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A mammalian RNA editing enzyme

MPS-Authors
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Melcher,  Thorsten
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Maas,  Stefan
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Herb,  Anne
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Sprengel,  Rolf
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Higuchi,  Miyoko
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Melcher, T., Maas, S., Herb, A., Sprengel, R., Seeburg, P. H., & Higuchi, M. (1996). A mammalian RNA editing enzyme. Nature, 379, 460-464. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/8559253.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-2271-6
Abstract
EDITING of RNA1 by site-selective adenosine deamination alters codons in brain-expressed pre-messenger RNAs for glutamate receptor (GluR) subunits2–4 including a codon for a channel determinant (Q/R site) in GluR-B, which controls the Ca2+ permeability of α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors5,6. Editing of GluR pre-mRNAs requires a double-stranded RNA (dsRNA) structure formed by exonic and intronic sequences4,7 and is catalysed by an unknown dsRNA adenosine deaminase. Here we report the cloning of complementary DNA for RED1, a dsRNA adenosine deaminase expressed in brain and peripheral tissues that efficiently edits the Q/R site in GluR-B pre-mRNA in vitro. This site is poorly edited by DRADA, which is distantly sequence-related to RED1. Both deaminases edit the R/G site in GluR-B pre-mRNA, indicating that members of an emerging gene family catalyse adenosine deamination in nuclear transcripts with distinct but overlapping substrate specificities.