Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense

Schürholz T, Dloczik L, Neumann E (1993)
Biophysical Journal 64(1): 58-67.

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The anion channel protein from Clavibacter michiganense ssp. nebraskense (Schurholz, Th. et al. 1991, J. Membrane Biol. 123: 1-8) was analyzed at different concentrations of KCl and KF. At 0.8 M KCl the conductance G(V(m)) increases exponentially from 21 pS at 50 mV up to 53 pS at V(m) = 200 mV, 20-degrees-C. The concentration dependence of G(V(m)) corresponds to a Michaelis-Menten type saturation function at all membrane voltage values applied (0-200 mV). The anion concentration K0.5, where G (V(m)) has its half-maximum value, increases from 0.12 M at 50 mV to 0.24 M at 175 mV for channels in a soybean phospholipid bilayer. The voltage dependence of the single channel conductance, which is different for charged and neutral lipid bilayers, can be described either by a two-state flicker (2SF) model and the Nernst-Planck continuum theory, or by a two barrier, one-site (2Bl S) model with asymmetric barriers. The increase in the number of open channels after a voltage jump from 50 mV to 150 mV has a time constant of 0.8 s. The changes of the single-channel conductance are much faster (<1 ms). The electric part of the gating process is characterized by the (reversible) molar electrical work DELTAG(el)theta = rhoz(g)FV(m) almost-equal-to -1.3 RT, which corresponds to the movement of one charge of the gating charge number \z(g)\ = 1 across the fraction rho = DELTAV(m)/V(m) = 0.15 of the membrane voltage V(m) = 200 mV. Unlike with chloride, the single channel conductance of fluoride has a maximum at about 150 mV in the presence of the buffer PIPES (greater-than-or-equal-to 5 mM, pH 6.8) with K0.5 almost-equal-to 1 M. It is shown that the decrease in conductance is due to a blocking of the channel by the PIPES anion. In summary, the results indicate that the anion transport by the Clavibacter anion channel (CAC) does not require a voltage dependent conformation change of the CAC.
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Schürholz T, Dloczik L, Neumann E. Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense. Biophysical Journal. 1993;64(1):58-67.
Schürholz, T., Dloczik, L., & Neumann, E. (1993). Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense. Biophysical Journal, 64(1), 58-67.
Schürholz, T., Dloczik, L., and Neumann, E. (1993). Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense. Biophysical Journal 64, 58-67.
Schürholz, T., Dloczik, L., & Neumann, E., 1993. Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense. Biophysical Journal, 64(1), p 58-67.
T. Schürholz, L. Dloczik, and E. Neumann, “Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense”, Biophysical Journal, vol. 64, 1993, pp. 58-67.
Schürholz, T., Dloczik, L., Neumann, E.: Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense. Biophysical Journal. 64, 58-67 (1993).
Schürholz, Theo, Dloczik, Larissa, and Neumann, Eberhard. “Single-channel analysis of the anion channel-forming protein from the plant pathogenic bacterium Clavibacter michiganense ssp. nebraskense”. Biophysical Journal 64.1 (1993): 58-67.
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