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Light-regulated photoreceptor phosphodiesterase

Thesis/Dissertation ·
OSTI ID:6940387

The primary function of the rod outer segment (ROS) is to transduce a photon signal into a cellular response. Two sites of cGMP interaction with the ROS phosphodiesterase have direct bearing on the mechanism of phototransduction. In addition to the phosphodiesterase catalytic site, high affinity non-catalytic sites occur that specifically bind cGMP. These non-catalytic binding sites, identified and partially characterized by photoaffinity labeling with {sup 32}P-cGMP, are present on both the {alpha} and {beta}-subunits, and their concentration was determined to exceed the total ROS cGMP content by 4-fold, suggesting a limited availability of cGMP for interaction with the phosphodiesterase catalytic site and the cation channel binding site. Binding of cGMP to these non-catalytic sites was reported by Yamazaki et al. to be inhibited by activation of G-protein, but the possibility was not eliminated that the G-protein-induced increase in phosphodiesterase activity may have limited the availability of cGMP for binding. In the present studies it was shown that this apparent inhibition of cGMP binding by G-protein can be entirely attributed to an increased hydrolysis of cGMP, that activated G-protein does not alter any parameter of these non-catalytic cGMP binding sites.

Research Organization:
Minnesota Univ., Minneapolis, MN (USA)
OSTI ID:
6940387
Country of Publication:
United States
Language:
English