Proteomics

Dataset Information

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Asc1p-dependent phosphorylation of Ubp3p-associated Bre5p


ABSTRACT: The phosphorylation of Bre5p was analyzed in ASC1 wild-type and Δasc1 cells. Bre5p was co-purified from cell extracts with its GFP-tagged interaction partner Ubp3p in GFP-trap experiments. Trapped proteins were in-gel digested with trypsin and analyzed with the Q Exactive HF (Thermo Scientific). Protein and phospho-peptide identification and calculation of LFQ intensities were done with the MaxQuant software. For validation of phospho-peptides/-sites single ion monitoring by tSIM analysis was performed.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces cerevisiae  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Oliver Valerius  

LAB HEAD: Oliver Valerius

PROVIDER: PXD007858 | Pride | 2017-10-09

REPOSITORIES: pride

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Publications

Capturing the Asc1p/Receptor for Activated C Kinase 1 (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast.

Opitz Nadine N   Schmitt Kerstin K   Hofer-Pretz Verena V   Neumann Bettina B   Krebber Heike H   Braus Gerhard H GH   Valerius Oliver O  

Molecular & cellular proteomics : MCP 20171005 12


The Asc1 protein of Saccharomyces cerevisiae is a scaffold protein at the head region of ribosomal 40S that links mRNA translation to cellular signaling. In this study, proteins that colocalize with Asc1p were identified with proximity-dependent Biotin IDentification (BioID), an in vivo labeling technique described here for the first time for yeast. Biotinylated Asc1p-birA*-proximal proteins were identified and quantitatively verified against controls applying SILAC and mass spectrometry. The mR  ...[more]

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