2006
Structure and Specific RNA Binding of ADAR2 Double-Stranded RNA Binding Motifs
STEFL, Richard; Ming XU; Lenka SKŘÍŠOVSKÁ; Ron EMESON; Frederic ALLAIN et al.Základní údaje
Originální název
Structure and Specific RNA Binding of ADAR2 Double-Stranded RNA Binding Motifs
Název česky
Structure and Specific RNA Binding of ADAR2 Double-Stranded RNA Binding Motifs
Autoři
STEFL, Richard; Ming XU; Lenka SKŘÍŠOVSKÁ; Ron EMESON a Frederic ALLAIN
Vydání
Structure, 2006, 0969-2126
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 5.738
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14310/06:00018473
Organizační jednotka
Přírodovědecká fakulta
UT WoS
Klíčová slova anglicky
RNA editing; MESSENGER-RNA; DSRNA-BINDING; ADENOSINE DEAMINASES; HUMAN TRANSCRIPTOME; RECEPTOR CHANNELS; CA2+ PERMEABILITY; MOLECULAR-BASIS; HUMAN BRAIN
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 22. 2. 2007 13:22, prof. Mgr. Richard Štefl, Ph.D.
V originále
Adenosine deaminases that act on RNA (ADARs) siteselectively modify adenosines to inosines within RNA transcripts, thereby recoding genomic information. How ADARs select specific adenosine moieties for deamination is poorly understood. Here, we report NMR structures of the two double-stranded RNA binding motifs (dsRBMs) of rat ADAR2 and an NMR chemical shift perturbation study of the interaction of the two dsRBMs with a 71 nucleotide RNA encoding the R/G site of the GluR-B. We have identified the protein and the RNA surfaces involved in complex formation, allowing us to present an NMR-based model of the complex. We have found that dsRBM1 recognizes a conserved pentaloop, whereas dsRBM2 recognizes two bulged bases adjacent to the editing site, demonstrating RNA structure-dependent recognition by the ADAR2 dsRBMs. In vitro mutagenesis studies with both the protein and the RNA further support our structural findings.
Česky
Adenosine deaminases that act on RNA (ADARs) siteselectively modify adenosines to inosines within RNA transcripts, thereby recoding genomic information. How ADARs select specific adenosine moieties for deamination is poorly understood. Here, we report NMR structures of the two double-stranded RNA binding motifs (dsRBMs) of rat ADAR2 and an NMR chemical shift perturbation study of the interaction of the two dsRBMs with a 71 nucleotide RNA encoding the R/G site of the GluR-B. We have identified the protein and the RNA surfaces involved in complex formation, allowing us to present an NMR-based model of the complex. We have found that dsRBM1 recognizes a conserved pentaloop, whereas dsRBM2 recognizes two bulged bases adjacent to the editing site, demonstrating RNA structure-dependent recognition by the ADAR2 dsRBMs. In vitro mutagenesis studies with both the protein and the RNA further support our structural findings.
Návaznosti
| MSM0021622413, záměr |
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