Plant Physiology Preview
Published on September 20, 2002; 10.1104/pp.008193
Received May 7, 2002
Returned for revision June 12, 2002
Accepted June 29, 2002
Distinct N-Terminal Regulatory Domains of Ca2+/H+ Antiporters
Jon K. Pittman , Coimbatore S. Sreevidya , Toshiro Shigaki , Hanayo Ueoka-Nakanishi , and Kendal D. Hirschi *
United States Department of Agriculture-Agricultural Research Service Children's Nutrition Research Center, Baylor College of Medicine, 1100 Bates Street, Houston, Texas 77030 (J.K.P., C.S.S., T.S., K.D.H.); Bio-Resources Division, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226-8503, Japan (H.U.-N.); and Vegetable and Fruit Improvement Center, Texas A&M University, College Station, Texas 77845 (K.D.H.)
* Corresponding author; email: kendalh{at}bcm.tmc.edu.
The regulation of intracellular Ca2+ levels is achieved in part by high-capacity vacuolar Ca2+/H+ antiporters. An N-terminal regulatory region (NRR) on the Arabidopsis Ca2+/H+ antiporter CAX1 (cation exchanger 1) has been shown previously to regulate Ca2+ transport by a mechanism of N-terminal auto-inhibition. Here, we examine the regulation of other CAX transporters, both within Arabidopsis and from another plant, mung bean (Vigna radiata), to ascertain if this mechanism is commonly used among Ca2+/H+ antiporters. Biochemical analysis of mung bean VCAX1 expressed in yeast (Saccharomyces cerevisiae) showed that N-terminal truncated VCAX1 had approximately 70% greater antiport activity compared with full-length VCAX1. A synthetic peptide corresponding to the NRR of CAX1, which can strongly inhibit Ca2+ transport by CAX1, could not dramatically inhibit Ca2+ transport by truncated VCAX1. The N terminus of Arabidopsis CAX3 was also shown to contain an NRR. Additions of either the CAX3 or VCAX1 regulatory regions to the N terminus of an N-terminal truncated CAX1 failed to inhibit CAX1 activity. When fused to N-terminal truncated CAX1, both the CAX3 and VCAX1 regulatory regions could only auto-inhibit CAX1 after mutagenesis of specific amino acids within this NRR region. These findings demonstrate that N-terminal regulation is present in other plant CAX transporters, and suggest distinct regulatory features among these transporters.
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