This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Soupene, E.
Right arrow Articles by Kustu, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Soupene, E.
Right arrow Articles by Kustu, S.

 Previous Article  |  Next Article 

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.



This article has been cited by other articles:

  • Fong, R. N., Kim, K.-S., Yoshihara, C., Inwood, W. B., Kustu, S. (2007). The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion. Proc. Natl. Acad. Sci. USA 104: 18706-18711 [Abstract] [Full Text]  
  • Khademi, S., Stroud, R. M. (2006). The Amt/MEP/Rh Family: Structure of AmtB and the Mechanism of Ammonia Gas Conduction.. Physiology 21: 419-429 [Abstract] [Full Text]  
  • Wei, Y., Deikus, G., Powers, B., Shelden, V., Krulwich, T. A., Bechhofer, D. H. (2006). Adaptive Gene Expression in Bacillus subtilis Strains Deleted for tetL.. J. Bacteriol. 188: 7090-7100 [Abstract] [Full Text]  
  • Zhang, Y., Wolfe, D. M., Pohlmann, E. L., Conrad, M. C., Roberts, G. P. (2006). Effect of AmtB homologues on the post-translational regulation of nitrogenase activity in response to ammonium and energy signals in Rhodospirillum rubrum. Microbiology 152: 2075-2089 [Abstract] [Full Text]  
  • Ji, Q., Hashmi, S., Liu, Z., Zhang, J., Chen, Y., Huang, C.-H. (2006). CeRh1 (rhr-1) is a dominant Rhesus gene essential for embryonic development and hypodermal function in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 103: 5881-5886 [Abstract] [Full Text]  
  • Chambrey, R., Goossens, D., Bourgeois, S., Picard, N., Bloch-Faure, M., Leviel, F., Geoffroy, V., Cambillau, M., Colin, Y., Paillard, M., Houillier, P., Cartron, J. P., Eladari, D. (2005). Genetic ablation of Rhbg in the mouse does not impair renal ammonium excretion. Am. J. Physiol. Renal Physiol. 289: F1281-F1290 [Abstract] [Full Text]  
  • Huang, C.-H., Peng, J. (2005). Evolutionary conservation and diversification of Rh family genes and proteins. Proc. Natl. Acad. Sci. USA 102: 15512-15517 [Abstract] [Full Text]  
  • Andrade, S. L. A., Dickmanns, A., Ficner, R., Einsle, O. (2005). Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc. Natl. Acad. Sci. USA 102: 14994-14999 [Abstract] [Full Text]  
  • Kim, K.-S., Feild, E., King, N., Yaoi, T., Kustu, S., Inwood, W. (2005). Spontaneous Mutations in the Ammonium Transport Gene AMT4 of Chlamydomonas reinhardtii. Genetics 170: 631-644 [Abstract] [Full Text]  
  • Nakhoul, N. L., DeJong, H., Abdulnour-Nakhoul, S. M., Boulpaep, E. L., Hering-Smith, K., Hamm, L. L. (2005). Characteristics of renal Rhbg as an NH4+ transporter. Am. J. Physiol. Renal Physiol. 288: F170-F181 [Abstract] [Full Text]  
  • Zheng, L., Kostrewa, D., Berneche, S., Winkler, F. K., Li, X.-D. (2004). The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli. Proc. Natl. Acad. Sci. USA 101: 17090-17095 [Abstract] [Full Text]  
  • Khademi, S., O'Connell, J. III, Remis, J., Robles-Colmenares, Y., Miercke, L. J. W., Stroud, R. M. (2004). Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 A. Science 305: 1587-1594 [Abstract] [Full Text]  
  • Soupene, E., Inwood, W., Kustu, S. (2004). From The Cover: Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2. Proc. Natl. Acad. Sci. USA 101: 7787-7792 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»