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(Received for publication, August 9, 1996)
From the Divisions of Cell Biology and § Genetics,
Research Institute, Hospital for Sick Children,
Toronto, Canada M5G 1X8
The gene mutated in cystic fibrosis codes for the
cystic fibrosis transmembrane conductance regulator (CFTR), a cyclic
AMP-activated chloride channel thought to be critical for salt and
water transport by epithelial cells. Plausible models exist to describe
a role for ATP hydrolysis in CFTR channel activity; however,
biochemical evidence that CFTR possesses intrinsic ATPase activity is
lacking. In this study, we report the first measurements of the rate of
ATP hydrolysis by purified, reconstituted CFTR. The mutation CFTRG551D
resides within a motif conserved in many nucleotidases and is known to
cause severe human disease. Following reconstitution the mutant protein
exhibited both defective ATP hydrolysis and channel gating, providing
direct evidence that CFTR utilizes ATP to gate its channel
activity.
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28463-28468
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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