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Plant and Cell Physiology Advance Access originally published online on June 13, 2007
Plant and Cell Physiology 2007 48(7):1010-1021; doi:10.1093/pcp/pcm071
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Localization and Topogenesis Studies of Cytoplasmic and Vacuolar Homologs of the Galanthus nivalis Agglutinin

Elke Fouquaert1, Sally L. Hanton2,4, Federica Brandizzi2,3, Willy J. Peumans1 and Els J. M. Van Damme1,*

1Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure Links 653, B-9000 Gent, Belgium
2Department of Biology, 112 Science Place, University of Saskatchewan, Saskatoon SK S7N 5E2 Canada
3US Department of Energy Plant Research Laboratory, Michigan State University, Plant Biology Building, East Lansing, MI 48824, USA

*Corresponding author: E-mail, ElsJM.VanDamme{at}UGent.be; Fax, +32-92646219.


  Abstract

The Galanthus nivalis agglutinin (GNA) is synthesized as a preproprotein. To corroborate the role of the different targeting peptides in the topogenesis of GNA and related proteins, different constructs were made whereby both the complete original GNA gene and different truncated sequences were coupled to the enhanced green fluorescent protein (EGFP). In addition, a GNA ortholog from rice that lacks the signal peptide and C-terminal propeptide sequence was fused to EGFP. These fusion constructs were expressed in tobacco BY-2 cells and their localization analyzed by confocal fluorescence microscopy. We observed that the processed preproprotein of GNA was directed towards the vacuolar compartment, whereas both the truncated forms of GNA corresponding to the mature lectin polypeptide and the rice ortholog of GNA were located in the nucleus and the cytoplasm. It can be concluded, therefore, that removal of the C-terminal propeptide and the signal peptide is sufficient to change the subcellular targeting of a normally vacuolar protein to the nuclear/cytoplasmic compartment of the BY-2 cells. These findings support the proposed hypothesis that cytoplasmic/nuclear GNA-like proteins and their vacuolar homologs are evolutionarily related and that the classical GNA-related lectins might have evolved from cytoplasmic orthologs through an evolutionary event involving the insertion of a signal peptide and a C-terminal propeptide.

Keywords: Cytoplasmic ortholog - Galanthus nivalis agglutinin - Lectin - Subcellular location

Abbreviations: CTP, C-terminal propeptide; EGFP, enhanced GFP; ER, endoplasmic reticulum; EYFP, enhanced yellow fluorescent protein; GFP, green fluorescent protein; GNA, Galanthus nivalis agglutinin; PVC, prevacuolar compartments; SP, signal peptide; UTR, untranslated region.

4Present address: Institute for Cell and Molecular Biology Medical School, University of Newcastle upon Tyne, Catherine Cookson Building, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.

(Received May 5, 2007; Accepted June 3, 2007)
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