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Journal of Bacteriology, October 2001, p. 5896-5903, Vol. 183, No. 20
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.20.5896-5903.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

GerN, an Endospore Germination Protein of Bacillus cereus, Is an Na+/H+-K+ Antiporter

Thomas W. Southworth,1 Arthur A. Guffanti,2 Anne Moir,1 and Terry A. Krulwich2,*

Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom,1 and Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, New York 100292

Received 17 May 2001/Accepted 13 July 2001

GerN, a Bacillus cereus spore germination protein, exhibits homology to a widely distributed group of putative cation transporters or channel proteins. GerN complemented the Na+-sensitive phenotype of an Escherichia coli mutant that is deficient in Na+/H+ antiport activity (strain KNabc). GerN also reduced the concentration of K+ required to support growth of an E. coli mutant deficient in K+ uptake (strain TK2420). In a fluorescence-based assay of everted E. coli KNabc membrane vesicles, GerN exhibited robust Na+/H+ antiport activity, with a Km for Na+ estimated at 1.5 mM at pH 8.0 and 25 mM at pH 7.0. Li+, but not K+, served as a substrate. GerN-mediated Na+/H+ antiport was further demonstrated in everted vesicles as energy-dependent accumulation of 22Na+. GerN also used K+ as a coupling ion without completely replacing H+, as indicated by partial inhibition by K+ of H+ uptake into right-side-out vesicles loaded with Na+. K+ translocation as part of the antiport was supported by the stimulatory effect of intravesicular K+ on 22Na+ uptake by everted vesicles and the dependence of GerN-mediated 86Rb+ efflux on the presence of Na+ in trans. The inhibitory patterns of protonophore and thiocyanate were most consistent with an electrogenic Na+/H+-K+ antiport. GerN-mediated Na+/H+-K+ antiport was much more rapid than GerN-mediated Na+/H+ antiport.

* Corresponding author. Mailing address: Box 1020, Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, 1 Gustave L. Levy Pl., New York, NY 10029. Phone: (212) 241-7280. Fax: (212) 996-7214. E-mail: terry.krulwich{at}mssm.edu.

Journal of Bacteriology, October 2001, p. 5896-5903, Vol. 183, No. 20
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.20.5896-5903.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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