Journal
PLANT PHYSIOLOGY
Volume 130, Issue 2, Pages 1054-1062Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.008193
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- NIGMS NIH HHS [1R01 GM 57427] Funding Source: Medline
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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 CAM (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 CAM, 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 CAM activity. When fused to N-terminal truncated CAM, both the CAX3 and VCAX1 regulatory regions could only auto-inhibit CAM 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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