Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Brief Communication
  • Published:

A direct role for Hsp90 in pre-RISC formation in Drosophila

Subjects

A Corrigendum to this article was published on 06 April 2011

This article has been updated

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.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Hsp90 is required for RISC formation in Drosophila RNAi.
Figure 2: Hsp90 is required for pre-RISC formation.

Similar content being viewed by others

Change history

  • 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.

References

  1. Siomi, H. & Siomi, M.C. Nature 457, 396–404 (2009).

    Article  CAS  Google Scholar 

  2. Kim, V.N., Han, J. & Siomi, M.C. Nat. Rev. Mol. Cell Biol. 10, 126–139 (2009).

    Article  CAS  Google Scholar 

  3. Kawamata, T. & Tomari, Y. Trends Biochem. Sci. 35, 368–376 (2010).

    Article  CAS  Google Scholar 

  4. Yoda, M. et al. Nat. Struct. Mol. Biol. 17, 17–23 (2010).

    Article  CAS  Google Scholar 

  5. Miyoshi, K., Tsukumo, H., Nagami, T., Siomi, H. & Siomi, M.C. Genes Dev. 19, 2837–2848 (2005).

    Article  CAS  Google Scholar 

  6. Matranga, C., Tomari, Y., Shin, C., Bartel, D.P. & Zamore, P.D. Cell 123, 607–620 (2005).

    Article  CAS  Google Scholar 

  7. Rivas, F.V. et al. Nat. Struct. Mol. Biol. 12, 340–349 (2005).

    Article  CAS  Google Scholar 

  8. Liu, J. et al. Science 305, 1437–1441 (2004).

    Article  CAS  Google Scholar 

  9. Maniataki, E. & Mourelatos, Z. Genes Dev. 19, 2979–2990 (2005).

    Article  CAS  Google Scholar 

  10. Höck, J. et al. EMBO Rep. 8, 1052–1060 (2007).

    Article  Google Scholar 

  11. Landthaler, M. et al. RNA 14, 2580–2596 (2008).

    Article  CAS  Google Scholar 

  12. Johnston, M., Geoffroy, M.C., Sobala, A., Hay, R. & Hutvagner, G. Mol. Biol. Cell 21, 1462–1469 (2010).

    Article  CAS  Google Scholar 

  13. Tahbaz, N., Carmichael, J.B. & Hobman, T.C. J. Biol. Chem. 276, 43294–43299 (2001).

    Article  CAS  Google Scholar 

  14. Smith, D.F. et al. Mol. Cell. Biol. 15, 6804–6812 (1995).

    Article  CAS  Google Scholar 

  15. Pare, J.M. et al. Mol. Biol. Cell 20, 3273–3284 (2009).

    Article  CAS  Google Scholar 

  16. Tahbaz, N. et al. EMBO Rep. 5, 189–194 (2004).

    Article  CAS  Google Scholar 

  17. Tomari, Y., Matranga, C., Haley, B., Martinez, N. & Zamore, P.D. Science 306, 1377–1380 (2004).

    Article  CAS  Google Scholar 

  18. Tomari, Y. et al. Cell 116, 831–841 (2004).

    Article  CAS  Google Scholar 

  19. Wang, Y. et al. Nature 456, 921–926 (2008).

    Article  CAS  Google Scholar 

  20. Roe, S.M. et al. J. Med. Chem. 42, 260–266 (1999).

    Article  CAS  Google Scholar 

Download references

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.

Author information

Authors and Affiliations

Authors

Contributions

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.

Corresponding author

Correspondence to Mikiko C Siomi.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Supplementary information

Supplementary Text and Figures

Supplementary Methods and Supplementary Figure 1 (PDF 1228 kb)

Rights and permissions

Reprints and permissions

About this article

Cite this article

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

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb.1875

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing