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Phosphorylation sites that influences the RNA-binding activity of Papi

ABSTRACT: We conducted UV cross-linking immunoprecipitation (CLIP) with and without phosphatase inhibitor and compared the outcome. The topmost band on the western blots appeared more prominent with the inhibitor. The RNA-binding activity of the band was also stronger with the inhibitor. We isolated the band and subjected to LC-MS/MS to identify the phosphorylated residues.

ORGANISM(S): Bombyx Mori

SUBMITTER: Mikiko C. Siomi

PROVIDER: PXD027395 | JPOST Repository | Tue Feb 01 00:00:00 GMT 2022

REPOSITORIES: jPOST

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			Action	DRS
	S1a_190807yam04_0820DS90_1ul.raw	Raw
	S1a_190807yam04_0820DS90_1ul_ySW18b_pSTY5.msf	Msf
	S1a_190807yam04_0820DS90_1ul_ySW18b_pSTY5.pdResult	Other
	S1a_190807yam04_0820DS90_1ul_ySW18b_pSTY5_PSM.xlsx	Xlsx
	S1b190807yam04_0809DS90_1ul.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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