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J Biol Chem, Vol. 274, Issue 52, 36973-36979, December 24, 1999
From the Department of Pharmacology, Case Western Reserve
University, Cleveland, Ohio 44106-4965
Salmonella typhimurium CorA is the
archetypal member of the largest family of Mg2+
transporters of the Bacteria and Archaea. It contains three
transmembrane segments. There are no conserved charged residues within
these segments indicating electrostatic interactions are not used in Mg2+ transport through CorA. Previous mutagenesis studies
of CorA revealed a single face of the third transmembrane segment that is important for Mg2+ transport. In this study, we mutated
hydroxyl-bearing and other conserved residues in the second
transmembrane segment to identify residues involved in transport.
Residues Ser260, Thr270, and Ser274
appear to be important for transport and are oriented such that they
would also line a face of an
The CorA Mg2+ Transport Protein of Salmonella
typhimurium
MUTAGENESIS OF CONSERVED RESIDUES IN THE SECOND MEMBRANE
DOMAIN*
and
-helix. In addition, the sequence 276YGMNF280, found in virtually all CorA
homologues, is critical for CorA function because even conservative
mutations are not tolerated at these residues. Finally, mutations of
residues in the second transmembrane segment, unlike those in the third
transmembrane segment, revealed cooperative behavior for the influx of
Mg2+. We conclude that the second transmembrane segment
forms a major part of the Mg2+ pore with the third
transmembrane segment of CorA.
*
This work was supported by National Institutes of Health
Grant GM39447 (to M. E. M.) and the Cell and Molecular Biology
Training Grant GM08056 (to M. A. S.).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.
To whom correspondence should be addressed: Dept. of Pharmacology,
School of Medicine, Case Western Reserve University, 10900 Euclid Ave.,
Cleveland, OH 44106-4965. Tel.: (216) 368-6187; Fax: (216) 368-3395;
E-mail: mxs100@po.cwru.edu.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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