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J. Biol. Chem., Vol. 265, Issue 29, 17520-17524, Oct, 1990
SS Karnik and HG Khorana
Cysteine residues 110 and 187 are essential for the formation of the
correct bovine rhodopsin structure (Karnik, S. S., Sakmar, T. P., Chen,
H.-B., and Khorana, H. G. (1988) Proc. Natl. Acad. Sci. U. S. A. 85,
8459-8463). We now show that the sulfhydryl groups of these 2 cysteine
residues interact to form a disulfide bond. Rhodopsin mutants containing
cysteine----serine substitutions were prepared as follows. In one mutant,
CysVII, all the 10 cysteine residues of rhodopsin were replaced by serines.
A second mutant, CysVIII, contained only C110 and C185; a third mutant,
CysIX, contained only C185 and C187 while the fourth mutant, CysX,
contained only C110 and C187. Only mutant CysX formed functional rhodopsin.
Mutants CysVIII and CysIX reacted with [3H]iodoacetic acid showing the
presence of free sulfhydryl groups while mutant CysX was inert to this
reagent. CysX reacted with cyanide ion to form a thiocyanate derivative
showing the presence of a disulfide bond. The C110-C187 disulfide bond is
buried in rhodopsin because reactions with disulfide reducing agents and
cyanide ion require prior treatment with denaturants.
Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
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