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Titolo:
In vitro analysis of the binding of ADAR2 to the pre-mRNA encoding the GluR-B R/G site
Autore:
Ohman, M; Kallman, AM; Bass, BL;
Indirizzi:
Univ Stockholm, Dept Mol Genome Res, S-10691 Stockholm, Sweden Univ Stockholm Stockholm Sweden S-10691 e Res, S-10691 Stockholm, Sweden Univ Utah, Dept Biochem, Howard Hughes Med Inst, Salt Lake City, UT 84132 USA Univ Utah Salt Lake City UT USA 84132 Inst, Salt Lake City, UT 84132 USA
Titolo Testata:
RNA-A PUBLICATION OF THE RNA SOCIETY
fascicolo: 5, volume: 6, anno: 2000,
pagine: 687 - 697
SICI:
1355-8382(200005)6:5<687:IVAOTB>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA ADENOSINE-DEAMINASE; GLUTAMATE-RECEPTOR CHANNELS; MESSENGER-RNA; CA2+ PERMEABILITY; DSRNA; PURIFICATION; SUBUNIT; DOMAIN; ENZYME;
Keywords:
ADAR; deamination; double-stranded RNA; dsRBM; RNA editing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Ohman, M Univ Stockholm, Dept Mol Genome Res, S-10691 Stockholm, Sweden Univ Stockholm Stockholm Sweden S-10691 10691 Stockholm, Sweden
Citazione:
M. Ohman et al., "In vitro analysis of the binding of ADAR2 to the pre-mRNA encoding the GluR-B R/G site", RNA, 6(5), 2000, pp. 687-697

Abstract

The ADAR family of RNA-editing enzymes deaminates adenosines within RNA that is completely or largely double stranded. In mammals, most of the characterized substrates encode receptors involved in neurotransmission, and these substrates are thought to be targeted by the mammalian enzymes ADAR1 and ADAR2. Although some ADAR substrates are deaminated very promiscuously, mammalian glutamate receptor B (gluR-B) pre-mRNA is deaminated at a few specific adenosines. Like most double-stranded RNA (dsRNA) binding proteins, ADARs bind to many different sequences, but few studies have directly measured and compared binding affinities. We have attempted to determine if ADAR deamination specificity occurs because the enzymes bind to targeted regions with higher affinities. To explore this question we studied binding of rat ADAR2 to a region of rat gluR-B pre-mRNA that contains the R/G editing site, and compared a wild-type molecule with one containing mutations that decreased R/G site editing. Although binding affinity to the two sequences was almost identical, footprinting studies indicate ADAR2 binds to the wild-type RNA at a discrete region surrounding the editing site, whereas binding to the mutant appeared nonspecific.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 01:32:41