Proteomics

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Mass spectrometry of PtGtsf1 interacted proteins in Paramecium tetraurelia


ABSTRACT: PtGtsf1 was fused with FlagHA and induced to express in Paramecium tetraurelia. The interacted proteins of PtGtsf1 was obtained by immunoprecipitation with anti-HA antibody, followed with mass spectrometry to identify the proteins. Meanwhile, FlagHA without PtGtsf1 was expressed in Paramecium tetraurelia as control and was performed with same procedures as PtGtsf1-FlagHA. By comparing the enrichment of proteins in PtGtsf1-FlagHA and control, the interacted proteins of PtGtsf1 in Paramecium tetraurelia were identified.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Paramecium Tetraurelia

SUBMITTER: Chundi Wang  

LAB HEAD: Chundi Wang

PROVIDER: PXD049029 | Pride | 2025-05-06

REPOSITORIES: Pride

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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]

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