lastnames":["Small"],"firstnames":["Ian"],"suffixes":[]}],"year":"2014","note":"_eprint: https://nph.onlinelibrary.wiley.com/doi/pdf/10.1111/nph.12928","keywords":"DYW domain, RNA editing, cytidine deaminase, pentatricopeptide repeat (PPR) proteins, zinc-binding motif","pages":"1090–1095","bibtex":"@article{boussardon_cytidine_2014,\n\ttitle = {The cytidine deaminase signature {HxE}(x){nCxxC} of {DYW1} binds zinc and is necessary for {RNA} editing of {ndhD}-1},\n\tvolume = {203},\n\tissn = {1469-8137},\n\turl = {https://nph.onlinelibrary.wiley.com/doi/abs/10.1111/nph.12928},\n\tdoi = {10/f6cv49},\n\tabstract = {In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. 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