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ATP-dependent human RISC assembly pathways
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Journal Article
ATP-dependent human RISC assembly pathways
2010
Overview
Small RNAs function within the context of RNA-induced silencing complexes (RISCs) containing Argonaute (AGO) subfamily proteins. Experiments now show that human RISC assembly is uncoupled from dicing and is facilitated by ATP to load the small RNA duplexes but is not necessary to unwind them. The four human AGO proteins show no obvious structural preferences for small RNA duplexes in contrast to the situation in flies and worms where small RNAs are actively sorted into distinct AGO proteins according to their structural features.
The assembly of RNA-induced silencing complex (RISC) is a key process in small RNA–mediated gene silencing. In humans, small interfering RNAs (siRNAs) and microRNAs (miRNAs) are incorporated into RISCs containing the Argonaute (AGO) subfamily proteins Ago1–4. Previous studies have proposed that, unlike
Drosophila melanogaster
RISC assembly pathways, human RISC assembly is coupled with dicing and is independent of ATP. Here we show by careful reexamination that, in humans, RISC assembly and dicing are uncoupled, and ATP greatly facilitates RISC loading of small-RNA duplexes. Moreover, all four human AGO proteins show remarkably similar structural preferences for small-RNA duplexes: central mismatches promote RISC loading, and seed or 3′-mid (guide position 12–15) mismatches facilitate unwinding. All these features of human AGO proteins are highly reminiscent of fly Ago1 but not fly Ago2.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Adenosine Triphosphate - metabolism
/ ATP
/ Biomedical and Life Sciences
/ Eukaryotic Initiation Factor-2 - isolation & purification
/ Eukaryotic Initiation Factor-2 - metabolism
/ Eukaryotic Initiation Factors - metabolism
/ Humans
/ Proteins
/ RNA
/ RNA, Small Interfering - metabolism
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