Ago-2, dAgo2, Argonaute
Gene model reviewed during 5.45
Low-frequency RNA-Seq exon junction(s) not annotated.
None of the polypeptides share 100% sequence identity.
Interacts with Fmr1, Dcr-1 and vig to form the RNA-induced silencing complex (RISC), a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are RpL5, RpL11 and Rm62 (PubMed:11498593, PubMed:14508492, PubMed:12368261). As part of the RISC complex, interacts with Tudor-SN (PubMed:14508492).
(Microbial infection) Interacts with cricket paralysis virus protein 1A; this interaction may block the RISC activity.
PAZ domain provides a major contribution for nucleic acid recognition. PAZ binds oligonucleotides of different lengths and has a strong preference for single-stranded nucleic acids (ssRNA or SSDNA) or RNA duplexes with single-stranded 3' overhangs. Can bind the characteristic two-base 3' overhangs of siRNAs, indicating that it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\AGO2 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\AGO2 in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for identity of: AGO2 CG7439
Source for merge of: AGO2 CG13452
"dop" is not allelic to "AGO2".
In contrast to what is stated in FBrf0194224, the "drop out" complementation group is not allelic to "AGO2". Recently isolated mRNA null mutations of the AGO2 locus fully complement dop mutant alleles. The molecular lesions of dop mutant alleles were reported in FBrf0194224 to represent in frame deletions of glutamine rich repeats (GRR) in the amino-terminus of AGO2. Analysis of 24 different D.melanogaster haplotypes show that the amino-terminal domain of AGO2 is highly variable and that the alteration of the amino-terminal GRR pattern observed in the dop allele is not unique. The GRR haplotype of dop is not the cause of the developmental phenotype of embryos derived from homozygous mothers. A D.melanogaster strain with the identical GRR haplotype does not exhibit gross developmental defects.
Annotations CG7439 and CG13452 merged as CG7439 in release 3 of the genome annotation.
The N-terminal glutamine rich repeat (GRR) domain of the long isoform of AGO2 appears to be subject to rapid evolution, with extensive variation in GRR copy number being seen among D. melanogaster strains isolated from natural and laboratory populations. GRR variation does not cause striking defects in embryonic development and assembly of the RNA induced silencing complex is unimpaired in embryos when GRR copy number is altered. The AGO2 locus also produces a putative short isoform that does not contain the N-terminal GRR containing domain.
Many miRNA* species, unlike their partner mature miRNAs, are preferentially incorporated into the AGO2 complex and are 3' modified. The miRNA strand selection of AGO2 is very sensitive to the base-pairing status of the 9th and 10th position of the miRNA duplex.
AGO2 binds endogenous short interfering RNAs (esiRNAs) derived from retrotransposons and esiRNAs arising from stem-loop structures.
The Dcr-2-r2d2 heterodimer acts as a gatekeeper for the assembly of AGO2 complexes, promoting the incorporation of siRNAs and disfavoring miRNAs as loading substrates for AGO2. A separate mechanism acts in parallel to favor miRNA/miRNA* duplexes and exclude siRNAs from assembly into AGO1 complexes.
dsRNA made from templates generated with primers directed against this gene are used to infer a role for this gene in the miRNA pathway.
AGO2 is not required for repeat-associated small interfering RNA (rasiRNA) production.
In vitro assays show that the AGO2 protein directly receives the double-stranded siRNA from the RISC complex machinery and cleaves the siRNA passenger strand, releasing the single-stranded guide.
AGO2 protein binds both strands of siRNA and cleaves the anti-guide strand to produce active RISC.
dsRNA has been made from templates generated with primers directed against this gene.
The orientation of the Dcr-2/r2d2 protein heterodimer on the siRNA duplex determines which siRNA strand associates with the core RISC (RNA-induced silencing complex) protein AGO2. r2d2 protein binds the siRNA end with the greatest double-stranded character, thereby orienting the Dcr-2/r2d2 heterodimer on the siRNA duplex. Strong binding by the r2d2 protein requires a 5'-phosphate on the siRNA strand that is excluded from the RISC.