English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

A mammalian RNA editing enzyme

MPS-Authors
/persons/resource/persons94319

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

/persons/resource/persons94165

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

/persons/resource/persons93388

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

/persons/resource/persons95439

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

/persons/resource/persons95292

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

/persons/resource/persons93415

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

Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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: https://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.