ArticleEMBO reports2021
DEAD-box polypeptide 43 facilitates piRNA amplification by actively liberating RNA from Ago3-piRISC.
Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- A model that integrates the different piRNA biogenesis pathways based on studies in silkwormCurrent research in insect science · 2025Review
- The dual role of Spn-E in supporting heterotypic ping-pong piRNA amplification in silkworms.EMBO reports · 2024Article
- An extended Tudor domain within Vreteno interconnects Gtsf1L and Ago3 for piRNA biogenesis in Bombyx mori.The EMBO journal · 2023Article
- Novel roles of PIWI proteins and PIWI-interacting RNAs in human health and diseases.Cell communication and signaling : CCS · 2023Review
- Single-cell RNA-seq uncovers dynamic processes orchestrated by RNA-binding protein DDX43 in chromatin remodeling during spermiogenesis.Nature communications · 2023Article
- Bombyx Vasa sequesters transposon mRNAs in nuage via phase separation requiring RNA binding and self-association.Nature communications · 2023Article
- Review
- Article
- Maelstrom functions in the production of Siwi-piRISC capable of regulating transposons iniScience · 2022Article
- Heterogeneous dissociation process of truncated RNAs by oligomerized Vasa helicase.Communications biology · 2021Article
- DEAD-box polypeptide 43 facilitates piRNA amplification by actively liberating RNA from Ago3-piRISC.EMBO reports · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The piRNA amplification pathway in Bombyx is operated by Ago3 and Siwi in their piRISC form. The DEAD-box protein, Vasa, facilitates Ago3-piRISC production by liberating cleaved RNAs from Siwi-piRISC in an ATP hydrolysis-dependent manner. However, the Vasa-like factor facilitating Siwi-piRISC production along this pathway remains unknown. Here, we identify DEAD-box polypeptide 43 (DDX43) as the Vasa-like protein functioning in Siwi-piRISC production. DDX43 belongs to the helicase superfamily II along with Vasa, and it contains a similar helicase core. DDX43 also contains a K-homology (KH) domain, a prevalent RNA-binding domain, within its N-terminal region. Biochemical analyses show that the helicase core is responsible for Ago3-piRISC interaction and ATP hydrolysis, while the KH domain enhances the ATPase activity of the helicase core. This enhancement is independent of the RNA-binding activity of the KH domain. For maximal DDX43 RNA-binding activity, both the KH domain and helicase core are required. This study not only provides new insight into the piRNA amplification mechanism but also reveals unique collaborations between the two domains supporting DDX43 function within the pathway.
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