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Article

Identification of membrane domains of the Na+/H+ antiporter (NhaA) protein from Helicobacter pylori required for ion transport and pH sensing.

The Journal of biological chemistry - 13 Jun 2003

Tsuboi Yumi, Inoue Hiroki, Nakamura Norihiro, Kanazawa Hiroshi

Abstract excerpt

The Na+/H+ antiporter from Helicobacter pylori (HP NhaA) is normally active within the pH range 6.0-8.5. In contrast, the NhaA from Escherichia coli (EC NhaA) is active only within the alkaline pH range 7.5-8.5. We studied structures of HP NhaA involved in ion transport and pH sensing by analyzing mutants with defects in NhaA activity. The 36 mutants were classified into three types. The first type exhibited very...

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PMID: 12670937
DOI: 10.1074/jbc.M301932200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Identification of membrane domains of the Na+/H+ antiporter (NhaA) protein from Helicobacter pylori required for ion transport and pH sensing.PMID 12670937Read ↗

The fourth transmembrane domain of the Helicobacter pylori Na+/H+ antiporter NhaA faces a water-filled channel required for ion transport.Semantic proximity Read ↗

Towards Molecular Understanding of the pH Dependence Characterizing NhaA of Which Structural Fold is Shared by Other Transporters.Semantic proximity Read ↗

Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.Semantic proximity Read ↗

A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli.Semantic proximity Read ↗

Helix VIII of NhaA Na(+)/H(+) antiporter participates in the periplasmic cation passage and pH regulation of the antiporter.Semantic proximity Read ↗

Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.Semantic proximity Read ↗

Regulation of NhaA by protons.Semantic proximity Read ↗

NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporter.Semantic proximity Read ↗

NhaA Na+/H+ antiporter mutants that hardly react to the membrane potential.Semantic proximity Read ↗

Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli.Semantic proximity Read ↗

NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability.Semantic proximity Read ↗

Lysine 300 is essential for stability but not for electrogenic transport of the Escherichia coli NhaA Na+/H+ antiporter.Semantic proximity Read ↗

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