Proton transport by sensory rhodopsins and its modulation by transducer-binding.
Proton transport by sensory rhodopsins and its modulation by transducer-binding.
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感觉视紫红质的质子传输及其通过传感器结合的调节。
DOI：
10.1016/s0005-2728(00)00142-0
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Spudich,JL
中科院分区：
文献类型：
--
作者：
Sasaki,J;Spudich,JL
盐生盐杆菌（Halobacterium salinarum）的趋光性受体古细菌感觉视紫红质（SR）的光诱导质子转移研究为深入了解SR向信号复合物中同源转导子亚基的信号转导机制提供了重要的信息。细菌视紫红质（BR）泵送机制的基本特征已保存在传感器的演变，进行光驱动的生电质子运输时，他们的换能器被删除。SRI与其转换器的相互作用阻断受体中的质子传导通道，从而抑制其质子泵送，表明泵机制而不是运输活性本身对信号传导具有功能重要性。SRII突变体的分析表明，质子化的席夫碱和它的抗衡Asp 73之间的盐桥约束受体在其非活性构象。类似地，在BR中，质子化席夫碱和Asp 85之间的相应盐桥有助于将蛋白质限制在其细胞质通道关闭的构象中。传感器嵌合体的研究进一步表明，受体构象的变化是通过跨膜螺旋-螺旋相互作用从传感器传递到它们的同源传感器。这些和其他结果在这里审查支持的信号传导机制，其中倾斜的螺旋细胞质侧（主要是向外倾斜的螺旋F），类似于发生在BR在其开放的细胞质通道构象，导致结构改变的换能器跨膜螺旋。
The study of light-induced proton transfers in the archaeal sensory rhodopsins (SR), phototaxis receptors in Halobacterium salinarum, has contributed important insights into their mechanism of signaling to their cognate transducer subunits in the signaling complex. Essential features of the bacteriorhodopsin (BR) pumping mechanism have been conserved in the evolution of the sensors, which carry out light-driven electrogenic proton transport when their transducers are removed. The interaction of SRI with its transducer blocks proton-conducting channels in the receptor thereby inhibiting its proton pumping, indicating that the pump machinery, rather than the transport activity itself, is functionally important for signaling. Analysis of SRII mutants has shown that the salt bridge between the protonated Schiff base and its counterion Asp73 constrains the receptor in its inactive conformation. Similarly, in BR, the corresponding salt bridge between the protonated Schiff base and Asp85 contributes to constraining the protein in a conformation in which its cytoplasmic channel is closed. Transducer chimera studies further indicate that the receptor conformational changes are transmitted from the sensors to their cognate transducers through transmembrane helix–helix interaction. These and other results reviewed here support a signaling mechanism in which tilting of helices on the cytoplasmic side (primarily outward tilting of helix F), similar to that which occurs in BR in its open cytoplasmic channel conformation, causes structural alterations in the transducer transmembrane helices.
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影响因子：
2.9
作者：
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DOI：
--
发表时间：
1985
期刊：
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影响因子：
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作者：
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影响因子：
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作者：
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DOI：
--
发表时间：
1993
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Spudich,EN;Spudich,JL
通讯作者：
Spudich,JL