Biochemical and biophysical characterization of a novel plant protein disulfide isomerase
| Autor: | Masa Cemazar, Adam Mechler, Christian W. Gruber, Lisandra L. Martin, David J. Craik |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular inorganic chemicals Magnetic Resonance Spectroscopy Oldenlandia Protein Disulfide-Isomerases Biophysics Microscopy Atomic Force Thioredoxin fold Biochemistry Biophysical Phenomena Biomaterials Cyclotides Non-covalent interactions Amino Acid Sequence Protein disulfide-isomerase Peptide sequence chemistry.chemical_classification biology Chemistry Organic Chemistry General Medicine Surface Plasmon Resonance biology.organism_classification Protein Structure Tertiary Molecular Weight Folding (chemistry) Plant protein Chromatography Gel Protein Multimerization |
| Zdroj: | Biopolymers. 92:35-43 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.21113 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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