Structure of the Dicer-2–R2D2 heterodimer bound to a small RNA duplex

In flies, Argonaute2 (Ago2) and small interfering RNA (siRNA) form an RNA-induced silencing complex to repress viral transcripts 1 . The RNase III enzyme Dicer-2 associates with its partner protein R2D2 and cleaves long double-stranded RNAs to produce 21-nucleotide siRNA duplexes, which are then loa...

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Veröffentlicht in:	Nature (London) Jg. 607; H. 7918; S. 393 - 398
Hauptverfasser:	Yamaguchi, Sonomi, Naganuma, Masahiro, Nishizawa, Tomohiro, Kusakizako, Tsukasa, Tomari, Yukihide, Nishimasu, Hiroshi, Nureki, Osamu
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	London Nature Publishing Group UK 14.07.2022 Nature Publishing Group
Schlagworte:	101/28 631/337/505 631/45/500 631/535/1258/1259 Animals Argonaute 2 protein Argonaute Proteins - metabolism Asymmetry Base Pairing Binding sites Cryoelectron Microscopy DNA helicase Drosophila melanogaster - chemistry Drosophila melanogaster - genetics Drosophila melanogaster - metabolism Drosophila Proteins - chemistry Drosophila Proteins - metabolism Drosophila Proteins - ultrastructure Electron microscopy Enzymes Humanities and Social Sciences Insects MicroRNAs MicroRNAs - metabolism Microscopy miRNA multidisciplinary Mutation Nucleotides Protein Multimerization Proteins Ribonuclease III Ribonuclease III - chemistry Ribonuclease III - metabolism Ribonuclease III - ultrastructure Ribonucleic acid RNA RNA Helicases - chemistry RNA Helicases - metabolism RNA Helicases - ultrastructure RNA Interference RNA, Double-Stranded - chemistry RNA, Double-Stranded - metabolism RNA, Double-Stranded - ultrastructure RNA, Small Interfering - chemistry RNA, Small Interfering - metabolism RNA, Small Interfering - ultrastructure RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism RNA-Binding Proteins - ultrastructure RNA-induced silencing complex RNA-Induced Silencing Complex - metabolism RNA-mediated interference Science Science (multidisciplinary) siRNA
ISSN:	0028-0836, 1476-4687, 1476-4687
Online-Zugang:	Volltext
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