Bombyx Vasa sequesters transposon mRNAs in nuage via phase separation requiring RNA binding and self-association

Hiroya Yamazaki, Yurika Namba, Shogo Kuriyama, Kazumichi M. Nishida, Asako Kajiya and Mikiko C. Siomi ()
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Hiroya Yamazaki: The University of Tokyo
Yurika Namba: The University of Tokyo
Shogo Kuriyama: The University of Tokyo
Kazumichi M. Nishida: The University of Tokyo
Asako Kajiya: The University of Tokyo
Mikiko C. Siomi: The University of Tokyo

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract Bombyx Vasa (BmVasa) assembles non-membranous organelle, nuage or Vasa bodies, in germ cells, known as the center for Siwi-dependent transposon silencing and concomitant Ago3-piRISC biogenesis. However, details of the body assembly remain unclear. Here, we show that the N-terminal intrinsically disordered region (N-IDR) and RNA helicase domain of BmVasa are responsible for self-association and RNA binding, respectively, but N-IDR is also required for full RNA-binding activity. Both domains are essential for Vasa body assembly in vivo and droplet formation in vitro via phase separation. FAST-iCLIP reveals that BmVasa preferentially binds transposon mRNAs. Loss of Siwi function derepresses transposons but has marginal effects on BmVasa-RNA binding. This study shows that BmVasa assembles nuage by phase separation via its ability to self-associate and bind newly exported transposon mRNAs. This unique property of BmVasa allows transposon mRNAs to be sequestered and enriched in nuage, resulting in effective Siwi-dependent transposon repression and Ago3-piRISC biogenesis.

Date: 2023
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DOI: 10.1038/s41467-023-37634-2

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