By a News Reporter-Staff News Editor at Biotech Week -- Research findings on Enzymes and Coenzymes are discussed in a new report. According to news reporting out of Irvine, California, by NewsRx editors, research stated, "Many pentatricopeptide repeat (PPR) proteins are RNA site specificity factors and include C-terminal DYW deaminase domains. ELI1 and DOT4 are required for editing single sites."
Our news journalists obtained a quote from the research from the University of California, "The DYW deaminase domain binds two zinc atoms. The C terminus of PLS-type PPR proteins shares molecular characteristics with cytidine deaminase. This study provides the first evidence that DYW deaminase domains bind zinc. Many transcripts expressed from plant organelle genomes are modified by C-to-U RNA editing. Nuclear encoded pentatricopeptide repeat (PPR) proteins are required as RNA binding specificity determinants in the RNA editing mechanism. Bioinformatic analysis has shown that most of the Arabidopsis PPR proteins necessary for RNA editing events include a C-terminal portion that shares structural characteristics with a superfamily of deaminases. The DYW deaminase domain includes a highly conserved zinc binding motif that shares characteristics with cytidine deaminases. The Arabidopsis PPR genes, ELI1 and DOT4, both have DYW deaminase domains and are required for single RNA editing events in chloroplasts. The ELI1 DYW deaminase domain was expressed as a recombinant protein in Escherichia coli and was shown to bind two zinc atoms per polypeptide. Thus, the DYW deaminase domain binds a zinc metal ion, as expected for a cytidine deaminase, and is potentially the catalytic component of an editing complex. Genetic complementation experiments demonstrate that large portions of the DYW deaminase domain of ELI1 may be eliminated, but the truncated genes retain the ability to restore editing site conversion in a mutant plant."
According to the news editors, the research concluded: "These results suggest that the catalytic activity can be supplied in trans by uncharacterized protein(s) of the editosome."
For more information on this research see: Identification of Two Pentatricopeptide Repeat Genes Required for RNA Editing and Zinc Binding by C-terminal Cytidine Deaminase-like Domains. Journal of Biological Chemistry, 2013;288(51):36519-36529. Journal of Biological Chemistry can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
Our news journalists report that additional information may be obtained by contacting M.L. Hayes, University of California, Dept. of Chem, Irvine, CA 92697, United States. Additional authors for this research include K. Giang, B. Berhane and R.M. Mulligan (see also Enzymes and Coenzymes).
Keywords for this news article include: Irvine, Peptides, Proteins, California, Hydrolases, Amino Acids, United States, Cytidine Deaminase, Enzymes and Coenzymes, Nucleoside Deaminases, North and Central America
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