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Investigating the Role of the DYW Deaminase in RNA Processing
Author(s) -
AldanaMendoza Jonathan A,
Hayes Michael lloyd
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.lb71
Subject(s) - rna editing , rna , cytidine deaminase , riboswitch , rna binding protein , biology , pentatricopeptide repeat , non coding rna , biochemistry , intron , post transcriptional modification , cytidine , computational biology , chemistry , genetics , microbiology and biotechnology , gene , enzyme
RNA editing is the process by which ribonucleic acid (RNA) molecules are enzymatically modified post synthesis on specific nucleosides. In land plants it is mostly comprised of cytidine (C) to uridine (U) transformations linked to proteins with the DYW deaminase domain within the pentatricopeptide repeat (PPR) protein family. The DWY deaminase domain is likely the catalytic RNA editing domain because of its conserved glutamate residue of the HXE motif, required in other known catalyzed cytidine deaminases. PPR proteins have been shown to play important roles in transcript maturation. The molecular specificity of RNA‐binding proteins is essential for RNA regulation. Understanding RNA recognition also allows re‐coding of RNA‐binding proteins that may be employed to modulate RNA regulation in vivo . We plan on investigating the binding of PPRs to natural RNA transcripts by using transition state analogs (TSA's) which could inhibit RNA editing in vitro . Using different synthetic RNA's we can identify the requirements for RNA editing activity. Using chloroplast extracts in vitro RNA editing efficiency can be compared to determine the necessary cis‐ ‐elements. In order to discover the associated PPR specificity factor. This would also provide insight into the degenerate recognition code of RNA editing. Support or Funding Information NIH Grant # GM 49001