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Plant and Cell Physiology Advance Access originally published online on July 27, 2005
Plant and Cell Physiology 2005 46(10):1603-1612; doi:10.1093/pcp/pci176
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Targeting of proConA to the Plant Vacuole depends on its Nine Amino-acid C-terminal Propeptide

Saint-Jore-Dupas Claude1, Gilbert Marie-Agnès1, Ramis Catalina2, Paris Nadine1, Kiefer-Meyer Marie-Christine1, Neuhaus Jean-Marc3, Faye Loïc1 and Gomord Véronique1,*

1 CNRS UMR 6037, IFRMP 23, GDR 2590, Université de Rouen, UFR des Sciences, Bâtiment Extension Biologie, 76821 Mont-Saint-Aignan CEDEX, France
2 Université centrale du Vénézuéla, Institut de Génétique, Faculté d‘Agronomie, Maracay, Aragua, Vénézuéla
3 Laboratoire de biochimie, Université de Neuchâtel, rue Emile-Argand 9, CH-2007 Neuchâtel, Switzerland

* Corresponding author: E-mail, vgomord{at}crihan.fr; Fax, +33-2-35-14-67-87.

Concanavalin A (ConA) is a well characterized and extensively used lectin accumulated in the protein bodies of jack bean cotyledons. ConA is synthesized as an inactive precursor proConA. The maturation of inactive proConA into biologically active ConA is a complex process including the removal of an internal glycopeptide and a C-terminal propeptide (CTPP), followed by a head-to-tail ligation of the two largest polypeptides. The cDNA encoding proConA was cloned and expressed in tobacco BY-2 cells. ProConA was slowly transported to the vacuole where its maturation into ConA was similar to that in jack bean cotyledons, apart from an incomplete final ligation. To investigate the role of the nine amino acid CTPP, a truncated form lacking the propeptide (proConA{Delta}9) was expressed in BY-2 cells. In contrast to proConA, proConA{Delta}9 was rapidly chased out of the endoplasmic reticulum (ER) and secreted into the culture medium. The CTPP was then fused to the C-terminal end of a secreted form of green fluorescent protein (secGFP). When expressed in tobacco BY-2 cells and leaf protoplasts, the chimaeric protein was located in the vacuole whereas secGFP was located in the culture medium and in the vacuole. Altogether, our results show we have isolated a new C-terminal vacuolar sorting determinant.

The nucleotide sequence of the proConA cDNA reported in this paper has been submitted to GenBank under the accession No. AF308777 [GenBank] .

(Received June 15, 2005; Accepted July 20, 2005)
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