Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins
- Natsuko Izumi1,4,
- Shinpei Kawaoka2,4,5,
- Satoshi Yasuhara2,
- Yutaka Suzuki3,
- Sumio Sugano3,
- Susumu Katsuma2,6 and
- Yukihide Tomari1,3,6
- 1Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
- 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
- 3Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
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↵4 These authors contributed equally to this work.
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.
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Footnotes
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↵6 Corresponding authors
E-mail tomari{at}iam.u-tokyo.ac.jp
E-mail katsuma{at}ss.ab.a.u-tokyo.ac.jp
- Received November 5, 2012.
- Accepted April 8, 2013.
- © 2013; Published by Cold Spring Harbor Laboratory Press for the RNA Society
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