Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence

Michal Maes; Abraham Rimon; Lena Kozachkov-Magrisso; Assaf Friedler; Etana Padan

doi:10.1074/jbc.M112.391128

Revealing the ligand binding site of NhaA Na⁺/H⁺ antiporter and its pH dependence

Michal Maes, Abraham Rimon, Lena Kozachkov-Magrisso, Assaf Friedler, Etana Padan

The Hebrew University of Jerusalem

Research output: Contribution to journal › Article › peer-review

Abstract

Background: Cell pH and Na⁺ homeostasis requires Na ⁺/H⁺ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li⁺ binding site. Conclusion: Binding of Li⁺ to purified NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. Significance: The pH-dependent NhaA-ligand binding is an insight into the mechanism of activity of NhaA and possibly other antiporters.

Original language	English
Pages (from-to)	38150-38157
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	287
Issue number	45
DOIs	https://doi.org/10.1074/jbc.M112.391128
State	Published - 2 Nov 2012

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M112.391128

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abstract = "Background: Cell pH and Na+ homeostasis requires Na +/H+ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li+ binding site. Conclusion: Binding of Li+ to purified NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. Significance: The pH-dependent NhaA-ligand binding is an insight into the mechanism of activity of NhaA and possibly other antiporters.",

author = "Michal Maes and Abraham Rimon and Lena Kozachkov-Magrisso and Assaf Friedler and Etana Padan",

year = "2012",

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AU - Maes, Michal

AU - Rimon, Abraham

AU - Kozachkov-Magrisso, Lena

AU - Friedler, Assaf

AU - Padan, Etana

PY - 2012/11/2

Y1 - 2012/11/2

N2 - Background: Cell pH and Na+ homeostasis requires Na +/H+ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li+ binding site. Conclusion: Binding of Li+ to purified NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. Significance: The pH-dependent NhaA-ligand binding is an insight into the mechanism of activity of NhaA and possibly other antiporters.

AB - Background: Cell pH and Na+ homeostasis requires Na +/H+ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li+ binding site. Conclusion: Binding of Li+ to purified NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. Significance: The pH-dependent NhaA-ligand binding is an insight into the mechanism of activity of NhaA and possibly other antiporters.

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U2 - 10.1074/jbc.M112.391128

DO - 10.1074/jbc.M112.391128

M3 - مقالة

C2 - 22915592

SN - 0021-9258

VL - 287

SP - 38150

EP - 38157

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 45

ER -

Revealing the ligand binding site of NhaA Na⁺/H⁺ antiporter and its pH dependence

Abstract

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