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A bioinformatic approach to the identification of a conserved domain in a sugarcane legumain that directs GFP to the lytic vacuole

Jackson, M. A., Rae, A. L., Casu, R. E., Grof, C. P. L., Bonnett, G. D. and Maclean, D. J. (2007) A bioinformatic approach to the identification of a conserved domain in a sugarcane legumain that directs GFP to the lytic vacuole. Functional Plant Biology, 34 : 633-644.


Author(s) Jackson, M. A.
Rae, A. L.
Casu, R. E.
Grof, C. P. L.
Bonnett, G. D.
Maclean, D. J.
Title A bioinformatic approach to the identification of a conserved domain in a sugarcane legumain that directs GFP to the lytic vacuole
Journal name Functional Plant Biology
Publication date 2007
Year available 2007
Volume number 34
ISSN 1445-4408
Start page 633
End page 644
Total pages 12
Editor(s) Henry, J.
Place of publication Australia
Publisher CSIRO Publishing
Collection year 2008
Subject C1
270402 Plant Physiology
780105 Biological sciences
Abstract Sugarcane is an ideal candidate as a biofactory for the production of alternate higher value products. One way of achieving this is to direct useful proteins into the vacuoles within the sugarcane storage parenchyma tissue. By bioinformatic analysis of gene sequences from putative sugarcane vacuolar proteins a motif has been identified that displays high conservation across plant legumain homologues that are known to function within vacuolar compartments. This. ve amino acid motif, represented by the sequence IRLPS in sugarcane is shown to direct an otherwise secreted GFP fusion protein into a large acidic and proteolytic vacuole in sugarcane callus cells as well as in diverse plant species. In mature sugarcane transgenic plants, the stability of GFP appeared to be dependent on cell type, suggesting that the vacuolar environment can be hostile to introduced proteins. This targeting motif will be a valuable tool for engineering plants such as sugarcane for production of novel products.
Keyword(s) Plant Sciences
biofactory
vacuole processing enzyme
Saccharum
vacuole targeting
Arabidopsis-thaliana
Plant-cells
Aspartic Proteinase
Fusion Proteins
Propeptide
 
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http://ezproxy.library.uq.edu.au/login?url=http://dx.doi.org/10.1071/FP07024   Article DOI - full text from publisher, Journal web site  
 
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