STEFL, Richard, Ming XU, Lenka SKŘÍŠOVSKÁ, Ron EMESON and Frederic ALLAIN. Structure and Specific RNA Binding of ADAR2 Double-Stranded RNA Binding Motifs. Structure. 2006, vol. 14, No 2, p. 345–355. ISSN 0969-2126.
Other formats:   BibTeX LaTeX RIS
Basic information
Original name Structure and Specific RNA Binding of ADAR2 Double-Stranded RNA Binding Motifs
Name in Czech Structure and Specific RNA Binding of ADAR2 Double-Stranded RNA Binding Motifs
Authors STEFL, Richard (203 Czech Republic, guarantor), Ming XU (840 United States of America), Lenka SKŘÍŠOVSKÁ (203 Czech Republic), Ron EMESON (840 United States of America) and Frederic ALLAIN (250 France).
Edition Structure, 2006, 0969-2126.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 5.738
RIV identification code RIV/00216224:14310/06:00018473
Organization unit Faculty of Science
UT WoS 000235431700021
Keywords in English RNA editing; MESSENGER-RNA; DSRNA-BINDING; ADENOSINE DEAMINASES; HUMAN TRANSCRIPTOME; RECEPTOR CHANNELS; CA2+ PERMEABILITY; MOLECULAR-BASIS; HUMAN BRAIN
Tags ADENOSINE DEAMINASES, CA2+ PERMEABILITY, DSRNA-BINDING, human brain, HUMAN TRANSCRIPTOME, MESSENGER-RNA, MOLECULAR-BASIS, RECEPTOR CHANNELS, RNA editing
Tags International impact, Reviewed
Changed by Changed by: prof. Mgr. Richard Štefl, Ph.D., učo 19362. Changed: 22/2/2007 13:22.
Abstract
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.
Abstract (in Czech)
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.
Links
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
PrintDisplayed: 21/5/2024 22:24