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Journal Article

Q/R site editing in kainate receptor GluR5 and GluR6 pre-mRNAs requires distant intronic sequences

MPS-Authors
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Herb,  Anne
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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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;

External Resource

http://www.pnas.org/cgi/reprint/93/5/1875?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&searchid=1050127900416_1336&stored_search=&FIRSTINDEX=0&minscore=5000&journalcode=pnas
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Citation

Herb, A., Higuchi, M., Sprengel, R., & Seeburg, P. H. (1996). Q/R site editing in kainate receptor GluR5 and GluR6 pre-mRNAs requires distant intronic sequences. Proceedings of the National Academy of Sciences of the United States of America, 93(5), 1875-1880. Retrieved from http://www.pnas.org/cgi/content/abstract/93/5/1875?maxtoshow%3D%26HITS%3D10%26hits%3D10%26RESULTFORMAT%3D%26searchid%3D1050127900416_1336%26stored_search%3D%26FIRSTINDEX%3D0%26minscore%3D5000%26journalcode%3Dpnas.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-2209-0
Abstract
RNA editing by adenosine deamination in brain-expressed pre-mRNAs for glutamate receptor (GluR) subunits alters gene-specified codons for functionally critical positions, such as the channel's Q/R site. We show by transcript analysis of minigenes transiently expressed in PC-12 cells that, in contrast to GluR-B pre-mRNA, where the two editing sites (Q/R and R/G) require base pairing with nearby intronic editing site complementary sequences (ECSs), editing in GluR5 and GluR6 pre-mRNAs recruits an ECS located as far as 1900 nucleotides distal to the Q/R site. The exon-intron duplex structure of the GluR5 and GluR6 pre-mRNAs appears to be a substrate of double-stranded RNA-specific adenosine deaminase. This enzyme when coexpressed in HEK 293 cells preferentially targets the adenosine of the Q/R site and of an unpaired position in the ECS which is highly edited in brain.