A direct role for Hsp90 in pre-RISC formation in Drosophila.
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.
Miyoshi
Tomohiro
T
Keio University School of Medicine, Tokyo, Japan.
Takeuchi
Akiko
A
Siomi
Haruhiko
H
Siomi
Mikiko C
MC
D000818:Animals; D001483:Base Sequence; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D034622:RNA Interference; D012323:RNA Processing, Post-Transcriptional; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D034743:RNA-Induced Silencing Complex / Q000378:metabolism*
D029721:Drosophila Proteins; D018841:HSP90 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C089272:Hsp83 protein, Drosophila; D034741:RNA, Small Interfering; D034743:RNA-Induced Silencing Complex