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• W70161866 abstract "Research Article1 November 1993free access The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. N.R. Salama N.R. Salama Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. Search for more papers by this author T. Yeung T. Yeung Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. Search for more papers by this author R.W. Schekman R.W. Schekman Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. Search for more papers by this author N.R. Salama N.R. Salama Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. Search for more papers by this author T. Yeung T. Yeung Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. Search for more papers by this author R.W. Schekman R.W. Schekman Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. Search for more papers by this author Author Information N.R. Salama1, T. Yeung1 and R.W. Schekman1 1Department of Molecular and Cell Biology, Howard Hughes Research Institute, University of California, Berkeley 94720. The EMBO Journal (1993)12:4073-4082https://doi.org/10.1002/j.1460-2075.1993.tb06091.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info SEC13 encodes a 33 kDa protein that participates in vesicle budding from the endoplasmic reticulum (ER). In order to purify a functional form of Sec13p, a SEC13-dihydrofolate reductase (mouse) fusion gene (SEC13:DHFR) was constructed that complements both sec13 temperature sensitive and null mutations. Methotrexate-agarose affinity chromatography facilitated the purification of two forms of the Sec13-dhfrp fusion protein: a monomeric form and a high molecular weight complex. The complex form consists of two subunits: Sec13-dhfrp and a 150 kDa protein (p150). Native immunoprecipitation experiments confirm that Sec13p exists in a complex with p150 in wild type cells. Functional analysis supports a role for both subunits in protein transport. Vesicle budding from the ER in a cell-free reaction is inhibited by Fab antibody fragments directed against either Sec13p or p150. The purified Sec13-dhfrp/p150 complex, but not the Sec13-dhfrp monomer, in combination with two other pure protein fractions (Sar1p and a Sec23/Sec24 protein complex) satisfies the requirement for cytosol in a cell-free vesicle budding reaction. The vesicles formed with the purified protein fractions are competent to fuse with the Golgi and are biochemically distinct from the ER membrane fraction from which they derive. Previous ArticleNext Article Volume 12Issue 111 November 1993In this issue RelatedDetailsLoading ..." @default.
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• W70161866 title "The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins." @default.
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