Long RNA hairpins that contain inosine are present in Caenorhabditis elegans poly(A)+ RNA.
Adenosine deaminases that act on RNA (ADARs) are RNA-editing enzymes that convert adenosine to inosine within double-stranded RNA. In the 12 years since the discovery of ADARs only a few natural substrates have been identified. These substrates were found by chance, when genomically encoded adenosines were identified as guanosines in cDNAs. To advance our understanding of the biological roles of ADARs, we developed a method for systematically identifying ADAR substrates. In our first application of the method, we identified five additional substrates in Caenorhabditis elegans. Four of those substrates are mRNAs edited in untranslated regions, and one is a noncoding RNA edited throughout its length. The edited regions are predicted to form long hairpin structures, and one of the RNAs encodes POP-1, a protein involved in cell fate decisions.
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University of Utah, Department of Biochemistry/Howard Hughes Medical Institute, 50 North Medical Drive, Salt Lake City, UT 84132, USA.
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D020413:3' Untranslated Regions / Q000737:chemistry; D000241:Adenosine / Q000378:metabolism; D000243:Adenosine Deaminase / Q000378:metabolism; D000818:Animals; D001483:Base Sequence; D017173:Caenorhabditis elegans / Q000235:genetics* / Q000378:metabolism; D006151:Guanosine / Q000378:metabolism; D007288:Inosine; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D017393:RNA Editing; D018510:RNA, Helminth / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction
D020413:3' Untranslated Regions; D018510:RNA, Helminth; D012333:RNA, Messenger; D006151:Guanosine; D007288:Inosine; D000243:Adenosine Deaminase; D000241:Adenosine