ArticleThe Journal of biological chemistry2013
The molecular basis of K+ exclusion by the Escherichia coli ammonium channel AmtB.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 19 citations in OpenAlex.
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Expression and Functional Analysis ofAnimals : an open access journal from MDPI · 2023Article
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- A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters.The Journal of biological chemistry · 2020Article
- SLC4A11 function: evidence for HAmerican journal of physiology. Cell physiology · 2020Article
- Ranking network mechanisms by how they fit diverse experiments and deciding onNPJ systems biology and applications · 2019Article
- Nitrogen isotope signature evidences ammonium deprotonation as a common transport mechanism for the AMT-Mep-Rh protein superfamily.Science advances · 2018Article
- The ctenidium of the giant clam, Tridacna squamosa, expresses an ammonium transporter 1 that displays light-suppressed gene and protein expression and may be involved in ammonia excretion.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2018Article
- Ammonia Transporters and Their Role in Acid-Base Balance.Physiological reviews · 2017Review
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- Growth Inhibition by External Potassium of Escherichia coli Lacking PtsN (EIIANtr) Is Caused by Potassium Limitation Mediated by YcgO.Journal of bacteriology · 2016Article
- Ammonia transport in the kidney by Rhesus glycoproteins.American journal of physiology. Renal physiology · 2014Review
- Uncoupling of ionic currents from substrate transport in the plant ammonium transporter AtAMT1;2.The Journal of biological chemistry · 2014Article
- Switching substrate specificity of AMT/MEP/ Rh proteins.Channels (Austin, Tex.) · 2014Review
- A molecular pathway for the egress of ammonia produced by nitrogenase.Scientific reports · 2013Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.