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Article: Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: Topological features and in vivo interactions

TitleStudies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: Topological features and in vivo interactions
Authors
Issue Date2005
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 2005, v. 102 n. 20, p. 7121-7126 How to Cite?
AbstractOligosaccharyl 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. © 2005 by The National Academy of Sciences of the USA.
Persistent Identifierhttp://hdl.handle.net/10722/178881
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYan, Aen_US
dc.contributor.authorWu, Een_US
dc.contributor.authorLennarz, WJen_US
dc.date.accessioned2012-12-19T09:50:22Z-
dc.date.available2012-12-19T09:50:22Z-
dc.date.issued2005en_US
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 2005, v. 102 n. 20, p. 7121-7126en_US
dc.identifier.issn0027-8424en_US
dc.identifier.urihttp://hdl.handle.net/10722/178881-
dc.description.abstractOligosaccharyl 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. © 2005 by The National Academy of Sciences of the USA.en_US
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_US
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCytosol - Metabolismen_US
dc.subject.meshEndoplasmic Reticulum - Metabolismen_US
dc.subject.meshHexosyltransferases - Chemistry - Metabolismen_US
dc.subject.meshMembrane Proteins - Chemistry - Metabolismen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPlasmids - Geneticsen_US
dc.subject.meshPolynucleotidesen_US
dc.subject.meshSaccharomyces Cerevisiae - Metabolismen_US
dc.subject.meshSaccharomyces Cerevisiae Proteins - Chemistry - Metabolismen_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.subject.meshUbiquitins - Metabolismen_US
dc.titleStudies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: Topological features and in vivo interactionsen_US
dc.typeArticleen_US
dc.identifier.emailYan, A: ayan8@hku.hken_US
dc.identifier.authorityYan, A=rp00823en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1073/pnas.0502669102en_US
dc.identifier.pmid15886282-
dc.identifier.scopuseid_2-s2.0-18844391758en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-18844391758&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume102en_US
dc.identifier.issue20en_US
dc.identifier.spage7121en_US
dc.identifier.epage7126en_US
dc.identifier.isiWOS:000229292200014-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYan, A=8621667000en_US
dc.identifier.scopusauthoridWu, E=8595988300en_US
dc.identifier.scopusauthoridLennarz, WJ=7101750236en_US

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