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Article: Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons

TitleTwo oligosaccharyl transferase complexes exist in yeast and associate with two different translocons
Authors
Issue Date2005
PublisherOxford University Press. The Journal's web site is located at http://glycob.oxfordjournals.org/
Citation
Glycobiology, 2005, v. 15 n. 12, p. 1407-1415 How to Cite?
AbstractOligosaccharyl transferase (OT) scans and selectively glycosylates -Asn-X-Thr/Ser-motifs in nascent polypeptide chains in the endoplasmic reticulum (ER). Several groups have reported different results for the composition of this enzyme complex. In this study, using a membrane protein two-hybrid approach, the split-ubiquitin system, we show that except for Ost3p and Ost6p, all of the other subunits of OT exist as dimers or oligomers in the yeast, Saccharomyces cerevisiae. Ost3p and Ost6p behave strikingly similar in a series of genetic and biochemical assays, but clearly do not exist in the same OT complex. This observation, as well as the results in an accompanying study to analyze the composition of OT complex by blue native gel electrophoresis using a series of wild-type and mutant yeast strains strongly suggests that two isoforms of the OT complex exist in the ER, differing only in the presence of Ost3p or Ost6p. Each of these two isoforms of the OT complex specifically interacts with two structurally similar, but functionally different translocon complexes: the Sec61 and the Ssh1 translocon complexes. © Published by Oxford University 2005.
Persistent Identifierhttp://hdl.handle.net/10722/178916
ISSN
2015 Impact Factor: 3.283
2015 SCImago Journal Rankings: 1.692
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYan, Aen_US
dc.contributor.authorLennarz, WJen_US
dc.date.accessioned2012-12-19T09:50:43Z-
dc.date.available2012-12-19T09:50:43Z-
dc.date.issued2005en_US
dc.identifier.citationGlycobiology, 2005, v. 15 n. 12, p. 1407-1415en_US
dc.identifier.issn0959-6658en_US
dc.identifier.urihttp://hdl.handle.net/10722/178916-
dc.description.abstractOligosaccharyl transferase (OT) scans and selectively glycosylates -Asn-X-Thr/Ser-motifs in nascent polypeptide chains in the endoplasmic reticulum (ER). Several groups have reported different results for the composition of this enzyme complex. In this study, using a membrane protein two-hybrid approach, the split-ubiquitin system, we show that except for Ost3p and Ost6p, all of the other subunits of OT exist as dimers or oligomers in the yeast, Saccharomyces cerevisiae. Ost3p and Ost6p behave strikingly similar in a series of genetic and biochemical assays, but clearly do not exist in the same OT complex. This observation, as well as the results in an accompanying study to analyze the composition of OT complex by blue native gel electrophoresis using a series of wild-type and mutant yeast strains strongly suggests that two isoforms of the OT complex exist in the ER, differing only in the presence of Ost3p or Ost6p. Each of these two isoforms of the OT complex specifically interacts with two structurally similar, but functionally different translocon complexes: the Sec61 and the Ssh1 translocon complexes. © Published by Oxford University 2005.en_US
dc.languageengen_US
dc.publisherOxford University Press. The Journal's web site is located at http://glycob.oxfordjournals.org/en_US
dc.relation.ispartofGlycobiologyen_US
dc.subject.meshAmino Acid Motifsen_US
dc.subject.meshCell Proliferationen_US
dc.subject.meshChromosomes - Chemistryen_US
dc.subject.meshCross-Linking Reagents - Pharmacologyen_US
dc.subject.meshDimerizationen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEndoplasmic Reticulum - Metabolismen_US
dc.subject.meshEpitopes - Chemistryen_US
dc.subject.meshGalactose - Metabolismen_US
dc.subject.meshHexosyltransferases - Chemistry - Physiologyen_US
dc.subject.meshImmunoprecipitationen_US
dc.subject.meshMembrane Proteins - Chemistry - Metabolism - Physiologyen_US
dc.subject.meshMembrane Transport Proteins - Chemistryen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshMutationen_US
dc.subject.meshPeptides - Chemistryen_US
dc.subject.meshPlasmids - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Isoformsen_US
dc.subject.meshProtein Transporten_US
dc.subject.meshSaccharomyces Cerevisiae - Enzymologyen_US
dc.subject.meshSaccharomyces Cerevisiae Proteins - Chemistry - Metabolism - Physiologyen_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.subject.meshUbiquitin - Chemistryen_US
dc.subject.meshBeta-Galactosidase - Metabolismen_US
dc.titleTwo oligosaccharyl transferase complexes exist in yeast and associate with two different transloconsen_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.doi10.1093/glycob/cwj026en_US
dc.identifier.pmid16096345-
dc.identifier.scopuseid_2-s2.0-28444451884en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-28444451884&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume15en_US
dc.identifier.issue12en_US
dc.identifier.spage1407en_US
dc.identifier.epage1415en_US
dc.identifier.isiWOS:000233492100017-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYan, A=8621667000en_US
dc.identifier.scopusauthoridLennarz, WJ=7101750236en_US
dc.identifier.citeulike406298-

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