Abstract
Heat-shock proteins (Hsps) are molecular chaperones that control protein folding and function. Argonaute 2 (Ago2), the effector in RNA interference (RNAi), is associated with Hsp90; however, its function in RNAi remains elusive. Here we show that Hsp90 is required for Ago2 to receive the small interfering RNA (siRNA) duplex from the RNA-induced silencing complex–loading complex in RNAi, suggesting a model where Hsp90 modifies Ago2 conformation to accommodate the siRNA duplex.
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25 August 2010
In the version of this article initially published, “2′-O-methyl group at the 10th nucleotide” should have read “2′-O-methyl groups at the 9th and 10th nucleotides.” The error has been corrected in the HTML and PDF versions of the article.
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Acknowledgements
We thank K. Miyoshi and T. Yoshihisa for providing technical advice and other members of the Siomi laboratory for discussions. This work was supported by Ministry of Education, Culture, Sports, Science and Technology of Japan grants to H.S. and M.C.S. M.C.S. is supported by Core Research for Evolutional Science and Technology from the Japan Science and Technology Agency.
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T.M. and A.T. conducted experiments; T.M., A.T., H.S. and M.C.S. designed experiments, interpreted data and prepared the manuscript.
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Miyoshi, T., Takeuchi, A., Siomi, H. et al. A direct role for Hsp90 in pre-RISC formation in Drosophila. Nat Struct Mol Biol 17, 1024–1026 (2010). https://doi.org/10.1038/nsmb.1875
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DOI: https://doi.org/10.1038/nsmb.1875
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