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Science 31 January 1992:
Vol. 255. no. 5044, pp. 600 - 603
DOI: 10.1126/science.1371017
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Articles
Science, Vol 255, Issue 5044, 600-603
Copyright © 1992 by American Association for the Advancement of Science
Regulation of adenylyl cyclase from Paramecium by an intrinsic potassium conductance
JE Schultz,
S Klumpp,
R Benz,
WJ Schurhoff-Goeters,
and
A Schmid
Pharmazeutisches Institut, Universitat Tubingen, Germany.
Hyperpolarization of the cell membrane of Paramecium stimulates adenosine 3',5'-monophosphate (cAMP) formation. Manipulations of the K+ resting conductance of the ciliate by adaptation in different buffers affected excitability of the cAMP generating system. Blockade of K+ channels inhibited hyperpolarization-stimulated cAMP formation. A mutant of Paramecium that is unable to control its K+ resting conductance had a defect in cAMP formation. Purified adenylyl cyclase, when incorporated into an artificial lipid bilayer membrane, revealed properties of a voltage-independent K+ channel. This indicates that the adenylyl cyclase of Paramecium has a secondary function as carrier of the K+ resting conductance. A hyperpolarization-activated K+ efflux appears to directly regulate adenylyl cyclase activity in vivo.
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