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J. Biol. Chem., Vol. 278, Issue 8, 6610-6617, February 21, 2003
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From the In plants and fungi, vacuolar transporters help
remove potentially toxic cations from the cytosol.
Metal/H+ antiporters are involved in metal
sequestration into the vacuole. However, the specific transport
properties and the ability to manipulate these transporters to alter
substrate specificity are poorly understood. The Arabidopsis
thaliana cation exchangers, CAX1 and
CAX2, can both transport Ca2+ into the vacuole. There are
11 CAX-like transporters in Arabidopsis; however, CAX2 was
the only characterized CAX transporter capable of vacuolar
Mn2+ transport when expressed in yeast. To determine the
domains within CAX2 that mediate Mn2+ specificity, six CAX2
mutants were constructed that contained different regions of the CAX1
transporter. One class displayed no alterations in Mn2+ or
Ca2+ transport, the second class showed a reduction in
Ca2+ transport and no measurable Mn2+
transport, and the third mutant, which contained a 10-amino acid domain
from CAX1 (CAX2-C), showed no reduction in Ca2+ transport
and a complete loss of Mn2+ transport. The subdomain
analysis of CAX2-C identified a 3-amino acid region that is responsible
for Mn2+ specificity of CAX2. This study provides
evidence for the feasibility of altering substrate specificity in a
metal/H+ antiporter, an important family of transporters
found in a variety of organisms.
Manganese Specificity Determinants in the Arabidopsis
Metal/H+ Antiporter CAX2*
§,§, and¶
**
United States Department of
Agriculture/Agricultural Research Service Children's Nutrition
Research Center, Baylor College of Medicine, Houston, Texas 77030, the
¶ Department of Human and Molecular Genetics, Baylor College
of Medicine, Houston, Texas 77030, and Vegetable and Fruit
Improvement Center, Texas A&M University, College Station, Texas
77845
*
This work was supported by the United States Department of
Agriculture/Agricultural Research Service under Cooperative Agreement 58-6250-6001 and by National Institutes of Health Grants CHRC 5 P30
and 1R01 GM57427.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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