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Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen

Citation

Wilson, RR and Lees, J and Buleid, NJ, Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen, Journal of Biological Chemistry, 273, (16) pp. 9637-9643. ISSN 0021-9258 (1998) [Refereed Article]

DOI: doi:10.1074/jbc.273.16.9637

Abstract

Protein-disulfide isomerase (PDI) has been shown to be a multifunctional enzyme catalyzing the formation of disulfide bonds, as well as being a component of the enzymes prolyl 4-hydroxylase (P4-H) and microsomal triglyceride transfer protein. It has also been proposed to function as a molecular chaperone during the refolding of denatured proteins in vitro. To investigate the role of this multifunctional protein within a cellular context, we have established a semi-permeabilized cell system that reconstitutes the synthesis, folding, modification, and assembly of procollagen as they would occur in the cell. We demonstrate here that P4-H associates transiently with the triple helical domain during the assembly of procollagen. The release of P4-H from the triple helical domain coincides with assembly into a thermally stable triple helix. However, if triple helix formation is prevented, P4-H remains associated, suggesting a role for this enzyme in preventing aggregation of this domain. We also show that PDI associates independently with the C-propeptide of monomeric procollagen chains prior to trimer formation, indicating a role for this protein in coordinating the assembly of heterotrimeric molecules. This demonstrates that PDI has multiple functions in the folding of the same protein, that is, as a catalyst for disulfide bond formation, as a subunit of P4-H during proline hydroxylation, and independently as a molecular chaperone during chain assembly.

Item Details

Item Type:Refereed Article
Research Division:Biological Sciences
Research Group:Biochemistry and Cell Biology
Research Field:Protein Trafficking
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Medical and Health Sciences
Author:Wilson, RR (Dr Richard Wilson)
ID Code:72432
Year Published:1998
Web of Science® Times Cited:104
Deposited By:Central Science Laboratory
Deposited On:2011-08-26
Last Modified:2011-08-26
Downloads:0

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