用单个残基调节电压传感器运动。
Tuning the voltage-sensor motion with a single residue.
机构信息
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.
出版信息
Biophys J. 2012 Aug 8;103(3):L23-L25. doi: 10.1016/j.bpj.2012.06.030.
Abstract
The Ciona intestinalis voltage-sensitive phosphatase (Ci-VSP) represents the first discovered member of enzymes regulated by a voltage-sensor domain (VSD) related to the VSD found in voltage-gated ion channels. Although the VSD operation in Ci-VSP exhibits original voltage dependence and kinetics compared to ion channels, it has been poorly investigated. Here, we show that the kinetics and voltage dependence of VSD movement in Ci-VSP can be tuned over 2 orders of magnitude and shifted over 120 mV, respectively, by the size of a conserved isoleucine (I126) in the S1 segment, thus indicating the importance of this residue in Ci-VSP activation. Mutations of the conserved Phe in the S2 segment (F161) do not significantly perturb the voltage dependence of the VSD movement, suggesting a unique voltage sensing mechanism in Ci-VSP.
摘要
秀丽隐杆线虫电压敏感磷酸酶（Ci-VSP）是第一个被发现的受电压传感器域（VSD）调控的酶，该 VSD 与电压门控离子通道中的 VSD 有关。尽管 Ci-VSP 中的 VSD 与离子通道相比，其工作方式具有独特的电压依赖性和动力学特征，但尚未得到充分研究。在这里，我们表明，S1 片段中保守的异亮氨酸（I126）的大小可以使 Ci-VSP 中的 VSD 运动的动力学和电压依赖性分别在 2 个数量级内进行调节，并向超过 120 mV 移动，这表明该残基对 Ci-VSP 的激活很重要。S2 片段中保守的苯丙氨酸（F161）的突变不会显著改变 VSD 运动的电压依赖性，这表明 Ci-VSP 具有独特的电压感应机制。
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