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Journal of Bacteriology, June 2002, p. 3396-3400, Vol. 184, No. 12
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.12.3396-3400.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Gas Channels for NH3: Proteins from Hyperthermophiles Complement an Escherichia coli Mutant

Eric Soupene,1 Tony Chu,1,{dagger} Rebecca W. Corbin,2,{ddagger} Donald F. Hunt,2 and Sydney Kustu1*

Department of Plant and Microbial Biology, University of California, Berkeley, California 94720,1 Department of Chemistry, University of Virginia, Charlottesville, Virginia 229012

Received 11 February 2002/ Accepted 20 March 2002

Ammonium transport (Amt) proteins appear to be bidirectional channels for NH3. The amt genes of the hyperthermophiles Aquifex aeolicus and Methanococcus jannaschii complement enteric amtB mutants for growth at 25 nM NH3 at 37°C. To our knowledge, Amt proteins are the first hyperthermophilic membrane transport proteins shown to be active in a mesophilic bacterium. Despite low expression levels, His-tagged Aquifex Amt could be purified by heating and nickel chelate affinity chromatography. It could be studied genetically in Escherichia coli.


* Corresponding author. Mailing address: Department of Plant and Microbial Biology, University of California, 111 Koshland Hall #3102, Berkeley, CA 94720-3102. Phone: (510) 643-9308. Fax: (510) 642-4995. E-mail: kustu{at}nature.berkeley.edu.

{dagger} Present address: University of California, San Diego, La Jolla, CA 92093-0348.

{ddagger} Present address: Ashland University, Department of Chemistry, Ashland, OH 44805.


Journal of Bacteriology, June 2002, p. 3396-3400, Vol. 184, No. 12
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.12.3396-3400.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




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