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

Nat Struct Mol Biol. 2010 Aug;17(8):1024-6. doi: 10.1038/nsmb.1875. Epub 2010 Jul 18.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / metabolism*
  • HSP90 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / metabolism*
  • Molecular Sequence Data
  • RNA Interference
  • RNA Processing, Post-Transcriptional
  • RNA, Small Interfering / genetics
  • RNA, Small Interfering / metabolism
  • RNA-Induced Silencing Complex / metabolism*

Substances

  • Drosophila Proteins
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Hsp83 protein, Drosophila
  • RNA, Small Interfering
  • RNA-Induced Silencing Complex