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

Subjects

  • A Corrigendum to this article was published on 06 April 2011

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.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

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

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. 1

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

  2. 2

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

  3. 3

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

  4. 4

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

  5. 5

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

  6. 6

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

  7. 7

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

  8. 8

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

  9. 9

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

  10. 10

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

  11. 11

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

  12. 12

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

  13. 13

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

  14. 14

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

  15. 15

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

  16. 16

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

  17. 17

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

  18. 18

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

  19. 19

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

  20. 20

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

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

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.

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

Further reading