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Plant and Cell Physiology Advance Access published online on July 27, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci176
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received June 15, 2005
Accepted July 20, 2005

Regular Paper

Targeting of proConA to the Plant Vacuole Depends on Its Nine Amino-Acid C-Terminal Propeptide

Saint-Jore-Dupas Claude 1, Gilbert Marie-Agnès 1, Ramis Catalina 2, Paris Nadine 1, Kiefer-Meyer Marie-Christine 1, Neuhaus Jean-Marc 3, Faye Loïc 1, and Gomord Véronique 1*

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

* To whom correspondence should be addressed.
Gomord Véronique, E-mail: vgomord{at}crihan.fr


  Abstract

Concanavalin A (ConA) is a well characterized and extensively used lectin accumulated in jack bean cotyledon's protein bodies. 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), and 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 as in jack bean cotyledons, excepted an incomplete final ligation. To investigate the role of the nine amino acids 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 ER and secreted in 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.

Keywords: BY-2 cells; Concanavalin A; GFP; targeting; vacuole; vacuolar sorting determinant.
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