First published online September 20, 2002; 10.1104/pp.008193
Plant Physiol, October 2002, Vol. 130, pp. 1054-1062
Distinct N-Terminal Regulatory Domains of
Ca2+/H+ Antiporters1
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.)
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.
1
This work was supported by the U.S. Department
of Agriculture-Agricultural Research Service (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.
© 2002 American Society of Plant Physiologists
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