Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MS data on PAF15 binding proteins

ABSTRACT: GST pull-down mass spectrometry data on PAF15 binding proteins

ORGANISM(S): Cellular Organisms

SUBMITTER: Masaaki Oyama

PROVIDER: PXD034088 | JPOST Repository | Fri Feb 24 00:00:00 GMT 2023

REPOSITORIES: jPOST

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	170306_chiba_GST_02.raw	Raw
	170306_hata_170306_chiba_GST_02_NCBIprot_Xenopus%20laevis.xlsx	Xlsx
	170307_chiba_PAF15_02.raw	Raw
	170307_hata_170307_chiba_PAF15_02_NCBIprot_Xenopus%20laevis.xlsx	Xlsx

Items per page:

1 - 4 of 4

Publications

The termination of UHRF1-dependent PAF15 ubiquitin signaling is regulated by USP7 and ATAD5.

Miyashita Ryota R Nishiyama Atsuya A Qin Weihua W Chiba Yoshie Y Kori Satomi S Kato Norie N Konishi Chieko C Kumamoto Soichiro S Kozuka-Hata Hiroko H Oyama Masaaki M Kawasoe Yoshitaka Y Tsurimoto Toshiki T Takahashi Tatsuro S TS Leonhardt Heinrich H Arita Kyohei K Nakanishi Makoto M

eLife 20230203

UHRF1-dependent ubiquitin signaling plays an integral role in the regulation of maintenance DNA methylation. UHRF1 catalyzes transient dual mono-ubiquitylation of PAF15 (PAF15Ub2), which regulates the localization and activation of DNMT1 at DNA methylation sites during DNA replication. Although the initiation of UHRF1-mediated PAF15 ubiquitin signaling has been relatively well characterized, the mechanisms underlying its termination and how they are coordinated with the completion of maintenance ...[more]

PMID: 36734974

Similar Datasets

Genome-wide mapping of the TET3 CXXC domain binding sites

Project description:The TET3 CXXC domain has unique DNA binding properties. It binds to DNA in a cytosine-dependent manner that prefers binding to CpG dinucleotides but is not restricted by the CpG-content, distinct from other well-characterized CXXC domains. To map the TET3 CXXC domain binding sites across the human genome, we purified the GST-tagged TET3 CXXC domain protein and performed the GST pull-down assay using the genomic DNA purified from HEK293T cells. The enriched DNA fragments were then sequenced and aligned to human genome(hg19). We used the GST pull-down assay followed by DNA deep sequencing to map the DNA bound by the TET3 CXXC domain in vitro.

2012-12-10 | E-GEOD-41551 | biostudies-arrayexpress

Genome-wide mapping of the TET3 CXXC domain binding sites

2012-12-10 | GSE41551 | GEO

Identification of SOX2-bound mRNA

Project description:In vitro pull down assay was performed using recombinant GST and GST fusion SOX2 protein to precipitate total RNA from urothelial carcinoma cell line BFTC905 Unbound RNA from both reactions and matrix-associated RNA from SOX2 pull down reaction was extracted using TRIZOL reagent

2011-10-26 | GSE33207 | GEO

Potential binding partners of profilin protein from Leishmania donovani

Project description:For identifying potential ligands of Leishmania profilin (LdPfn) protein, full length profilin was cloned and expressed with GST tag. Only GST tag protein was used as a negative control. Employing pull down assay and with the help of LC-MS, the potential binding partners of profilin protein in Leishmania promastigotes were detected.

2022-03-10 | PXD026036 | Pride

RNA pull down assay of GST-ZFP36L1 (wildtype and mutant)

Project description:RNA pull down assay of GST-ZFP36L1 (wildtype and mutant)

| PRJNA561512 | ENA

SONAR discovers RNA binding proteins from analysis of large-scale protein-protein interactomes.

Project description:RNA metabolism is controlled by an expanding yet incomplete catalog of RNA binding proteins (RBPs), many of which lack characterized RNA binding domains. Approaches to expand the RBP repertoire to discover non-canonical RBPs are currently needed. Here, HaloTag fusion pull-down of twelve nuclear and cytoplasmic RBPs followed by quantitative mass-spectrometry (MS) demonstrates that proteins interacting with multiple RBPs in an RNA-dependent manner are enriched for RBPs. This motivated SONAR, a computational approach that predicts RNA binding activity by analyzing large-scale affinity precipitation-MS protein-protein interactomes. Without relying on sequence or structure information, SONAR identifies 1923 human, 489 fly and 745 yeast RBPs, including over 100 human candidate RBPs that contain zinc finger domains. Enhanced CLIP confirms RNA binding activity and identifies transcriptome-wide RNA binding sites for SONAR-predicted RBPs, revealing unexpected RNA binding activity for disease-relevant proteins and DNA binding proteins.

2016-10-06 | GSE86035 | GEO

Identification of circGlis3 binding proteins in MS-1 cells by LC-MS

Project description:To identify the potential circGlis3 binding proteins, we extracted the total protein from MS-1 cells and performed RNA Pull-down assay. Then RNA-interacting proteins were subjected to mass spectrometry.

2021-11-15 | PXD024693 | Pride

Identification of SOX2-bound mRNA

2011-10-25 | E-GEOD-33207 | biostudies-arrayexpress

Identification of circGlis3 binding proteins in MIN6 cells by LC-MS

Project description:To identify the potential circGlis3 binding proteins, we extracted the total protein from MIN6 cells and performed RNA Pull-down assay. Then RNA-interacting proteins were subjected to mass spectrometry.

2023-11-02 | PXD037024 | Pride

RNA interactome capture in E. coli to identify RNA-binding proteins

Project description:RNA-binding proteins (RPBs) are deeply involved in fundamental cellular processes in bacteria and are vital for their survival. Despite this, few studies have so far been dedicated to globally identifying bacterial RBPs. We have adapted the RNA interactome capture (RIC) technique, originally developed for eukaryotic systems, to globally identify RBPs in bacteria. RIC takes advantage of the base pairing potential of poly(A) tails to pull-down mRNA-protein complexes. By overexpressing poly(A) polymerase I, we drastically increase the fraction of polyadenylated RNA in Escherichia coli, allowing us to pull-down RNA-protein complexes using immobilized oligo-d(T) as bait. With this approach, we identified 169 putative RBPs, roughly half of which are already annotated as RNA-binding

2022-11-13 | GSE217569 | GEO