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  RED2, a brain specific member of the RNA specific adenosine deaminase family

Melcher, T., Maas, S., Herb, A., Sprengel, R., Higuchi, M., & Seeburg, P. H. (1996). RED2, a brain specific member of the RNA specific adenosine deaminase family. The Journal of Biological Chemistry, 271(50), 31795-31798. Retrieved from http://www.jbc.org/content/271/50/31795.abstract.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-2264-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-FFC0-1
Genre: Journal Article
Alternative Title : RED2, a brain specific member of the RNA specific adenosine deaminase family

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JBiolChem_271_1996_31795.pdf (Any fulltext), 268KB
 
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 Creators:
Melcher, Thorsten1, Author              
Maas, Stefan1, Author              
Herb, Anne1, Author              
Sprengel, Rolf1, Author              
Higuchi, Miyoko1, Author              
Seeburg, Peter H.1, Author              
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1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

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 Abstract: The mammalian RNA-specific adenosine deaminases DRADA/dsRAD (alias ADAR) and RED1 (alias ADARB1) have been implicated in the site-selective editing of brain-expressed pre-mRNAs for glutamate receptor subunits and of antigenomic RNA of hepatitis delta virus. These enzymes are expressed in many if not all tissues, predicting an as yet unappreciated significance for adenosine deamination-mediated recoding of gene transcripts in the mammalian organism. We now report the molecular cloning of cDNA for RED2 (alias ADARB2), a third member of the RNA-specific adenosine deaminase family in the rodent. RED2 is closely sequence-related to RED1 but appears to be expressed only in the brain, where expression is widespread reaching highest levels in olfactory bulb and thalamus. RED2 further differs from RED1 in having a 54-residue amino-terminal extension which includes an arginine-rich motif. Different from DRADA and RED1, recombinantly expressed RED2 did not deaminate adenosines in extended synthetic dsRNA or in GluR-B pre-mRNA. However, a chimera of RED1 and RED2 edited the GluR-B Q/R and R/G sites with moderate efficiency. Our data suggest that RED2 may edit brain-specific transcripts with distinct structural features.

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Language(s): eng - English
 Dates: 1996-09-161996-12-13
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 271 (50) Sequence Number: - Start / End Page: 31795 - 31798 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1