Functional replacement of Trypanosoma brucei Argonaute by the human slicer Argonaute2
- 12 April 2006
- journal article
- Published by Cold Spring Harbor Laboratory in RNA
- Vol. 12 (6) , 943-947
- https://doi.org/10.1261/rna.20806
Abstract
RNA interference (RNAi) is widespread throughout the eukaryotic lineage, from protozoa to man. Central to all RNAi phenomena is a member of the Argonaute protein family, and, in the case of dsRNA-triggered mRNA cleavage, the Ago protein functions as the RNAi endonuclease or slicer. However, at present there is no definite experimental evidence that slicer Argonautes can be interchanged between distantly related organisms. Here, we show that the human slicer Argonaute2 (HsAgo2), but not HsAgo1, functions in RNAi in the early divergent protozoan Trypanosoma brucei, thus mimicking the situation in mammalian cells. This finding indicates that the basic features of the RNAi mechanism are conserved from T. brucei to man.Keywords
This publication has 24 references indexed in Scilit:
- Crystal Structure of Argonaute and Its Implications for RISC Slicer ActivityScience, 2004
- Human Argonaute2 Mediates RNA Cleavage Targeted by miRNAs and siRNAsMolecular Cell, 2004
- Characterization of the interactions between mammalian PAZ PIWI domain proteins and DicerEMBO Reports, 2004
- Argonaute Protein in the Early Divergent Eukaryote Trypanosoma brucei: Control of Small Interfering RNA Accumulation and Retroposon Transcript AbundanceMolecular and Cellular Biology, 2004
- R2D2, a Bridge Between the Initiation and Effector Steps of the Drosophila RNAi PathwayScience, 2003
- An siRNA ribonucleoprotein is found associated with polyribosomes in Trypanosoma bruceiRNA, 2003
- A microRNA in a Multiple-Turnover RNAi Enzyme ComplexScience, 2002
- RNA interference is mediated by 21- and 22-nucleotide RNAsGenes & Development, 2001
- Domains in gene silencing and cell differentiation proteins: the novel PAZ domain and redefinition of the Piwi domainTrends in Biochemical Sciences, 2000
- An RNA-directed nuclease mediates post-transcriptional gene silencing in Drosophila cellsNature, 2000