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PtCaf1 interacted proteins in EV and PtGTSF1 KD of Paramecium tetraurelia

ABSTRACT: The DNA fragment of PtCAF1, one of the core component of PRC2, is fused with FlagHA and transformed into the macronuclear of Paramecium tetraurelia. The interacted proteins of PtCaf1 in Empty vector (EV) control and PtGTSF1 silenced cells were immunoprecipitated with anti-HA antibody, followed with mass spectrometry.

INSTRUMENT(S):

ORGANISM(S): Paramecium Tetraurelia

SUBMITTER: Chundi Wang

LAB HEAD: Chundi Wang

PROVIDER: PXD054662 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	PtCAF1_E_019_1.raw	Raw
	PtCAF1_E_019_2.raw	Raw
	PtCAF1_E_EV_1.raw	Raw
	PtCAF1_E_EV_2.raw	Raw
	proteinGroups.txt	Txt

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Publications

GTSF1 is required for transposon silencing in the unicellular eukaryote Paramecium tetraurelia.

Wang Chundi C Lyv Liping L Solberg Therese T Zhang Haoyue H Wen Zhiwei Z Gao Feng F

Nucleic acids research 20241101 21

The PIWI-interacting RNA (piRNA) pathway is crucial for transposon repression and the maintenance of genomic integrity. Gametocyte-specific factor 1 (GTSF1), a PIWI-associated protein indispensable for transposon repression, has been recently shown to potentiate the catalytic activity of PIWI in many metazoans. Whether the requirement of GTSF1 extends to PIWI proteins beyond metazoans is unknown. In this study, we identified a homolog of GTSF1 in the unicellular eukaryote Paramecium tetraurelia ...[more]

PMID: 39441077

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