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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Mulligan, R. Michael Diaz, Michael F. Hayes, Michael L. Dang, Kim N. |
| Description | Author Affiliation: Hayes ML ( From the Developmental and Cell Biology, University of California, Irvine, California 92697.); Dang KN ( From the Developmental and Cell Biology, University of California, Irvine, California 92697.); Diaz MF ( From the Developmental and Cell Biology, University of California, Irvine, California 92697.); Mulligan RM ( From the Developmental and Cell Biology, University of California, Irvine, California 92697 rmmullig@uci.edu.) |
| 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. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 16 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-04-17 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Arabidopsis Proteins Chemistry Arabidopsis Metabolism Cytidine Deaminase Glutamic Acid RNA Editing RNA, Plant Agrobacterium Genetics Amino Acid Motifs Conserved Sequence Gene Expression Regulation, Plant Molecular Sequence Data Protein Isoforms Protein Structure, Tertiary Structure-Activity Relationship Transformation, Genetic Transgenes Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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