Recoverin alters its surface properties depending on both calcium-binding and N-terminal myristoylation.
Recoverin alters its surface properties depending on both calcium-binding and N-terminal myristoylation.
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恢复素根据钙结合和 N 末端肉豆蔻酰化改变其表面特性。
DOI：
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发表时间：
1993
期刊：
影响因子：
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通讯作者：
F. Tokunaga
中科院分区：
文献类型：
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作者：
M. Kataoka;K. Mihara;F. Tokunaga
本文用小角X射线散射和圆二色性方法研究了脊椎动物光感受器的23 kDa钙结合蛋白recoverin的溶液结构和钙依赖性结构变化，以及N-末端豆蔻酰化的影响。CD光谱不受N-末端豆蔻酰化的影响，但强烈地受Ca 2+的影响，表明单独的N-末端豆蔻酰化不会引起构象变化。由Ca 2+诱导的recoverin的主要构象变化的特征在于在α-螺旋含量的蛋白质和在去除Ca 2+后的全球尺寸的增加减少。在Ca ~（2+）存在下，未豆蔻酰化的recoverin在溶液中呈单体球状，而N端豆蔻酰化导致聚集。在没有Ca 2+的情况下，未豆蔻酰化的恢复蛋白倾向于聚集，而豆蔻酰化的恢复蛋白变成单体和球状。这些观察结果表明，recoverin改变其表面性质，这取决于钙结合和N-末端豆蔻酰化。蜂毒肽仅在不存在Ca 2+的情况下与肉豆蔻酰化的恢复素非特异性地相互作用。这可能表明恢复素与其正常生理靶酶之间的相互作用的性质。
The solution structure and calcium-dependent structural changes of recoverin, a 23 kDa calcium binding protein of vertebrate photoreceptors, have been studied by small-angle X-ray scattering and CD, as well as the effect of N-terminal myristoylation. The CD spectrum is not affected by N-terminal myristoylation, but strongly affected by Ca2+, indicating that N-terminal myristoylation alone does not cause a conformational change. The major conformational change in recoverin induced by Ca2+ is characterized as a decrease in the alpha-helical content of the protein and an increase in global size upon removal of Ca2+. In the presence of Ca2+, unmyristoylated recoverin is monomeric and globular in solution, while N-terminal myristoylation brings about aggregation. In the absence of Ca2+, unmyristoylated recoverin tends to aggregate, while myristoylated recoverin becomes monomeric and globular. These observations indicate that recoverin changes its surface properties depending on both calcium binding and N-terminal myristoylation. Melittin interacts non-specifically only with the myristoylated recoverin in the absence of Ca2+. This may be indicative of the properties of the interaction between recoverin and its normal physiological target enzyme.