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Plant Physiol, January 2001, Vol. 125, pp. 437-446
Na+/H+ Antiporter from
Synechocystis Species PCC 6803, Homologous to SOS1,
Contains an Aspartic Residue and Long C-Terminal Tail Important for the
Carrier Activity
Akira
Hamada,
Takashi
Hibino,
Tatsunosuke
Nakamura, and
Teruhiro
Takabe*
Research Institute of Meijo University, Tenpaku-ku, Nagoya, Aichi
468-8502, Japan (A.H., T.T.); Department of Chemistry, Faculty of
Science and Technology, Meijo University, Tenpaku-ku, Nagoya, Aichi
468-8502, Japan (T.H., T.T.); and Laboratory of Membrane Biochemistry,
Faculty of Pharmaceutical Science, Chiba University, Inage-ku, Chiba
263-8522, Japan (T.N.)
A putative Na+/H+ antiporter gene whose
deduced amino acid sequence was highly homologous to the NhaP
antiporter from Pseudomonas aeruginosa and SOS1
antiporter from Arabidopsis was isolated from Synechocystis sp. PCC 6803. The
Synechocystis NhaP antiporter (SynNhaP) was expressed in
Escherichia coli mutant cells, which were deficient in
Na+/H+ antiporters. It was found that the
SynNhaP complemented the salt-sensitive phenotype of the E.
coli mutant. Membrane vesicles prepared from the E.
coli mutant transformed with the SynNhaP exhibited the Na+/H+ and Li+/H+
antiporter activities, and their activities were insensitive to
amiloride. Moreover, its activity was very high between pH 5 and 9. The
replacement of aspartate-138 in SynNhaP with glutamate or
tyrosine inactivated the SynNhaP antiporter activity. The deletion of a
part of the long C-terminal hydrophilic tail significantly inhibited
the antiporter activity. A topological model suggests that
aspartate-138 in SynNhaP is conserved in NhaP, SOS1, and AtNHX1 and is
involved in the exchange activity. Thus, it appeared that the SynNhaP
would provide a model system for the study of structural and functional
properties of eucaryotic Na+/H+ antiporters.
*
Corresponding author; e-mail takabe{at}meijo-u.ac.jp; fax
81-52-832-1545.
© 2001 American Society of Plant Physiologists
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