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


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.

SUBMITTER: Yamazaki H 

PROVIDER: S-EPMC10081994 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

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

Yamazaki Hiroya H   Namba Yurika Y   Kuriyama Shogo S   Nishida Kazumichi M KM   Kajiya Asako A   Siomi Mikiko C MC  

Nature communications 20230407 1


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 e  ...[more]

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