Trans Membrane Domain IV Is Involved in Ion Transport Activity and pH Regulation of the NhaA-Na+/H+ Antiporter of Escherichia coli

We have previously shown that the activity of NhaA is regulated by pH and found mutations that affect dramatically the pH dependence of the rate but not the K m (for Na+ and Li+) of NhaA. In the present work, we found that helix IV is involved both in ion translocation as well as in pH regulation of...

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Veröffentlicht in:	Biochemistry (Easton) 2002-01, Vol.41 (2), p.609-617
Hauptverfasser:	Galili, Livnat, Rothman, Andrea, Kozachkov, Lena, Rimon, Abraham, Padan, Etana
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Cell Membrane - metabolism Cysteine - chemistry Cytoplasm - metabolism Dose-Response Relationship, Drug Escherichia coli - chemistry Escherichia coli - metabolism Escherichia coli Proteins Ethylmaleimide - pharmacology Hydrogen-Ion Concentration Ions Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Mutation Phenotype Plasmids - metabolism Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Protein Transport Sequence Homology, Amino Acid Sodium - metabolism Sodium-Hydrogen Exchangers - chemistry Sodium-Hydrogen Exchangers - metabolism Time Factors
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