Quantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae.

ABSTRACT: Asparagine-linked glycosylation is a common posttranslational protein modification regulating the structure, stability and function of many proteins. The N-linked glycosylation machinery involves enzymes responsible for the assembly of the lipid-linked oligosaccharide (LLO), which is then transferred to the asparagine residues on the polypeptides by the enzyme oligosaccharyltransferase (OST). A major goal in the study of protein glycosylation is to establish quantitative methods for the analysis of site-specific extent of glycosylation. We developed a sensitive approach to examine glycosylation site occupancy in Saccharomyces cerevisiae by coupling stable isotope labeling (SILAC) approach to parallel reaction monitoring (PRM) mass spectrometry (MS). We combined the method wit

SUBMITTER: Poljak K 

PROVIDER: S-EPMC5750847 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature