Editing of the GLuR-B ion channel RNA in vitro by recombinant double-stranded RNA adenosine deaminase.

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Abstract
Double‐stranded RNA (dsRNA)‐specific adenosine deaminase (DRADA) has been implicated as an enzyme responsible for the editing of RNA transcripts encoding glutamate‐gated ion channel subunits (GLuR) in brain. In one case, the editing alters the gene‐encoded glutamine (Q) to an arginine (R) located within the channel‐forming domain of the alpha‐amino‐3‐hydroxy‐5‐methyl‐isoxazole‐4‐propionic acid (AMPA) receptor subunit GLuR‐B. The result of editing at this site, called the ‘Q/R’ site, is a profound alteration of the Ca2+ permeability of the GLuR channel. Using recombinantly expressed DRADA proteins, we now demonstrate in vitro that DRADA is indeed involved in editing of the GLuR‐B RNA. In addition to the formation of an RNA duplex structure involving exon and intron sequences, Q/R site‐selective editing by DRADA also requires a cofactor protein(s) commonly present even in non‐neuronal cells. The accuracy and efficiency of this RNA editing system appear to be determined by the quantitative balance between DRADA, cofactor and substrate GLuR‐B RNA.

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