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Published on March 31, 2006; 10.1104/pp.106.076786

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Received January 7, 2006
Returned for revision February 9, 2006
Accepted March 22, 2006

Functional characterization of ice plant SKD1, an AAA-type ATPase associated with ER-Golgi network, and its role in adaptation to salt stress

Yingtzy Jou , Chih-Pin Chiang , Guang-Yuh Jauh , and Hungchen Emilie Yen *

Department of Life Sciences, National Chung Hsing University, Taichung, Taiwan 40227
Institute of Plant and Microbial Biology, Academia Sinica, Nankang, Taipei, Taiwan 11529

* Corresponding author; email: heyen{at}dragon.nchu.edu.tw.

A salt-induced gene mcSKD1 (suppressor of K+ transport growth defect) able to facilitate K+ uptake has previously been identified from the halophyte ice plant (Mesembryanthemum crystallinum L.). The sequence of mcSKD1 is homologous to VPS4 (vacuolar protein sorting), an AAA (ATPase associated with a variety of cellular activities)-type ATPase that participates in the sorting of vacuolar proteins into multivesicular bodies in yeast. Recombinant mcSKD1 exhibited ATP hydrolytic activities in vitro with a half-maximal rate at an ATP concentration of 1.25 mM. Point mutations on active site residues abolished its ATPase activity. ADP is both a product and a strong inhibitor of the reaction. ADP-binding form of mcSDK1 greatly reduced its catalytic activity. The mcSKD1 protein accumulated ubiquitously in both vegetative and reproductive parts of plants. Highest accumulation was observed in cells actively engaging in the secretory processes, such as bladder cells of leaf epidermis. Membrane fractionation and double labeling immunofluorescence showed the predominate localization of mcSKD1 in the ER-Golgi network. Immunoelectron microscopy identified the formation of mcSKD1 proteins into small aggregates in the cytosol and associated with membrane continuum within the endomembrane compartments. These results indicated that this ATPase participates in the ER-Golgi mediated protein sorting machinery for both housekeeping function and compartmentalization of excess Na+ under high salinity.




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