ArticleProceedings of the National Academy of Sciences of the United States of America2005
Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
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- BCL2-ASSOCIATED ATHANOGENE4 Regulates the KAT1 Potassium Channel and Controls Stomatal Movement.Plant physiology · 2019Article
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- Single-subunit oligosaccharyltransferases ofThe Journal of biological chemistry · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- OST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylation.Journal of cell science · 2013Article
- Analysis of Sec61p and Ssh1p interactions in the ER membrane using the split-ubiquitin system.BMC cell biology · 2013Article
- The contribution of systematic approaches to characterizing the proteins and functions of the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- DOLICHOL PHOSPHATE MANNOSE SYNTHASE1 mediates the biogenesis of isoprenyl-linked glycans and influences development, stress response, and ammonium hypersensitivity in Arabidopsis.The Plant cell · 2011Article
- Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Dimeric organization of the yeast oligosaccharyl transferase complex.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- LOW PSII ACCUMULATION1 is involved in efficient assembly of photosystem II in Arabidopsis thaliana.The Plant cell · 2006Article
- Generation, annotation, and analysis of an extensive Aspergillus niger EST collection.BMC microbiology · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Oligosaccharyl transferase (OT) catalyzes the cotranslational N-glycosylation of nascent polypeptides in the endoplasmic reticulum in all eukaryotic systems. Due to the inherent difficulty in characterizing this membrane protein complex, the mode of enzymatic action has not been resolved. Here, we used a membrane protein two-hybrid approach, the split-ubiquitin system, to address two aspects of the enzyme complex in yeast: the topological features, as well as the in vivo interactions of all of the components. We investigated the N- and C-terminal orientation of these proteins and the presence or the absence of a cleavable signal sequence at their N termini. We found that Ost2p and Stt3p have only their N terminus located in the cytosol, whereas Ost3p and Swp1p have only their C terminus oriented in the cytosol. In the case of Ost5p and Ost6p, both their N and C termini are present in the cytosol. These findings also suggested that Ost2p, Stt3p, Ost5p, and Ost6p do not have a cleavable N-terminal signal sequence. The pairwise analysis of in vivo interactions among all of the OT subunits demonstrated that OT subunits display specific interactions with each other in a functional complex. By comparing this interaction pattern with that detected in vitro in a nonfunctional complex, we proposed that a distinct conformation rearrangement takes place when the enzyme complex changes from the nonfunctional state to the activated functional state. This finding is consistent with earlier work by others indicating that OT exhibits allosteric properties.
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