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dc.contributor.authorNOLAN, DEREK
dc.date.accessioned2010-01-28T17:29:35Z
dc.date.available2010-01-28T17:29:35Z
dc.date.issued2005
dc.date.submitted2005en
dc.identifier.citationRubotham, J., Woods, K., Garcia-Salcedo, J.A., Pays, E. and Nolan, D.P., Characterization of two protein disulphide iosmerases from the endocytic pathway of Trypanosoma brucei, Journal of Biological Chemistry, 280, 2005, 10410, 10418en
dc.identifier.otherY
dc.identifier.urihttp://hdl.handle.net/2262/36527
dc.descriptionPUBLISHEDen
dc.description.abstractProteins from the endocytic pathway in bloodstream forms of Trypanosome brucei are modified by the addition of linear poly-N-acetyllactosamine side chains, which permits their isolation by tomato lectin affinity chromatography. Antibodies against this tomato lectin binding fraction were employed to screen a cDNA expression library from bloodstream forms of T. brucei. Two cDNAs were prominent among those selected. These cDNAs coded for two putative protein disulfide isomerases (PDIs) that respectively contained one and two double-cysteine redox-active sites and corresponded to a single domain PDI and a class 1 PDI. Assays of the purified recombinant proteins demonstrated that both proteins possess isomerase activity, but only the single domain PDI had a reducing activity. These PDIs possess a number of unusual features that distinguish them from previously characterized PDIs. The expression of both is developmentally regulated, they both co-localize with markers of the endocytic pathway, and both are modified by N-glycosylation. The larger PDI possesses N-glycans containing poly-N-acetyllactosamine, a modification that is indicative of processing in the Golgi and suggests the presence of a novel trafficking pathway for PDIs in trypanosomes. Although generally PDIs are considered essential, neither activity appeared to be essential for the growth of trypanosomes, at least in vitro.en
dc.format.extent10410en
dc.format.extent10418en
dc.format.extent661559 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relation.ispartofseriesJournal of Biological Chemistryen
dc.relation.ispartofseries280en
dc.rightsYen
dc.subjectBiochemistry
dc.titleCharacterization of two protein disulphide iosmerases from the endocytic pathway of Trypanosoma bruceien
dc.typeJournal Articleen
dc.contributor.sponsorWellcome Trusten
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/denolan
dc.identifier.rssinternalid30142
dc.identifier.rssurihttp://dx.doi.org/10.1074/jbc.M409375200


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