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Transducin subunit stoichiometry and cellular distribution in rod outer segments.

机译:杆外段的转导蛋白亚基化学计量和细胞分布。

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摘要

Transducin is a heterotrimeric GTP-binding protein found in the outer segment of vertebrate retinas that links the photoactivation of rhodopsin (R*) with activation of a robust type VI cGMP phosphodiesterase (PDE6). Association of the alpha subunit of Transducin (G(alphat)) with the beta-gamma complex (G(betagamma)) is necessary for interaction of the holoprotein with R* and exchange of a GTP for a previously bound GDP. We have investigated the abundances of the three Transducin subunits by eluting them from bovine rod outer segment membranes by centrifugation under various conditions in vitro. We find that a substantial amount of G(betagamma) is eluted from ROS under conditions that do not elute G(alphat) and that there is an overall three to fourfold molar excess of G(betagamma) to G(alphat) in rod outer segments. These results suggest that the production and/or turnover of G(alphat), G(beta), and G(gamma) in the rod outer segment are controlled independently.
机译:转导蛋白是在脊椎动物视网膜的外部片段中发现的异三聚体GTP结合蛋白,将视紫红质(R *)的光激活与强大的VI型cGMP磷酸二酯酶(PDE6)的激活联系在一起。转导蛋白的α亚基(G(alphat))与β-γ复合物(G(betagamma))的结合对于全蛋白与R *的相互作用以及GTP交换为先前结合的GDP是必需的。我们已经通过在体外在各种条件下离心从牛杆外节膜上洗脱下来的3个Transducin亚基进行了研究。我们发现在不洗脱G(alphat)的条件下从ROS洗脱出大量的G(betagamma),并且在杆外段中G(betagamma)相对于G(alphat)的摩尔总量为三到四倍。这些结果表明,杆外段中Gα,Gβ和Gγ的产生和/或周转是独立控制的。

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