Modulation of ADAR1 editing activity by Z-RNA in vitro Export

@article{citeulike:340650, abstract = {RNA editing by A-to-I modification has been recognized as an important molecular mechanism for generating RNA and protein diversity. In mammals, it is mediated by a family of adenosine deaminases that act on RNAs (ADARs). The large version of the editing enzyme ADAR1 (ADAR1-L), expressed from an interferon-responsible promoter, has a Z-DNA/Z-RNA binding domain at its N-terminus. We have tested the in vitro ability of the enzyme to act on a 50 bp segment of dsRNA with or without a Z-RNA forming nucleotide sequence. A-to-I editing efficiency is markedly enhanced in presence of the sequence favoring Z-RNA. In addition, an alteration in the pattern of modification along the RNA duplex becomes evident as reaction times decrease. These results suggest that the local conformation of dsRNA molecules might be an important feature for target selectivity by ADAR1 and other proteins with Z-RNA binding domains. 10.1093/nar/gki849}, author = {Koeris, Michael and Funke, Lars and Shrestha, Jay and Rich, Alexander and Maas, Stefan}, citeulike-article-id = {340650}, citeulike-linkout-0 = {http://dx.doi.org/10.1093/nar/gki849}, citeulike-linkout-1 = {http://nar.oxfordjournals.org/content/33/16/5362.abstract}, citeulike-linkout-2 = {http://nar.oxfordjournals.org/content/33/16/5362.full.pdf}, citeulike-linkout-3 = {http://www.ingentaconnect.com/content/oup/nar/2005/00000033/00000016/art05362}, citeulike-linkout-4 = {http://view.ncbi.nlm.nih.gov/pubmed/16177183}, citeulike-linkout-5 = {http://www.hubmed.org/display.cgi?uids=16177183}, day = {21}, doi = {10.1093/nar/gki849}, issn = {0305-1048}, journal = {Nucl. Acids Res.}, keywords = {z-dna}, month = {September}, number = {16}, pages = {5362--5370}, posted-at = {2009-11-09 08:14:08}, priority = {2}, publisher = {Oxford University Press}, title = {Modulation of ADAR1 editing activity by Z-RNA in vitro}, url = {http://dx.doi.org/10.1093/nar/gki849}, volume = {33}, year = {2005} }

TY - JOUR ID - citeulike:340650 L3 - citeulike-article-id:340650 N2 - RNA editing by A-to-I modification has been recognized as an important molecular mechanism for generating RNA and protein diversity. In mammals, it is mediated by a family of adenosine deaminases that act on RNAs (ADARs). The large version of the editing enzyme ADAR1 (ADAR1-L), expressed from an interferon-responsible promoter, has a Z-DNA/Z-RNA binding domain at its N-terminus. We have tested the in vitro ability of the enzyme to act on a 50 bp segment of dsRNA with or without a Z-RNA forming nucleotide sequence. A-to-I editing efficiency is markedly enhanced in presence of the sequence favoring Z-RNA. In addition, an alteration in the pattern of modification along the RNA duplex becomes evident as reaction times decrease. These results suggest that the local conformation of dsRNA molecules might be an important feature for target selectivity by ADAR1 and other proteins with Z-RNA binding domains. 10.1093/nar/gki849 IS - 16 JF - Nucl. Acids Res. SN - 0305-1048 EP - 5370 TI - Modulation of ADAR1 editing activity by Z-RNA in vitro PB - Oxford University Press VL - 33 SP - 5362 KW - z-dna AU - Koeris, Michael AU - Funke, Lars AU - Shrestha, Jay AU - Rich, Alexander AU - Maas, Stefan PY - 2005/09/21/ UR - http://dx.doi.org/10.1093/nar/gki849 ER -