Results 11 to 20 of about 79 (69)
The Na+ and K+ transport deficiency of an E. coli mutant lacking the NhaA and NhaB proteins is apparent and caused by impaired osmoregulation [PDF]
Cells of the E. coli mutant EP432, which lacks the two Na+/H+ antiporters, NhaA and NhaB, have been reported to have an impaired sodium transport activity (Harel-Bronstein et al. (1995) J. Biol. Chem. 270, 3816–3822). Here we report that active transport
Michael I Verkhovsky +7 more
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Functional characterization of a NapA Na(+)/H(+) antiporter from Thermus thermophilus. [PDF]
Na(+)/H(+) antiporters are ubiquitous membrane proteins and play an important role in cell homeostasis. We amplified a gene encoding a member of the monovalent cation:proton antiporter-2 (CPA2) family (TC 2.A.37) from the Thermus thermophilus genome and ...
Furrer, E M +7 more
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Calcium transport mediated by NhaA, a Na+/H+ antiporter from Escherichia coli [PDF]
In everted membrane vesicles of E. coli strain EP432/pGM42, which has only one Na+/H+ antiporter (NhaA), external CaC4 inhibits dissipation of the respiration-dependent ΔpH in response to the addition of NaCl at pH 7.5, and decreases equilibrium ...
P.A. Dibrov, Dibrov, P.A.
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PeNhaD1 encodes a putative Na+/H+ antiporter from the salt-resistant tree Populus euphratica. It is the first characterization of a member of the NhaD type ion transporter family of plant origin.
Brosché, Mikael +6 more
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A167P NhaA mutant growth and expression.
(A) The double mutant A167P (TM V)-N359D (TM XII) and the previously [24] isolated mutant F267C (TM IX) are shown in red (ball and stick) on the NhaA structure without TM I, for clarity (ribbon presentation by PyMol). Asp163 and Asp164 are shown in black
Miyer Patino-Ruiz (546856) +6 more
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Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli.
Following on from our previous discovery of Na+ pumping by the NADH:ubiquinone oxidoreductase (complex I) of Klebsiella pneumoniae, we show here that complex I from Escherichia coli is a Na+ pump as well.
Schmid C +3 more
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pH dependence of the Na+, Li+/H+ antiporter activity in everted membrane vesicles of variant A167P.
Everted membrane vesicles were prepared from EP432 cells grown in LBK (pH 7) and expressing WT (□) or A167P (Δ). The Na+/H+ and Li+/H+ antiporter activity was determined in the presence of 10 mM NaCl (filled symbols) or 10 mM LiCl (open symbols) at the ...
Miyer Patino-Ruiz (546856) +6 more
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Expression level, growth phenotype and Na+/H+ antiporter activity of variant A167P.
aFor characterization of variant A167P, the E coli KNabc (lines 1–4) and E coli EP432 (lines 5–9) cells were transformed with plasmids expressing the indicated variants.
Miyer Patino-Ruiz (546856) +6 more
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Recently, a two-dimensional crystal structure of NhaA, the Na+/H+ antiporter of Escherichia coli has been obtained [Williams, K. A., Kaufer, U. G., Padan, E., Schuldiner, S. and Kühlbrandt, W. (1999) EMBO J., 18, 3558−3563]. In these crystals NhaA exists
Padan, E. +3 more
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Na+/H+ antiporter activity of variant A167P in isolated everted membrane vesicles.
For measurement of the Na+/H+ antiporter activity at the indicated pHs, E. coli EP432/A167P cells expressing variant A167P (A and B) or the wild type (C and D) were grown in LBK (pH 7.0) and everted membrane vesicles were isolated.
Miyer Patino-Ruiz (546856) +6 more
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