biostudies-literatureOpitz NDeutsche Forschungsgemeinschaft2199-2218https://www.ebi.ac.uk/biostudies/studies/S-EPMC5724181biostudies-literatureUnknown16(12)The Asc1 protein of <i>Saccharomyces cerevisiae</i> 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 <i>Bio</i>tin <i>ID</i>entification (BioID), an <i>in vivo</i> 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 mRNA-binding proteins Sro9p and Gis2p appeared together with Scp160p, each providing ribosomes with nuclear transcripts. The cap-binding protein eIF4E (Cdc33p) and the eIF3/a-subunit (Rpg1p) were identified reflecting the encounter of proteins involved in the initiation of Molecular & cellular proteomics : MCPCapturing the Asc1p/<i>R</i>eceptor for <i>A</i>ctivated <i>C K</i>inase <i>1</i> (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast.PMC5724181GSC 226/2VA352/2–1SFB860Neumann BKrebber HOpitz NSchmitt KHofer-Pretz VBraus GHValerius OfalseCapturing the Asc1p/<i>R</i>eceptor for <i>A</i>ctivated <i>C K</i>inase <i>1</i> (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast.The Asc1 protein of <i>Saccharomyces cerevisiae</i> 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 <i>Bio</i>tin <i>ID</i>entification (BioID), an <i>in vivo</i> 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 mRNA-binding proteins Sro9p and Gis2p appeared together with Scp160p, each providing ribosomes with nuclear transcripts. The cap-binding protein eIF4E (Cdc33p) and the eIF3/a-subunit (Rpg1p) were identified reflecting the encounter of proteins involved in the initiation of 2017-01-01T00:00:00Z2017 Dec2026-05-03T03:54:07.77Z2019-03-27T00:09:22ZS-EPMC57241812898271510.1074/mcp.M116.06665410.1074/mcp.m116.066654