Ultrasensitivity of an adaptive bacterial motor.

Ultrasensitivity of an adaptive bacterial motor.
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自适应细菌运动的超敏性。

DOI:
10.1016/j.jmb.2013.02.016
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发表时间:
2013-05-27
影响因子:
5.6
通讯作者:
Berg, Howard C.
Berg, Howard C.
中科院分区:
生物学2区
文献类型:
--
作者:
Yuan, Junhua;Berg, Howard C.

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大肠杆菌的鞭毛马达已经被证明通过调节Chey-P结合的分子的数量来适应趋化反应调节因子Chey-P的稳态水平的变化。以前已经在含有不同数量的Chey-P的细胞上进行了运动超敏感性的测量,因此也就是含有不同数量的薄膜。在这里,我们设计了一个实验来测量含有固定数量薄膜的电机的灵敏度,发现希尔系数大约是以前观察到的两倍。这种超敏感性为进一步深入了解电机切换机制提供了依据,并在多个电机的趋化、信号放大和协调方面发挥了重要作用。这里观察到的希尔系数似乎是已知的最高的变构蛋白质复合体,无论是生物的还是合成的。极端的运动超敏感性拓宽了我们对变构机制的理解,并对未来合成蛋白质开关的设计起到了启发作用。
The flagellar motor of Escherichia coli has been shown to adapt to changes in the steady-state level of the chemotaxis response regulator, CheY-P, by adjusting the number of molecules to which CheY-P binds, FliM. Previous measurements of motor ultrasensitivity have been made on cells containing different amounts of CheY-P, and thus different amounts of FliM. Here, we designed an experiment to measure the sensitivity of motors containing fixed amounts of FliM, finding Hill coefficients about twice as large as those observed before. This ultrasensitivity provides further insights into the motor switching mechanism and plays important roles in chemotaxis signal amplification and coordination of multiple motors. The Hill coefficients observed here appear to be the highest known for allosteric protein complexes, either biological or synthetic. Extreme motor ultrasensitivity broadens our understanding of mechanisms of allostery, and serves as an inspiration for future design of synthetic protein switches.
DOI: 10.1038/245380a0
发表时间: 1973-01-01
期刊: NATURE
影响因子: 64.8
作者:
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通讯作者: ANDERSON, RA
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期刊: FEBS LETTERS
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