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Article: New findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker

TitleNew findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker
Authors
Issue Date2003
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2003, v. 278 n. 35, p. 33078-33087 How to Cite?
AbstractAt present, there is very limited knowledge about the structural organization of the yeast oligosaccharyl transferase (OT) complex and the function of each of its nine subunits. Because of the failure of the yeast two-hybrid system to reveal interactions between luminal domains of these subunits, we utilized a membrane permeable, thiocleavable cross-linking reagent dithiobis-succinimidyl propionate to biochemically study the interactions of various OT subunits. Four essential gene products, Ost1p, Wbp1p, Swp1p, and Stt3p were shown to be cross-linked to each other in a pairwise fashion. In addition, Ost1p was found to be cross-linked to all other eight OT subunits individually. This led us to propose that Ost1p may reside in the core of the OT complex and could play an important role in its assembly. Ost4p and Ost5p were found to only interact with specific components of the OT complex and may function as an additional anchor for optimal stability of Stt3p and Ost1p in the membrane, respectively. Interestingly, Ost3p and Ost6p subunits exhibited a surprisingly identical pattern of cross-linking to other subunits, which is consistent with their proposed redundant function. Based on these findings, we analyzed the distribution of the lysine residues that are likely to be involved in cross-linking of OT subunits and propose that the OT subunits interact with each other through either their transmembrane domains and/or a region proximal to it, rather than through their luminal or cytoplasmic domains.
Persistent Identifierhttp://hdl.handle.net/10722/178807
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYan, Aen_US
dc.contributor.authorAhmed, Een_US
dc.contributor.authorYan, Qen_US
dc.contributor.authorLennarz, WJen_US
dc.date.accessioned2012-12-19T09:49:51Z-
dc.date.available2012-12-19T09:49:51Z-
dc.date.issued2003en_US
dc.identifier.citationJournal Of Biological Chemistry, 2003, v. 278 n. 35, p. 33078-33087en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/178807-
dc.description.abstractAt present, there is very limited knowledge about the structural organization of the yeast oligosaccharyl transferase (OT) complex and the function of each of its nine subunits. Because of the failure of the yeast two-hybrid system to reveal interactions between luminal domains of these subunits, we utilized a membrane permeable, thiocleavable cross-linking reagent dithiobis-succinimidyl propionate to biochemically study the interactions of various OT subunits. Four essential gene products, Ost1p, Wbp1p, Swp1p, and Stt3p were shown to be cross-linked to each other in a pairwise fashion. In addition, Ost1p was found to be cross-linked to all other eight OT subunits individually. This led us to propose that Ost1p may reside in the core of the OT complex and could play an important role in its assembly. Ost4p and Ost5p were found to only interact with specific components of the OT complex and may function as an additional anchor for optimal stability of Stt3p and Ost1p in the membrane, respectively. Interestingly, Ost3p and Ost6p subunits exhibited a surprisingly identical pattern of cross-linking to other subunits, which is consistent with their proposed redundant function. Based on these findings, we analyzed the distribution of the lysine residues that are likely to be involved in cross-linking of OT subunits and propose that the OT subunits interact with each other through either their transmembrane domains and/or a region proximal to it, rather than through their luminal or cytoplasmic domains.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshCross-Linking Reagents - Pharmacologyen_US
dc.subject.meshCytoplasm - Metabolismen_US
dc.subject.meshDetergents - Pharmacologyen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshHexosyltransferasesen_US
dc.subject.meshLipid Metabolismen_US
dc.subject.meshMembrane Proteins - Chemistryen_US
dc.subject.meshMicrosomes - Metabolismen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshPlasmids - Metabolismen_US
dc.subject.meshPrecipitin Testsen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshSaccharomyces Cerevisiae Proteinsen_US
dc.subject.meshSchizosaccharomyces - Metabolismen_US
dc.subject.meshTransferases - Chemistry - Metabolismen_US
dc.subject.meshTwo-Hybrid System Techniquesen_US
dc.titleNew findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linkeren_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.doi10.1074/jbc.M305337200en_US
dc.identifier.pmid12805367-
dc.identifier.scopuseid_2-s2.0-0041856249en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0041856249&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume278en_US
dc.identifier.issue35en_US
dc.identifier.spage33078en_US
dc.identifier.epage33087en_US
dc.identifier.isiWOS:000184901800073-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYan, A=8621667000en_US
dc.identifier.scopusauthoridAhmed, E=7102824466en_US
dc.identifier.scopusauthoridYan, Q=55106768500en_US
dc.identifier.scopusauthoridLennarz, WJ=7101750236en_US

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