LIGHT-REGULATED AND GTP-REGULATED INTERACTION OF GTPASE AND OTHER PROTEINS WITH BOVINE PHOTORECEPTOR-MEMBRANES
LIGHT-REGULATED AND GTP-REGULATED INTERACTION OF GTPASE AND OTHER PROTEINS WITH BOVINE PHOTORECEPTOR-MEMBRANES
复制标题
DOI：
10.1038/283587a0
复制
发表时间：
1980-01-01
期刊：
影响因子：
64.8
通讯作者：
KUHN, H
中科院分区：
文献类型：
--
作者：
KUHN, H
光通过感光杆外节（ROS）吸收不仅导致视紫红质分子的光谱和结构变化1，而且还导致包括GTP酶7 -10在内的几种酶活性的激活2 - 6。这种效应的机制尚不清楚;然而，在所有光诱导酶激活的作用光谱已被测量的情况下（参见，例如，参考文献4，8），它匹配的吸收光谱的视紫红质。这表明，漂白的视紫红质是在酶的活化的主要步骤，和一些光诱导的变化的分子相互作用的酶与视紫红质，主要的内在ROS膜蛋白，应该参与。我确实发现光诱导视紫红质激酶11、GTdR（本文报道）和其他蛋白质与感光细胞膜相互作用的深刻变化。这些变化在黑暗中是可逆的，受到GTP的强烈影响，并且被认为参与了光对酶活性的调节。光诱导的结合的GTP酶和其随后的洗脱与GTP被用来纯化这种酶。
Light absorption by photoreceptor rod outer segments (ROS) leads not only to spectral and structural changes in the rhodopsin molecule1but also to the activation of several enzymatic activities2–6including GTPase7–10. The mechanism of this effect is not known; however, in all cases where the action spectrum of light-induced enzyme activation has been measured (see, for example, refs 4, 8), it matched the absorption spectrum of rhodopsin. This suggests that bleaching of rhodopsin is the primary step in enzyme activation, and that some light-induced changes in the molecular interaction of the enzymes with rhodopsin, the major intrinsic ROS membrane protein, should be involved. I have indeed found that light induces profound changes in the interaction of rhodopsin kinase11, GTPase (reported here), and other proteins with the photoreceptor membrane. These changes are reversible in the dark, are strongly influenced by GTP, and are thought to be involved in the regulation of enzyme activity by light. The light-induced binding of the GTPase and its subsequent elution with GTP was used to purify this enzyme.