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Arabidopsis Sec21p and Sec23p Homologs. Probable Coat Proteins of Plant COP-Coated Vesicles1

Ali Movafeghi, Nicole Happel, Peter Pimpl, Gui-Hua Tai, and David G. Robinson*

Abteilung Strukturelle Zellphysiologie, Albrecht-von-Haller Institut für Pflanzenwissenschaften, Universität Göttingen, Untere Karspüle 2, D-37073 Göttingen, Germany

Intracellular protein transport between the endoplasmic reticulum (ER) and the Golgi apparatus and within the Golgi apparatus is facilitated by COP (coat protein)-coated vesicles. Their existence in plant cells has not yet been demonstrated, although the GTP-binding proteins required for coat formation have been identified. We have generated antisera against glutathione-S-transferase-fusion proteins prepared with cDNAs encoding the Arabidopsis Sec21p and Sec23p homologs (AtSec21p and AtSec23p, respectively). The former is a constituent of the COPI vesicle coatomer, and the latter is part of the Sec23/24p dimeric complex of the COPII vesicle coat. Cauliflower (Brassica oleracea) inflorescence homogenates were probed with these antibodies and demonstrated the presence of AtSec21p and AtSec23p antigens in both the cytosol and membrane fractions of the cell. The membrane-associated forms of both antigens can be solubilized by treatments typical for extrinsic proteins. The amounts of the cytosolic antigens relative to the membrane-bound forms increase after cold treatment, and the two antigens belong to different protein complexes with molecular sizes comparable to the corresponding nonplant coat proteins. Sucrose-density-gradient centrifugation of microsomal cell membranes from cauliflower suggests that, although AtSec23p seems to be preferentially associated with ER membranes, AtSec21p appears to be bound to both the ER and the Golgi membranes. This could be in agreement with the notion that COPII vesicles are formed at the ER, whereas COPI vesicles can be made by both Golgi and ER membranes. Both AtSec21p and AtSec23p antigens were detected on membranes equilibrating at sucrose densities equivalent to those typical for in vitro-induced COP vesicles from animal and yeast systems. Therefore, a further purification of the putative plant COP vesicles was undertaken.

1   A.M. was the recipient of a scholarship from the Ministry of Culture and Education of the Government of Iran. G.-H.T. was a Research Fellow of the Alexander-von-Humboldt Stiftung (Bonn, Germany). This work was also supported by funds from the Deutsche Forschungsgemeinschaft (grant no. SFB 523).
*   Corresponding author; e-mail drobins{at}uni-goettingen.de; fax 49-551-397833.

Plant Physiol. (1999) 119: 1437-1446
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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