Siwi cooperates with Par-1 kinase to resolve the autoinhibitory effect of Papi for Siwi-piRISC biogenesis

Hiromi Yamada, Kazumichi M. Nishida, Yuka W. Iwasaki, Yosuke Isota, Lumi Negishi and Mikiko C. Siomi ()
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Hiromi Yamada: The University of Tokyo
Kazumichi M. Nishida: The University of Tokyo
Yuka W. Iwasaki: Keio University School of Medicine
Yosuke Isota: The University of Tokyo
Lumi Negishi: The University of Tokyo
Mikiko C. Siomi: The University of Tokyo

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Bombyx Papi acts as a scaffold for Siwi-piRISC biogenesis on the mitochondrial surface. Papi binds first to Siwi via the Tudor domain and subsequently to piRNA precursors loaded onto Siwi via the K-homology (KH) domains. This second action depends on phosphorylation of Papi. However, the underlying mechanism remains unknown. Here, we show that Siwi targets Par-1 kinase to Papi to phosphorylate Ser547 in the auxiliary domain. This modification enhances the ability of Papi to bind Siwi-bound piRNA precursors via the KH domains. The Papi S547A mutant bound to Siwi, but evaded phosphorylation by Par-1, abrogating Siwi-piRISC biogenesis. A Papi mutant that lacked the Tudor and auxiliary domains escaped coordinated regulation by Siwi and Par-1 and bound RNAs autonomously. Another Papi mutant that lacked the auxiliary domain bound Siwi but did not bind piRNA precursors. A sophisticated mechanism by which Siwi cooperates with Par-1 kinase to promote Siwi-piRISC biogenesis was uncovered.

Date: 2022
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DOI: 10.1038/s41467-022-29193-9

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