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Papi interacting proteins in mitochondrial fraction of BmN4 cells

ABSTRACT: We incubated Papi-Flag in BmN4 mitochondrial lysates in the presence of 32P-ATP. Upon incubation, Papi-Flag was 32P-labeled, suggesting the presence of kinases for Papi in the fraction. Papi-Flag was immunoprecipitated after incubation in mitochondrial lysates under ATP-free conditions. The proteins were eluted from the beads with a high salt buffer and subjected to LC-MS/MS. This identified six proteins of which were annotated as kinases.

ORGANISM(S): Bombyx Mori

SUBMITTER: Mikiko C. Siomi

PROVIDER: PXD027396 | JPOST Repository | Tue Feb 01 00:00:00 GMT 2022

REPOSITORIES: jPOST

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			Action	DRS
	190809yam01_0820DS120_2ul.raw	Raw
	190809yam01_0820DS120_2ul_ySW18b_pSTY5.msf	Msf
	190809yam01_0820DS120_2ul_ySW18b_pSTY5.pdResult	Other
	190809yam01_0820DS120_2ul_ySW18b_pSTY5_PSM.xlsx	Xlsx
	190809yam02_0820DS120_2ul.raw	Raw

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Publications

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

Yamada Hiromi H Nishida Kazumichi M KM Iwasaki Yuka W YW Isota Yosuke Y Negishi Lumi L Siomi Mikiko C MC

Nature communications 20220321 1

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 ...[more]

PMID: 35314687

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