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Am J Physiol Cell Physiol 273: C1278-C1289, 1997;
0363-6143/97 $5.00
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Vol. 273, Issue 4, C1278-C1289, October 1997

Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis

Hiroshi Ishihara and Michael J. Welsh

Howard Hughes Medical Institute, Departments of Internal Medicine and Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242

ATP hydrolysis by the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel predicts that energy from hydrolysis might cause asymmetric transitions in the gating cycle. We found that 3-(N-morpholino)propanesulfonic acid (MOPS) blocked the open channel by binding to a site 50% of the way through the electrical field. Block by MOPS revealed two distinct states, O1 and O2, which showed a strong asymmetry during bursts of activity; the first opening in a burst was in the O1 state and the last was in the O2 state. Addition of a nonhydrolyzable nucleoside triphosphate prevented the transition to the O2 state and prolonged the O1 state. These data indicate that ATP hydrolysis by the nucleotide-binding domains drives a series of asymmetric transitions in the gating cycle. They also indicate that ATP hydrolysis changes the conformation of the pore, thereby altering MOPS binding.

chloride channel; gating; cystic fibrosis transmembrane conductance regulator; buffer; anion; 3-(N-morpholino)propanesulfonic acid


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