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  Structural requirements for RNA editing in glutamate receptor pre-mRNAs by recombinant double-stranded RNA adenosine deaminase

Maas, S., Melcher, T., Herb, A., Seeburg, P. H., Keller, W., Krause, S., et al. (1996). Structural requirements for RNA editing in glutamate receptor pre-mRNAs by recombinant double-stranded RNA adenosine deaminase. The Journal of Biological Chemistry, 271(21), 12221-12226. doi:10.1074/jbc.271.21.12221.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-0BEA-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-FFB8-6
Genre: Journal Article
Other : Different structural and enzymatic requirements for RNA editing in glutamate receptor pre-mRNAs

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JBiolChem_271_1996_12221.pdf (Any fulltext), 811KB
 
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http://www.jbc.org/content/271/21/12221.full.pdf (Supplementary material)
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 Creators:
Maas, Stefan1, Author              
Melcher, Thorsten1, Author              
Herb, Anne1, Author              
Seeburg, Peter H.1, Author              
Keller, Walter, Author
Krause, Sabine, Author
Higuchi, Miyoko1, Author              
O'Connell , Mary A., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

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 Abstract: Pre-mRNAs for brain-expressed ionotropic glutamate receptor subunits undergo RNA editing by site-specific adenosine deamination, which alters codons for molecular determinants of channel function. This nuclear process requires double-stranded RNA structures formed by exonic and intronic sequences in the pre-mRNA and is likely to be catalyzed by an adenosine deaminase that recognizes these structures as a substrate. DRADA, a double-stranded RNA adenosine deaminase, is a candidate enzyme for L-glutamate-activated receptor channel (GluR) pre-mRNA editing. We show here that DRADA indeed edits GluR pre-mRNAs, but that it displays selectivity for certain editing sites. Recombinantly expressed DRADA, both in its full-length form and in an N-terminally truncated version, edited the Q/R site in GluR6 pre-mRNA and the R/G site but not the Q/R site of GluR-B pre-mRNA. This substrate selectivity correlated with the base pairing status and sequence environment of the editing-targeted adenosines. The Q/R site of GluR-B pre-mRNA was edited by an activity partially purified from HeLa cells and thus differently structured editing sites in GluR pre-mRNAs appear to be substrates for different enzymatic activities.

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Language(s): eng - English
 Dates: 1996-02-281995-12-111996-02-281996-05-24
 Publication Status: Published in print
 Pages: 5
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 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 (21) Sequence Number: - Start / End Page: 12221 - 12226 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1