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Plant Physiol, November 2001, Vol. 127, pp. 1020-1029

Regulation of CAX1, an Arabidopsis Ca2+/H+ Antiporter. Identification of an N-Terminal Autoinhibitory Domain1

Jon K. Pittman and Kendal D. Hirschi*

Plant Physiology Group, U.S. Department of Agriculture/Agricultural Research Service Children's Nutrition Research Center, Baylor College of Medicine, 1100 Bates Street, Houston, Texas 77030 (J.K.P., K.D.H.); and Vegetable and Fruit Improvement Center, Texas A&M University, College Station, Texas 77845 (K.D.H.)

Regulation of Ca2+ transport determines the duration of a Ca2+ signal, and hence, the nature of the biological response. Ca2+/H+ antiporters such as CAX1 (cation exchanger 1), play a key role in determining cytosolic Ca2+ levels. Analysis of a full-length CAX1 clone suggested that the CAX1 open reading frame contains an additional 36 amino acids at the N terminus that were not found in the original clone identified by suppression of yeast (Saccharomyces cerevisiae) vacuolar Ca2+ transport mutants. The long CAX1 (lCAX1) could not suppress the yeast Ca2+ transport defects despite localization to the yeast vacuole. Calmodulin could not stimulate lCAX1 Ca2+/H+ transport in yeast; however, minor alterations in the 36-amino acid region restored Ca2+/H+ transport. Sequence analysis suggests that a 36-amino acid N-terminal regulatory domain may be present in all Arabidopsis CAX-like genes. Together, these results suggest a structural feature involved in regulation of Ca2+/H+ antiport.


1 This work was supported by the U.S. Department of Agriculture/Agricultural Research Service (under Cooperative Agreement No. 58-6250-6001) and by the National Institutes of Health (grant nos. CHRC 5 P30 and 1R01 GM57427).

* Corresponding author; e-mail kendalh{at}bcm.tmc.edu; fax 713-798-7078.

© 2001 American Society of Plant Physiologists



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