Sort   by:  
 Page size 
ProteomicsQuantitative Rps2 BioID to monitor Asc1-dependent rearrangement at the head region of the 40S ribosome
In a previous study we applied a quantitative proximity-labeling technique called Biotin Identification (BioID, Roux et al., 2012) to analyze the microenvironment of the Gβ-like scaffold protein Asc1 (Opitz et al., 2017). The WD40-repeat protein Asc1 binds to the head region of the small 40S ribosom...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2019-11-07 | PXD015611 | Pride
Asc1 Bre5 Sro9 Bioid Def1 Stm1 Rps2 Silac Ribosome Rps3 Translation Ubp3 Saccharomyces cerevisiae Vps30 
ProteomicsSplit-TurboID with Bre5 and Rps2 in Saccharomyces cerevisiae
The in vivo labeling technique Split-Biotin identification (Split-BioID, De Munter et al., 2017, Schopp et al., 2017, Cho et al., 2020) was used to capture the common microenvironment of Bre5 and the ribosomal protein Rps2 (uS5). Biotinylated proteins were enriched from cell lysates using affinity p...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-11-10 | PXD028879 | Pride
Split-turboid Rps2 Split-bioid Us5 Silac Saccharomyces cerevisiae Ribosome Bre5 
ProteomicsProxiome at the 40S ribosomal head region according to proximity labeling MS experiments
The in vivo labeling technique Biotin identification (BioID, Roux et al., 2012) was used to capture proteins in the microenvironments of the ribosomal proteins Rps3 (uS3) and Rps20 (us10) in Saccharomyces cerevisiae. Biotinylated proteins were captured from cell lysates using affinity purification a...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-11-10 | PXD027267 | Pride
Rps20 Us10 Us3 Silac Saccharomyces cerevisiae Ribosome Rps3 Bira* Bioid 
ProteomicsAsc1p-dependent phosphorylation of Ubp3p-associated Bre5p
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). Pro...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-10-09 | PXD007858 | Pride
Bre5 Phosphorylation Ubp3 Saccharomyces cerevisiae Asc1/rack1 
ProteomicsProximity labeling of the SmSTRIPAK complex in Sordaria macrospora using the SCI1 subunit as bait to identify its SmSTRIPAK-dependent microenvironment
In this study, we used the in vivo proximity labeling biotin identification (BioID; Roux et al., 2012) method to capture proteins of the microenvironment of the striatin interacting kinase and phosphatase complex of the filamentous fungus Sordaria macrospora (SmSTRIPAK). For that, the TurboID biotin...
ORGANISM(S): Sordaria macrospora 
2026-08-19 | PXD069198 | Pride
Sordaria macrospora Turboid Stripak Proximity labeling Bioid 
ProteomicsPhosphorylation of Asc1p and Asc1p-dependent phospho-proteome
Phosphorylation of Asc1p and Asc1p-dependent phospho-proteome We determined 1) the phosphorylation sites within the Asc1 protein purified from Saccharomyces cerevisiae via its Strep-tag and 2) the Asc1p-dependent phospho-proteome. 1) Phospho-sites within tryptic peptides of Asc1p were identified usi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-12-13 | PXD003031 | Pride
Lc-msms Asc1p Rack1 Silac Signal transduction Phosphorylation Saccharomyces cerevisiae Translation 
ProteomicsCapturig the Asc1p/RACK1 microenviroment at the head region of the 40S ribosome with quantitative BioID
The Asc1 protein of Saccharomyces cerevisiae is a Gβ-like scaffold protein considered to organize the local microenvironment at the head region of ribosomes in order to link mRNA translation with cellular signaling. In this study we used the in vivo protein labeling technique proximity-dependent Bio...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-10-09 | PXD005612 | Pride
Lc-msms Asc1p Rack1 Silac Signal transduction Saccharomyces cerevisiae Bioid Translation 
ProteomicsVerticillium dahliae Frq and Frh form a Frq-Frh complex in dependence on arginine 806 (R806) of Frh
The plant pathogenic fungus Verticillium dahliae has homologs of the clock genes [Cascant-Lopez et al., 2020], which are well described in Neurospora crassa [Diernfellner et al., 2020]. In N. crassa, frequency (Frq) and the Frq-interacting RNA helicase (Frh) interact and form the Frq-Frh complex [Ch...
ORGANISM(S): Verticillium dahliae JR2 
2023-07-12 | PXD041716 | Pride
Frh Clock proteins Frq-interacting rna helicase Frq Verticillium dahliae jr2 Frequency 
ProteomicsEstablishment of TurboID proximity proteomics in the filamentous fungus Sordaria macrospora
Biotin identification (BioID) is a proximity-dependent labeling technique to study protein-protein co-localization in vivo. Although BioID has been applied in animal cells, plants and yeast, the method remained to be established in filamentous fungi. In this study, we established BioID for the filam...
ORGANISM(S): Sordaria macrospora 
2022-10-25 | PXD034217 | Pride
Sordaria macrospora Turboid Stripak Proximity labeling Bioid 
ProteomicsThe velvet protein Vel1 controls initial plant root colonization and conidia formation for xylem distribution in Verticillium wilt
Velvet domain proteins coordinate developmental processes and secondary metabolism in fungi. In this study, we characterized the role of all four velvet proteins in the life cycle of the plant pathogenic fungus Verticillium dahliae. From other fungi, the formation of different homo-and heterodimers ...
ORGANISM(S): Verticillium dahliae JR2 
2021-02-23 | PXD021861 | Pride
Velvet domain Verticillium dahliae Velvet proteins Plant pathogen 
Sort   by:  
 Page size