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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides
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Published on: June 20, 2010

New oligosaccharyltransferase assay method.

Daisuke Kohda1, Masaki Yamada, Mayumi Igura

  • 1Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan. kohda@bioreg.kyushu-u.ac.jp

Glycobiology
|August 19, 2007
PubMed
Summary
This summary is machine-generated.

We developed a novel assay for oligosaccharyltransferase (OST) enzyme activity. This new method analyzes N-linked glycosylation without needing prior knowledge of the oligosaccharide structures, advancing glycomics research.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycoscience

Background:

  • Oligosaccharyltransferase (OST) is crucial for N-linked protein glycosylation, a vital post-translational modification across all domains of life.
  • Existing in vitro OST assays require prior knowledge of the specific oligosaccharide structures, limiting their application in unexplored areas like archaeal glycosylation.

Purpose of the Study:

  • To develop a novel, versatile in vitro assay for oligosaccharyltransferase (OST) activity.
  • To enable the study of N-linked glycosylation in systems where oligosaccharide structures are unknown, particularly in Archaea.

Main Methods:

  • A new in vitro assay utilizing fluorescently labeled peptide substrates.
  • Separation of glycopeptide products from peptide substrates using polyacrylamide gel electrophoresis (PAGE).
  • Analysis of glycopeptide formation via fluorescence gel imaging.

Main Results:

  • Demonstrated the assay's efficacy using yeast OST.
  • Successfully detected OST activity in the membrane fraction of the hyperthermophilic archaeon Pyrococcus furiosus.
  • The assay does not require a priori knowledge of the oligosaccharide moiety.

Conclusions:

  • The developed fluorescence-based PAGE assay provides a powerful new tool for studying OST activity.
  • This method overcomes limitations of existing assays, facilitating research into N-linked glycosylation across diverse organisms, including Archaea.