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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.
Afiliação
  • Melcher T; Laboratory for Neurobiology, Max-Planck Institute for Medical Research, Jahnstrasse 12, 69120 Heidelberg, Germany. seeburg@sun0.urz.uni-heidelberg.de
J Biol Chem ; 271(50): 31795-8, 1996 Dec 13.
Article em En | MEDLINE | ID: mdl-8943218
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.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Química Encefálica / Adenosina Desaminase Limite: Animals Idioma: En Revista: J Biol Chem Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Alemanha
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Química Encefálica / Adenosina Desaminase Limite: Animals Idioma: En Revista: J Biol Chem Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Alemanha