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• W1841496789 abstract "Research Article1 April 1993free access Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit. D.C. John D.C. John Department of Biochemistry and Molecular Biology, University of Manchester, UK. Search for more papers by this author M.E. Grant M.E. Grant Department of Biochemistry and Molecular Biology, University of Manchester, UK. Search for more papers by this author N.J. Bulleid N.J. Bulleid Department of Biochemistry and Molecular Biology, University of Manchester, UK. Search for more papers by this author D.C. John D.C. John Department of Biochemistry and Molecular Biology, University of Manchester, UK. Search for more papers by this author M.E. Grant M.E. Grant Department of Biochemistry and Molecular Biology, University of Manchester, UK. Search for more papers by this author N.J. Bulleid N.J. Bulleid Department of Biochemistry and Molecular Biology, University of Manchester, UK. Search for more papers by this author Author Information D.C. John1, M.E. Grant1 and N.J. Bulleid1 1Department of Biochemistry and Molecular Biology, University of Manchester, UK. The EMBO Journal (1993)12:1587-1595https://doi.org/10.1002/j.1460-2075.1993.tb05803.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Prolyl 4-hydroxylase (P4-H) catalyses a vital post-translational modification in the biosynthesis of collagen. The enzyme consists of two distinct polypeptides forming an alpha 2 beta 2 tetramer (alpha = 64 kDa, beta = 60 kDa), the beta-subunit being identical to the multifunctional enzyme protein disulfide isomerase (PDI). By studying the cell-free synthesis of the rat alpha-subunit of P4-H we have shown that the alpha-subunit can be translocated, glycosylated and the signal peptide cleaved by dog pancreatic microsomal membranes to yield both singly and doubly glycosylated forms. When translations were carried out under conditions which prevent disulfide bond formation, the product synthesized formed aggregates which were associated with the immunoglobulin heavy chain binding protein (BiP). Translations carried out under conditions that promote disulfide bond formation yielded a product that was not associated with BiP but formed a complex with the endogenous beta-subunit (PDI). Complex formation was detected by co-precipitation of the newly synthesized alpha-subunit with antibodies raised against PDI, by sucrose gradient centrifugation and by chemical cross-linking. When microsomal vesicles were depleted of PDI, BiP and other soluble endoplasmic reticulum proteins, no complex formation was observed and the alpha-subunit aggregated even under conditions that promote disulfide bond formation. We have therefore demonstrated that the enzyme P4-H can be assembled at synthesis in a cell-free system and that the solubility of the alpha-subunit is dependent upon its association with PDI. Previous ArticleNext Article Volume 12Issue 41 April 1993In this issue RelatedDetailsLoading ..." @default.
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• W1841496789 title "Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit." @default.
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