Induction of protein body formation in plant leaves by elastin-like polypeptide fusions
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BioMed Central
Open Access
Research article
Induction of protein body formation in plant leaves by elastin-like polypeptide fusions Andrew J Conley1,2, Jussi J Joensuu2,3, Rima Menassa*2 and Jim E Brandle2,4 Address: 1Department of Biology, University of Western Ontario, London, ON, Canada, 2Southern Crop Protection and Food Research Centre, Agriculture and Agri- Food Canada, London, ON, Canada , 3VTT Technical Research Centre of Finland, Espoo, Finland and 4Vineland Research and Innovation Centre, Vineland Station, ON, Canada Email: Andrew J Conley - [email protected]; Jussi J Joensuu - [email protected]; Rima Menassa* - [email protected]; Jim E Brandle - [email protected] * Corresponding author
Published: 7 August 2009 BMC Biology 2009, 7:48
doi:10.1186/1741-7007-7-48
Received: 20 April 2009 Accepted: 7 August 2009
This article is available from: http://www.biomedcentral.com/1741-7007/7/48 © 2009 Conley et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract Background: Elastin-like polypeptides are synthetic biopolymers composed of a repeating pentapeptide 'VPGXG' sequence that are valuable for the simple non-chromatographic purification of recombinant proteins. In addition, elastin-like polypeptide fusions have been shown to enhance the accumulation of a range of different recombinant proteins in plants, thus addressing the major limitation of plant-based expression systems, which is a low production yield. This study's main objectives were to determine the general utility of elastin-like polypeptide protein fusions in various intracellular compartments and to elucidate elastin-like polypeptide's mechanism of action for increasing recombinant protein accumulation in the endoplasmic reticulum of plants. Results: The effect of elastin-like polypeptide fusions on the accumulation of green fluorescent protein targeted to the cytoplasm, chloroplasts, apoplast, and endoplasmic reticulum was evaluated. The endoplasmic reticulum was the only intracellular compartment in which an elastin-like polypeptide tag was shown to significantly enhance recombinant protein accumulation. Interestingly, endoplasmic reticulumtargeted elastin-like polypeptide fusions induced the formation of a novel type of protein body, which may be responsible for elastin-like polypeptide's positive effect on recombinant protein accumulation by excluding the heterologous protein from normal physiological turnover. Although expressed in the leaves of plants, these novel protein bodies appeared similar in size and morphology to the prolamin-based protein bodies naturally found in plant seeds. The elastin-like polypeptide-induced protein bodies were highly mobile organelles, exhibiting various dynamic patterns of movement throughout the cells, which were dependent on i
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