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dc.contributor.authorSilberstein, Susana
dc.contributor.authorKelleher, Daniel J.
dc.contributor.authorGilmore, Reid
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:24Z
dc.date.available2022-08-23T16:54:24Z
dc.date.issued1992-11-25
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1992 Nov 25;267(33):23658-63.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid1429707
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42494
dc.description.abstractOligosaccharyltransferase has been purified from canine microsomal membranes as a protein complex with three nonidentical subunits of 66, 63/64, and 48 kDa. The 66- and 63/64-kDa subunits were found to be identical to ribophorins I and II, respectively. The ribophorins are integral membrane glycoproteins that were previously shown to be localized exclusively to the rough endoplasmic reticulum. The 48-kDa subunit (OST48) of the oligosaccharyltransferase complex is not a glycoprotein and is not recognized by antibodies to either ribophorin. Here, we describe the characterization of a cDNA clone that encodes OST48. Like ribophorins I and II, OST48 was found to be an integral membrane protein, with the majority of the polypeptide located within the lumen of the endoplasmic reticulum. OST48 does not show significant amino acid sequence homology to either ribophorin I or II. A 45-kDa integral membrane protein, designated WBP1, from the yeast Saccharomyces cerevisiae was found to be 25% identical in sequence to OST48. Recently, WBP1 was shown to be essential for in vivo and in vitro expression of oligosaccharyltransferase activity in yeast. We conclude that OST48 and WBP1 are homologous gene products.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=1429707&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/267/33/23658.long
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectCell Line
dc.subjectCloning, Molecular
dc.subjectDogs
dc.subjectFungal Proteins
dc.subject*Hexosyltransferases
dc.subjectMacromolecular Substances
dc.subjectMembrane Proteins
dc.subjectMicrosomes
dc.subjectMolecular Sequence Data
dc.subjectMolecular Weight
dc.subjectPancreas
dc.subjectPolymerase Chain Reaction
dc.subjectRestriction Mapping
dc.subjectSaccharomyces cerevisiae
dc.subjectSequence Homology, Amino Acid
dc.subjectTransferases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleThe 48-kDa subunit of the mammalian oligosaccharyltransferase complex is homologous to the essential yeast protein WBP1
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry glycotransferase)
dc.source.volume267
dc.source.issue33
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/838
dc.identifier.contextkey579725
html.description.abstract<p>Oligosaccharyltransferase has been purified from canine microsomal membranes as a protein complex with three nonidentical subunits of 66, 63/64, and 48 kDa. The 66- and 63/64-kDa subunits were found to be identical to ribophorins I and II, respectively. The ribophorins are integral membrane glycoproteins that were previously shown to be localized exclusively to the rough endoplasmic reticulum. The 48-kDa subunit (OST48) of the oligosaccharyltransferase complex is not a glycoprotein and is not recognized by antibodies to either ribophorin. Here, we describe the characterization of a cDNA clone that encodes OST48. Like ribophorins I and II, OST48 was found to be an integral membrane protein, with the majority of the polypeptide located within the lumen of the endoplasmic reticulum. OST48 does not show significant amino acid sequence homology to either ribophorin I or II. A 45-kDa integral membrane protein, designated WBP1, from the yeast Saccharomyces cerevisiae was found to be 25% identical in sequence to OST48. Recently, WBP1 was shown to be essential for in vivo and in vitro expression of oligosaccharyltransferase activity in yeast. We conclude that OST48 and WBP1 are homologous gene products.</p>
dc.identifier.submissionpathoapubs/838
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.source.pages23658-63


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