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Science 10 March 1995:
Vol. 267. no. 5203, pp. 1491 - 1494
DOI: 10.1126/science.7878468
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Articles

Science, Vol 267, Issue 5203, 1491-1494
Copyright © 1995 by American Association for the Advancement of Science

articles

Glutamate receptor RNA editing in vitro by enzymatic conversion of adenosine to inosine

SM Rueter, CM Burns, SA Coode, P Mookherjee, and RB Emeson

Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232-6600.

RNA encoding the B subunit of the alpha-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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Structural Requirements for RNA Editing in Glutamate Receptor Pre-mRNAs by Recombinant Double-stranded RNA Adenosine Deaminase.
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Early-Onset Epilepsy and Postnatal Lethality Associated with an Editing-Deficient GluR-B Allele in Mice.
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