<<< Full experiment listing

PXD024590

PXD024590 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAnalysis of the substrate specificities and reaction kinetics of the yeast oligosaccharyltransferase isoforms
DescriptionOligosaccharyltransferase (OST) catalyzes the central step in N-linked protein glycosylation, the transfer of a pre-assembled oligosaccharide from its lipid carrier onto asparagine residues of secretory proteins. The prototypic hetero-octameric OST complex from the yeast Saccharomyces cerevisiae exists as two isoforms that contain either Ost3p or Ost6p. These two OST complexes have different protein substrate specificities in vivo. The two OST complexes were purified from genetically engineered strains expressing only one isoform. The kinetic properties and substrate specificities were characterized using a quantitative in vitro glycosylation assay with short peptides and different synthetic lipid-linked oligosaccharide (LLO) substrates. We showed that the peptide sequence close to the glycosylation sequon affected peptide affinity and turnover rate. The length of the lipid moiety affected LLO affinity, while the lipid double bond stereochemistry had a greater influence on LLO turnover rates. The two OST complexes had similar affinities for both the peptide and LLO substrates but showed significantly different turnover rates.
HostingRepositoryPRIDE
AnnounceDate2021-05-19
AnnouncementXMLSubmission_2021-05-19_00:44:03.381.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD024590
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterChia-wei Lin
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListN-acetylhexosaminylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-03-08 22:54:27ID requested
12021-05-19 00:44:03announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: yeast oligosaccharyltransferase, site-occupancy, substract specificity
Contact List
Prof. Markus Aebi
contact affiliationInstitute of Microbiology, ETH Zurich
contact emailmarkus.aebi@micro.biol.ethz.ch
lab head
Chia-wei Lin
contact affiliationFunctional genomics center Zurich
contact emaillin.chiawei@fgcz.ethz.ch
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/05/PXD024590
PRIDE project URI
Repository Record List
[ + ]