A Conserved Lysine in an Ion-Pair with a Catalytic Glutamate Is Critical for U-to-C RNA Editing but Restricts C-to-U RNA Editing.

ABSTRACT: Plants make pyrimidine base substitutions in organellar mRNAs through the action of sequence-specific nuclear-encoded enzymes. Pentatricopeptide repeat (PPR) proteins are essential for ensuring specificity, while the enzymatic DYW domain is often present at the C-terminus of a PPR protein and dependent on the variant possessing C-to-U and/or U-to-C RNA editing activities. Expression of exogenous DYW-KP variant enzymes in bacteria leads to the modification of RNAs suggestive of U-to-C base changes. The modified RNAs could only be purified from the interphase of an acidic guanidinium thiocyanate-phenol-chloroform experiment. It was projected that in bacteria stable RNA-enzyme cross-links form from a lysyl attack. In this study, RNA editing was examined for dual U-to-C/C-to-U editing enzyme K

SUBMITTER: Chun SO 

PROVIDER: S-EPMC11713852 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature