Locking CNGA1 channels in the open and closed state

Biophysical Journal
Anil V NairV Torre

Abstract

With the aim of understanding the relation between structure and gating of CNGA1 channels from bovine rod, an extensive cysteine scanning mutagenesis was performed. Each residue from Phe-375 to Val-424 was mutated into a cysteine one at a time and the modification caused by various sulfhydryl reagents was analyzed. The addition of the mild oxidizing agent copper phenanthroline (CuP) in the open (presence of 1 mM cGMP) or closed state locked the channel in the respective states. A subsequent treatment with the reducing agent DTT restored normal gating fully in the open state and partially in the closed state. This action of CuP was not observed when F380 was mutated into a cysteine in the cysteine-free CNGA1 channel and in the double mutant C314S&F380C. These observations suggest that these effects are mediated by the formation of a disulfide bond (S-S) between F380C and the endogenous Cys-314 in the S5 segment. It can be rationalized by supposing that during gating the S6 segment rotates anticlockwise-when viewed from the extracellular side-by approximately 30 degrees .

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Citations

Apr 2, 2008·European Biophysics Journal : EBJ·Monica MazzoliniVincent Torre
Jan 10, 2009·European Biophysics Journal : EBJ·Anil V NairMonica Mazzolini
Jun 3, 2009·European Biophysics Journal : EBJ·Anil V NairMonica Mazzolini
Nov 10, 2009·Pflügers Archiv : European journal of physiology·Monica MazzoliniVincent Torre
Mar 18, 2009·The Journal of General Physiology·Monica MazzoliniVincent Torre
Feb 24, 2010·The Journal of General Physiology·Li DaiMichael C Sanguinetti
Feb 2, 2010·HFSP Journal·Paola LupieriPaolo Carloni
Oct 18, 2006·Proteins·Claudio AnselmiVincent Torre
Jun 24, 2015·Biomolecular Concepts·Paul Linsdell
Nov 21, 2009·Environmental Science & Technology·Nikolay N KolmakovAdelino V M Canario

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