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J Biol Chem, Vol. 274, Issue 12, 7865-7869, March 19, 1999

Roles of the Transducin alpha -Subunit alpha 4-Helix/alpha 4-beta 6 Loop in the Receptor and Effector Interactions

Michael Natochin, Alexey E. Granovsky, Khakim G. Muradov, and Nikolai O. Artemyev

From the Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242

The visual GTP-binding protein, transducin, couples light-activated rhodopsin (R*) with the effector enzyme, cGMP phosphodiesterase in vertebrate photoreceptor cells. The region corresponding to the alpha 4-helix and alpha 4-beta 6 loop of the transducin alpha -subunit (Gtalpha ) has been implicated in interactions with the receptor and the effector. Ala-scanning mutagenesis of the alpha 4-beta 6 region has been carried out to elucidate residues critical for the functions of transducin. The mutational analysis supports the role of the alpha 4-beta 6 loop in the R*-Gtalpha interface and suggests that the Gtalpha residues Arg310 and Asp311 are involved in the interaction with R*. These residues are likely to contribute to the specificity of the R* recognition. Contrary to the evidence previously obtained with synthetic peptides of Gtalpha , our data indicate that none of the alpha 4-beta 6 residues directly or significantly participate in the interaction with and activation of phosphodiesterase. However, Ile299, Phe303, and Leu306 form a network of interactions with the alpha 3-helix of Gtalpha , which is critical for the ability of Gtalpha to undergo an activational conformational change. Thereby, Ile299, Phe303, and Leu306 play only an indirect role in the effector function of Gtalpha .

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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