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  Editing of α-Amino-3-hydroxy-5-methylisoxazole-4-propionic Acid Receptor GluR-B Pre-mRNA in Vitro Reveals Site-selective Adenosine to Inosine Conversion

Melcher, T., Maas, S., Higuchi, M., Keller, W., Seeburg, P. H., Major, G., et al. (1995). Editing of α-Amino-3-hydroxy-5-methylisoxazole-4-propionic Acid Receptor GluR-B Pre-mRNA in Vitro Reveals Site-selective Adenosine to Inosine Conversion. The Journal of Biological Chemistry, 270(15), 8566-8570. doi:10.1074/jbc.270.15.8566.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A7E9-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AE56-C
Genre: Journal Article

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JBiolChem_270_1995_8566.pdf (Any fulltext), 7MB
 
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 Creators:
Melcher, Thorsten1, Author              
Maas, Stefan1, Author              
Higuchi, Miyoko1, Author              
Keller, Walter, Author
Seeburg, Peter H.1, Author              
Major, Guy, Author
Larkman, Alan U., Author
Jonas, Peter2, Author              
Sakmann, Bert2, Author              
Jack, J. Julian B., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: In neurons of the mammalian brain primary transcripts of genes encoding subunits of glutamate receptor channels can undergo RNA editing, leading to altered properties of the transmitter-activated channel. Editing of these transcripts is a nuclear process that targets specific adenosines and requires a double-stranded RNA structure configured from complementary exonic and intronic sequences. We show here that the two independent editing sites in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR-B pre-mRNA are edited with positional accuracy by nuclear extract from HeLa cells. Nucleotide analysis by thin layer chromatography of the edited RNA sequences revealed selective adenosine to inosine conversion, most likely reflecting the participation of double-stranded RNA adenosine deaminase. Our results predict the presence of inosine-containing codons in other mammalian mRNAs.

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Language(s): eng - English
 Dates: 1995-01-301995-04-14
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 666720
DOI: 10.1074/jbc.270.15.8566
Other: 4183
 Degree: -

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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: 270 (15) Sequence Number: - Start / End Page: 8566 - 8570 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1