Biochemical and biophysical characterization of a novel plant protein disulfide isomerase

Gruber, C. W., Cemazar, M, Mechler, A, Martin, L. L. and Craik, D. J. (2009) Biochemical and biophysical characterization of a novel plant protein disulfide isomerase. Biopolymers: Peptide Science, 92 1: 35-43. doi:10.1002/bip.21113


Author Gruber, C. W.
Cemazar, M
Mechler, A
Martin, L. L.
Craik, D. J.
Title Biochemical and biophysical characterization of a novel plant protein disulfide isomerase
Journal name Biopolymers: Peptide Science   Check publisher's open access policy
ISSN 0006-3525
Publication date 2009-01
Year available 2008
Sub-type Article (original research)
DOI 10.1002/bip.21113
Volume 92
Issue 1
Start page 35
End page 43
Total pages 9
Editor Murray Goodwyn
Place of publication Hokoben NJ, USA
Publisher John Wiley & Sons
Collection year 2010
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
0607 Plant Biology
060799 Plant Biology not elsewhere classified
Abstract We recently isolated a protein disulfide isomerase (PDI) from the Rubiaceae (coffee family) plant Oldenlandia affinis (OaPDI) and demonstrated that it facilitates the production of disulfide-knotted defense proteins called cyclotides. PDIs are major folding catalysts in the eukaryotic ER where they are responsible for formation, breakage, or shuffling of disulfide bonds in substrate polypeptides and are important chaperones in the secretory pathway. Here, we report the first detailed analysis of the oligomerization behavior of a plant PDI, based on characterization of OaPDI using various biochemical and biophysical techniques, including size-exclusion chromatography, NMR spectroscopy, surface plasmon resonance and atomic force microscopy. In solution at low concentration OaPDI comprises mainly monomers, but fractions of dimers and/or higher-order oligomers were observed at increased conditions, raising the possibility that dimerization and/or oligomerization could be a mechanism to adapt to the various-sized polypeptide substrates of PDI. Unlike mammalian PDIs, oligomerization of the plant PDI is not driven by the formation of intermolecular disulfide bonds, but by noncovalent interactions. The information derived in this study advances our understanding of the oligomerization behavior of OaPDI in particular but is potentially of broader interest for understanding the mechanism and role of oligomerization, and hence the catalytic and physiological mechanism, of the ubiquitous folding catalyst PDI.
Keyword monomer
noncovalent dimerization
thioredoxin-fold
cyclotides
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Thu, 03 Sep 2009, 08:52:44 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience