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Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/214245
- Title
- Protein disulphide isomerases: diversity and roles in plants
- Author(s)
- Bhave, Mrinal; Wu, Huimei; Kamboj, Atul
- Abstract
- The 'foldase' enzyme protein disulphide isomerase (PDI) interacts with nascent polypeptides in the lumen of the endoplasmic reticulum to catalyze the formation of new disulphide bonds, as well as breakage and alternative isomerization of incorrectly formed bonds, during protein folding and maturation processes in eukaryotic cells. PDI belongs to the thioredoxin (TRX) superfamily that catalyzes cellular redox reactions and has an active site with the conserved motif WCXXC. PDI is a member of the larger PDI-like (PDIL) protein family, its subclasses varying in numbers, positions and sequences of functional domains and active sites and in subcellular locations and functions, many including PDI also playing chaperone roles. The human PDIL family has been studied in great detail, its members exhibiting activities ranging from the archetypical disulphide formation/isomerisation to a multitude of chaperone roles of relevance to cell biology and medicine, for example, in neurodegenerative diseases, apoptosis and cancer. The plant PDIL families are larger and more diverse and have been associated with some unique roles such as storage protein folding; however, information on plant PDILs is much more limited. This work overviews the key properties and functions of human PDILs, summarises the diversity and known functions of plant PDILs, and contemplates the directions for future research on PDILs, particularly in plants.
- Publication type
- Book chapter
- Research centre
- Swinburne University of Technology. Faculty of Life and Social Sciences. Environment and Biotechnology Centre
- Source
- Protein biochemistry, synthesis, structure, and cellular functions series: Protein folding / Eric C Walters (ed.), Chapter 1, pp. 1-40
- Publication year
- 2011
- FOR Code(s)
- 060104 Cell Metabolism; 060702 Plant Cell and Molecular Biology; 060705 Plant Physiology
- Keyword(s)
- Chaperone; PDI; Protein folding; Stress response
- Publisher
- Nova Science Publishers
- ISBN
- 9781617289903, 1617289906
- Copyright
- Copyright © 2011 Nova Science Publishers, Inc.
- Peer reviewed
