Hsp90 facilitates accurate loading of precursor piRNAs into PIWI proteins

Abstract

This paper provides evidence that the Hsp90 chaperone machinery participates in loading of piRNAs by PIWI proteins. The chaperone appears to influence correct 5′-nucleotide preference.

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.