All in One: Leishmania major STT3 Proteins Substitute for the Whole Oligosaccharyltransferase Complex in Saccharomyces cerevisiae

Nasab, Farnoush Parsaie, Schulz, Benjamin L., Gamarro, Francisco, Parodi, Armando J. and Aebi, Markus (2008) All in One: Leishmania major STT3 Proteins Substitute for the Whole Oligosaccharyltransferase Complex in Saccharomyces cerevisiae. Molecular Biology of the Cell, 19 9: 3758-3768. doi:10.1091/mbc.E08-05-0467

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Author Nasab, Farnoush Parsaie
Schulz, Benjamin L.
Gamarro, Francisco
Parodi, Armando J.
Aebi, Markus
Title All in One: Leishmania major STT3 Proteins Substitute for the Whole Oligosaccharyltransferase Complex in Saccharomyces cerevisiae
Formatted title
All in One: Leishmania major STT3 Proteins Substitute for the Whole Oligosaccharyltransferase Complex in Saccharomyces cerevisiae
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2008-09
Sub-type Article (original research)
DOI 10.1091/mbc.E08-05-0467
Open Access Status File (Publisher version)
Volume 19
Issue 9
Start page 3758
End page 3768
Total pages 11
Place of publication United States
Publisher American Society for Cell Biology
Language eng
Subject 0601 Biochemistry and Cell Biology
Formatted abstract
The transfer of lipid-linked oligosaccharide to asparagine residues of polypeptide chains is catalyzed by oligosaccharyltransferase (OTase). In most eukaryotes, OTase is a hetero-oligomeric complex composed of eight different proteins, in which the STT3 component is believed to be the catalytic subunit. In the parasitic protozoa Leishmania major, four STT3 paralogues, but no homologues to the other OTase components seem to be encoded in the genome. We expressed each of the four L. major STT3 proteins individually in Saccharomyces cerevisiae and found that three of them, LmSTT3A, LmSTT3B, and LmSTT3D, were able to complement a deletion of the yeast STT3 locus. Furthermore, LmSTT3D expression suppressed the lethal phenotype of single and double deletions in genes encoding other essential OTase subunits. LmSTT3 proteins did not incorporate into the yeast OTase complex but formed a homodimeric enzyme, capable of replacing the endogenous, multimeric enzyme of the yeast cell. Therefore, these protozoan OTases resemble the prokaryotic enzymes with respect to their architecture, but they used substrates typical for eukaryotic cells: N-X-S/T sequons in proteins and dolicholpyrophosphate-linked high mannose oligosaccharides.
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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