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Literature DB >> 9518558

Topological study of Vibrio alginolyticus NhaB Na+/H+ antiporter using gene fusions in Escherichia coli cells.

H Enomoto¹, T Unemoto, M Nishibuchi, E Padan, T Nakamura.

Abstract

NhaB, an Na+/H+ antiporter, of Vibrio alginolyticus is a 528-amino-acid protein. Hydropathy profile-based computer analysis predicted that the NhaB might contain up to 13 membrane-spanning domains. To examine this hypothesis, we applied the phoA fusion method to the cloned nhaB gene. Eighteen plasmid-borne nhaB-phoA fusion genes were constructed in Escherichia coli cells and the alkaline phosphatase activity and expression level of the fusion proteins analyzed. These results and the results obtained with additional constructs indicated that V. alginolyticus NhaB has a unique topology consisting of nine transmembrane segments with the N-terminus in the cytoplasm and the C-terminus in the periplasm. Copyright 1998 Elsevier Science B.V.

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Year: 1998 PMID： 9518558 DOI： 10.1016/s0005-2736(97)00245-9

Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002

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Cited

7 in total

1. Na+/H+ antiporter from Synechocystis species PCC 6803, homologous to SOS1, contains an aspartic residue and long C-terminal tail important for the carrier activity.

Authors: A Hamada; T Hibino; T Nakamura; T Takabe
Journal: Plant Physiol Date: 2001-01 Impact factor: 8.340

2. Residue aspartate-147 from the third transmembrane region of Na(+)/H(+) antiporter NhaB of Vibrio alginolyticus plays a role in its activity.

Authors: T Nakamura; Y Fujisaki; H Enomoto; Y Nakayama; T Takabe; N Yamaguchi; N Uozumi
Journal: J Bacteriol Date: 2001-10 Impact factor: 3.490

3. Evidence in support of a four transmembrane-pore-transmembrane topology model for the Arabidopsis thaliana Na+/K+ translocating AtHKT1 protein, a member of the superfamily of K+ transporters.

Authors: Y Kato; M Sakaguchi; Y Mori; K Saito; T Nakamura; E P Bakker; Y Sato; S Goshima; N Uozumi
Journal: Proc Natl Acad Sci U S A Date: 2001-05-08 Impact factor: 11.205

4. Determination of transmembrane topology of an inward-rectifying potassium channel from Arabidopsis thaliana based on functional expression in Escherichia coli.

Authors: N Uozumi; T Nakamura; J I Schroeder; S Muto
Journal: Proc Natl Acad Sci U S A Date: 1998-08-18 Impact factor: 11.205

Topological study of Vibrio alginolyticus NhaB Na+/H+ antiporter using gene fusions in Escherichia coli cells.

1. Na+/H+ antiporter from Synechocystis species PCC 6803, homologous to SOS1, contains an aspartic residue and long C-terminal tail important for the carrier activity.

2. Residue aspartate-147 from the third transmembrane region of Na(+)/H(+) antiporter NhaB of Vibrio alginolyticus plays a role in its activity.

3. Evidence in support of a four transmembrane-pore-transmembrane topology model for the Arabidopsis thaliana Na+/K+ translocating AtHKT1 protein, a member of the superfamily of K+ transporters.

4. Determination of transmembrane topology of an inward-rectifying potassium channel from Arabidopsis thaliana based on functional expression in Escherichia coli.

5. Roles of NhaA, NhaB, and NhaD Na+/H+ antiporters in survival of Vibrio cholerae in a saline environment.

6. Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.

7. Mutation of two key aspartate residues alters stoichiometry of the NhaB Na⁺/H⁺ exchanger from Klebsiella pneumoniae.