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pubmed-article:11741603pubmed:abstractTextThe amino acid, either a glutamine (Q) or an arginine (R), at the Q/R site of the pore-lining segment (M2) of a vertebrate AMPA receptor subunit critically influences the properties of the receptor. The R codon of the mammalian AMPA receptor subunit 2 (GRIA2) transcript is not coded by the chromosomal sequence, but is created by posttranscriptional RNA editing activities. On the other hand, the R codons of some teleost GRIA2 homologs are coded by chromosomal sequences. To elucidate the evolution of the utilization of Q/R RNA editing in modifying vertebrate GRIA2 transcripts, the GRIA2 genes of five fish species and an amphibian were studied. The putative hagfish GRIA2 homolog (hfGRIA2) encodes an R codon, whereas shark and bullfrog GRIA2 genes specify a Q codon at the genomic Q/R site. All gnathostoma GRIA2 genes possess an intron splitting the coding regions of M2 and the third hydrophobic region (M3). The intronic components required for Q/R RNA editing are preserved in all the Q-coding vertebrate GRIA2 genes but are absent from the R-coding GRIA2 genes. Interestingly, the hfGRIA2 is intronless, suggesting that hfGRIA2 is unlikely evolved from a Q/R editing-competent gene. Results of this study suggest that modification of GRIA2 transcripts by Q/R editing is most likely acquired after the separation of the Agnatha and Gnathostome.lld:pubmed
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pubmed-article:11741603pubmed:authorpubmed-author:ChenC CCClld:pubmed
pubmed-article:11741603pubmed:authorpubmed-author:ChenY CYClld:pubmed
pubmed-article:11741603pubmed:authorpubmed-author:LinW HWHlld:pubmed
pubmed-article:11741603pubmed:authorpubmed-author:KungS SSSlld:pubmed
pubmed-article:11741603pubmed:authorpubmed-author:ChowW YWYlld:pubmed
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pubmed-article:11741603pubmed:pagination277-81lld:pubmed
pubmed-article:11741603pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11741603pubmed:year2001lld:pubmed
pubmed-article:11741603pubmed:articleTitleQ/R RNA editing of the AMPA receptor subunit 2 (GRIA2) transcript evolves no later than the appearance of cartilaginous fishes.lld:pubmed
pubmed-article:11741603pubmed:affiliationDepartment of Life Science, National Tsing-Hua University, 101, Sec 2, Kang Fu Road, 30043, Hsinchu, Taiwan, ROC.lld:pubmed
pubmed-article:11741603pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11741603pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:11741603pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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