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Editing of glutamate receptor subunit B pre-mRNA in vitro by site-specific deamination of adenosine

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Abstract

EDITING of the glutamate receptor subunit B (GluR-B) pre-mRNA at a single adenosine residue results in an amino-acid change that profoundly alters the electrophysiological properties of the receptor1–7. Here we show that the GluR-B pre-mRNA is efficiently and accurately edited in vitro, and that base-pair interactions between the editing site and a sequence in the downstream intron8 are required for substrate recognition. In addition, we directly demonstrate that editing results from the conversion of adenosine to inosine by enzymatic deamination. The biochemical properties of this GluR-B editing activity are similar to those of a double-stranded-RNA-dependent adenosine deaminase9–15, but RNA competition and column fractionation experiments indicate that the GluR-B editing and deaminase activities are distinct. Thus, the GluR-B editing enzyme may contain the adenosine deaminase, or a similar activity, and an RNA recognition subunit that specifically targets the enzyme to the editing site.

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Authors and Affiliations

  1. Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 01238, USA

    Jing-Hua Yang & Tom Maniatis

  2. Department of Psychiatry, Columbia University, New York, New York, 10032, USA

    Pamela Sklar

  3. Howard Hughes Medical Institute and Department of Biochemistry, Columbia University, New York, New York, 10032, USA

    Richard Axel

Authors
  1. Jing-Hua Yang
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  2. Pamela Sklar
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  3. Richard Axel
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  4. Tom Maniatis
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Yang, JH., Sklar, P., Axel, R. et al. Editing of glutamate receptor subunit B pre-mRNA in vitro by site-specific deamination of adenosine. Nature 374, 77–81 (1995). https://doi.org/10.1038/374077a0

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  • DOI: https://doi.org/10.1038/374077a0

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