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Plant Physiology 132:1892-1900 (2003)
© 2003 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

C-Terminal KDEL Sequence of A KDEL-Tailed Cysteine Proteinase (Sulfhydryl-Endopeptidase) Is Involved in Formation of KDEL Vesicle and in Efficient Vacuolar Transport of Sulfhydryl-Endopeptidase1

Takashi Okamoto2,*, Tomoo Shimada, Ikuko Hara-Nishimura, Mikio Nishimura and Takao Minamikawa

Department of Biological Sciences, Tokyo Metropolitan University, Hachioji, Tokyo, 192–0397 Japan (T.O., T.M.); Department of Botany, Graduate School of Science, Kyoto University, Kyoto, 606–8502 Japan (T.S., I.H.-R.); and Department of Cell Biology, National Institute of Basic Biology, Okazaki, 444–8585 Japan (M.N.)

Sulfhydryl-endopeptidase (SH-EP) is a papain-type vacuolar proteinase expressed in cotyledons of germinated Vigna mungo seeds, and the enzyme possesses a C-terminal propeptide containing KDEL tail, an endoplasmic reticulum retention signal for soluble proteins. SH-EP is transported to vacuoles via a KDEL vesicle (KV) through a Golgi complex-independent route. To see the function of the KDEL sequence of SH-EP, wild-type SH-EP and its KDEL deletion mutant (SH-EP{Delta}KDEL) were heterologously expressed in Arabidopsis and in cultured tobacco Bright Yellow 2 cells, and their intracellular transport pathways and localizations were analyzed. A combination of the results from analyses for transformed Arabidopsis and tobacco (Nicotiana tabacum) cells indicated that wild-type SH-EP is packed into KV-like vesicles through the KDEL sequence and is transported to vacuoles in the cells of transformants. In contrast, KV was not formed/induced in the cells expressing SH-EP{Delta}KDEL, and the mutant protein was mainly secreted. Therefore, the C-terminal KDEL sequence of the KDEL-tailed cysteine proteinase is thought to be involved in the formation of KV, and in the efficient vacuolar transport of the proteins through KV.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.021147.

1 This work was supported in part by the Ministry of Education, Science and Culture of Japan (Grant-in-Aid for Scientific Research no. 12740441) and by the Japan Science Society (Sasakawa Scientific Research grant no. 12–246).

2 Present address: Universität Hamburg, Institut für Allgemeine Botanik, AMP 2, Ohnhorststrasse 18, 22609 Hamburg, Germany.

* Corresponding author; e-mail okamoto-takashi{at}c.metro-u.ac.jp; fax 49–40–428–16–229.

Received January 28, 2003; returned for revision February 26, 2003; accepted April 29, 2003.




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