Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins

  1. Yukihide Tomari1,3,6
  1. 1Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
  2. 2Department of Agricultural and Environmental Biology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan
  3. 3Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

    1. ↵4 These authors contributed equally to this work.

    • ↵5 Present address: Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.

    Abstract

    PIWI-interacting RNAs (piRNAs) defend the genome against transposon activity in animal gonads. The Hsp90 chaperone machinery has been implicated in the piRNA pathway, but its exact role remains obscure. Here, we examined the effect of 17-N-allylamino-17-demethoxygeldanamycin (17-AAG), an Hsp90-specific inhibitor, on the piRNA pathway. In the silkworm ovary-derived BmN4 cells, 17-AAG treatment reduced the level of piRNAs and PIWI proteins. In vitro, the 5′-nucleotide preference upon precursor piRNA loading was compromised by 17-AAG, whereas 3′-end trimming and 2′-O-methylation were unaffected. Our data highlight a role of Hsp90 in accurate loading of precursor piRNAs into PIWI proteins.

    Keywords

    Footnotes

    • Received November 5, 2012.
    • Accepted April 8, 2013.

    This Article

    1. Published in Advance May 16, 2013, doi: 10.1261/rna.037200.112 RNA Copyright © 2013 RNA Society

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