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Related Experiment Videos

The N-oligosaccharyltransferase complex from yeast

R Knauer1, L Lehle

  • 1Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, Germany.

FEBS Letters
|May 9, 1994
PubMed
Summary
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N-Oligosaccharyltransferase (NOT) is crucial for N-glycosylation in eukaryotes. This study identifies a conserved four-protein complex in yeast, homologous to the mammalian enzyme, revealing conserved organization of this essential pathway.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • N-Oligosaccharyltransferase (N-OT) mediates N-glycosylation of proteins in the endoplasmic reticulum.
  • This pathway is essential and highly conserved across eukaryotic organisms.

Purpose of the Study:

  • To characterize the enzymatic complex responsible for N-glycosylation in Saccharomyces cerevisiae.
  • To investigate the conservation of N-OT complex composition between yeast and mammals.

Main Methods:

  • Isolation of an enzymatically active N-OT complex from yeast microsomal membranes.
  • Protein identification and molecular mass determination.
  • Sequence homology analysis comparing yeast and mammalian N-OT components.

Main Results:

Related Experiment Videos

  • A four-protein N-OT complex was isolated from yeast, comprising Wbp1p, Swp1p, a 60/62 kDa protein (homologous to ribophorin I), and a 34 kDa protein.
  • Yeast Wbp1p and Swp1p show homology to mammalian OST 48 and ribophorin II, respectively.
  • The identified yeast proteins share homology with known subunits of the mammalian N-OT complex.

Conclusions:

  • The N-glycosylation enzyme complex in yeast shares significant structural and functional conservation with its mammalian counterpart.
  • This study highlights the conserved organization of N-OT activity across eukaryotes, underscoring the fundamental nature of this post-translational modification.