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Glycobiology Advance Access published online on August 11, 2005
Glycobiology, doi:10.1093/glycob/cwj025
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Received July 4, 2005
Accepted July 29, 2005

Article

The 3.4 kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast

Urs Spirig 1 +, Daniel Bodmer 1 +, Michael Wacker 1, Patricie Burda 1, and Markus Aebi 1*

1 Institute for Microbiology, ETH Zurich, CH-8092 Zurich, Switzerland

* To whom correspondence should be addressed.
Markus Aebi, E-mail: aebi{at}micro.biol.ethz.ch


  Abstract

In the central reaction of N-linked glycosylation, the oligosaccharyltransferase complex (OTase) catalyzes the transfer of a lipid-linked core-oligosaccharide onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum. The Saccharomyces cerevisiae Otase has been shown to consist of at least eight subunits. We analyzed this enzyme complex, applying the technique of blue native gel electrophoresis. Using available antibodies, six different subunits were detected in the wild-type complex, including Stt3p, Ost1p, Wbp1p, Swp1p, Ost3p, and Ost6p. We demonstrate that the small 3.4 kDa subunit Ost4p is required for incorporation of either Ost3p or Ost6p into the complex, resulting in two, functionally distinct OTase complexes in vivo. Ost3p and Ost6p are not absolutely required for oligosaccharyltransferase activity, but modulate the affinity of the enzyme towards different protein substrates.

Keywords: blue native gel electrophoresis/N-linked protein glycosylation/oligosaccharyltransferase/Saccharomyces cerevisiae.
+these two authors contributed equally to this study
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