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J. Biol. Chem., Vol. 279, Issue 10, 9532-9538, March 5, 2004

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A Superfamily of Voltage-gated Sodium Channels in Bacteria^*

Ryuta Koishi, Haoxing Xu, Dejian Ren, Betsy Navarro, Benjamin W. Spiller¶, Qing Shi, and David E. Clapham||

From the Howard Hughes Medical Institute, Department of Cardiovascular Research, Children's Hospital, and Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115 and ^¶Children's Hospital, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115

NaChBac, a six--helical transmembrane-spanning protein cloned from Bacillus halodurans, is the first functionally characterized bacterial voltage-gated Na⁺-selective channel (Ren, D., Navarro, B., Xu, H., Yue, L., Shi, Q., and Clapham, D. E. (2001) Science 294, 2372-2375). As a highly expressing ion channel protein, NaChBac is an ideal candidate for high resolution structural determination and structure-function studies. The biological role of NaChBac, however, is still unknown. In this report, another 11 structurally related bacterial proteins are described. Two of these functionally expressed as voltage-dependent Na⁺ channels (Na_VPZ from Paracoccus zeaxanthinifaciens and Na_VSP from Silicibacter pomeroyi). Na_VPZ and Na_VSP share 40% amino acid sequence identity with NaChBac. When expressed in mammalian cell lines, both Na_VPZ and Na_VSP were Na⁺-selective and voltage-dependent. However, their kinetics and voltage dependence differ significantly. These single six--helical transmembrane-spanning subunits constitute a widely distributed superfamily (Na_VBac) of channels in bacteria, implying a fundamental prokaryotic function. The degree of sequence homology (22-54%) is optimal for future comparisons of Na_VBac structure and function of similarity and dissimilarity among Na_VBac proteins. Thus, the Na_VBac superfamily is fertile ground for crystallographic, electrophysiological, and microbiological studies.

Received for publication, December 1, 2003 , and in revised form, December 9, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at www.jbc.org) contains information on the cloning of additional NaChBac homologs.

These two authors contributed equally to this work.

Present address: 511 Goddard Laboratories, Dept. of Biology, University of Pennsylvania, Philadelphia, PA 19104.

^|| To whom correspondence should be addressed: Howard Hughes Medical Institute, Dept. of Cardiovascular Research, Children's Hospital and Dept. of Neurobiology, Harvard Medical School, 320 Longwood Ave., Boston, MA 02115. Tel.: 617-355-6163; Fax: 617-731-0787; E-mail: dclapham{at}enders.tch.harvard.edu.

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