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Glutamate Receptor RNA Editing in Vitro by Enzymatic Conversion of Adenosine to Inosine

Susan M. Rueter, Colleen M. Burns, Sarah A. Coode, Paramita Mookherjee and Ronald B. Emeson
Science
New Series, Vol. 267, No. 5203 (Mar. 10, 1995), pp. 1491-1494
Stable URL: http://www.jstor.org/stable/2886548
Page Count: 4
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Abstract

RNA encoding the B subunit of the α-amino-3-hydroxy-5-methyl-4- isoxazolepropionic acid (AMPA) subtype of ionotropic glutamate receptor (GluR-B) undergoes a posttranscriptional modification in which a genomically encoded adenosine is represented as a guanosine in the GluR-B complementary DNA. In vitro editing of GluR-B RNA transcripts with HeLa cell nuclear extracts was found to result from an activity that converts adenosine to inosine in regions of double-stranded RNA by enzymatic base modification. This activity is consistent with that of a double-stranded RNA-specific adenosine deaminase previously described in Xenopus oocytes and widely distributed in mammalian tissues.

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