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The molecular basis of K+ exclusion by the Escherichia coli ammonium channel AmtB.

ABSTRACT: Members of the Amt family of channels mediate the transport of ammonium. The form of ammonium, NH3 or NH4(+), carried by these proteins remains controversial, and the mechanism by which they select against K(+) ions is unclear. We describe here a set of Escherichia coli AmtB proteins carrying mutations at the conserved twin-histidine site within the conduction pore that have altered substrate specificity and now transport K(+). Subsequent work established that AmtB-mediated K(+) uptake occurred against a concentration gradient and was membrane potential-dependent. These findings indicate that the twin-histidine element serves as a filter to prevent K(+) conduction and strongly support the notion that Amt proteins transport cations (NH4(+) or, in mutant proteins, K(+)) rather than NH3 gas molecules through their conduction pores.

SUBMITTER: Hall JA

PROVIDER: S-EPMC3656265 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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The molecular basis of K+ exclusion by the Escherichia coli ammonium channel AmtB.

Hall Jason A JA Yan Dalai D

The Journal of biological chemistry 20130401 20

Members of the Amt family of channels mediate the transport of ammonium. The form of ammonium, NH3 or NH4(+), carried by these proteins remains controversial, and the mechanism by which they select against K(+) ions is unclear. We describe here a set of Escherichia coli AmtB proteins carrying mutations at the conserved twin-histidine site within the conduction pore that have altered substrate specificity and now transport K(+). Subsequent work established that AmtB-mediated K(+) uptake occurred ...[more]

PMID: 23546877

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