DUF283 domain of Dicer proteins has a double-stranded RNA-binding fold.
Two RNases, Dicer and Argonaute, are at the heart of the RNA interference (RNAi) molecular machinery responsible for gene silencing. Both RNases contain multiple domains, most of which have been characterized or have functions that can be predicted based on sequence comparisons. However, Dicers of higher eukaryotes contain the domain known as DUF283 which at present has no assigned role. Using sensitive profile-profile comparisons, we detected a divergent double-stranded RNA-binding domain coinciding with the DUF283 of Dicer. This finding has potential implications regarding the mechanistic role of Dicer in RNAi.
Dlakić
Mensur
M
Department of Microbiology, Montana State University Bozeman, MT 59717, USA. mdlakic@montana.edu
D000595:Amino Acid Sequence; D000818:Animals; D053487:DEAD-box RNA Helicases / Q000737:chemistry*; D004722:Endoribonucleases / Q000737:chemistry*; D020868:Gene Silencing; D006801:Humans; D008390:Markov Chains; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D012330:RNA, Double-Stranded / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry*; D043244:Ribonuclease III; D017386:Sequence Homology, Amino Acid
D012330:RNA, Double-Stranded; D016601:RNA-Binding Proteins; D004722:Endoribonucleases; C408087:DICER1 protein, human; D043244:Ribonuclease III; D053487:DEAD-box RNA Helicases