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枯草芽孢杆菌组氨酸激酶DesK膜结构域温度感应能力的遗传学证据

Genetic evidence for the temperature-sensing ability of the membrane domain of the Bacillus subtilis histidine kinase DesK.

作者信息

Hunger Karen, Beckering Carsten L, Marahiel Mohamed A

机构信息

Philipps-Universität Marburg, FB Chemie/Biochemie, Hans-Meerwein-Strasse, 35032 Marburg, Germany.

出版信息

FEMS Microbiol Lett. 2004 Jan 15;230(1):41-6. doi: 10.1016/S0378-1097(03)00852-8.

Abstract

A decrease in environmental temperature leads to the synthesis of Delta5-unsaturated fatty acids in Bacillus subtilis by the fatty acid desaturase Des. Des is regulated by the two-component system DesKR. To understand the mechanism of cold signal perception and transduction by the membrane domain and the cytosolic domain of DesK, we expressed the cytosolic domain of DesK in trans under the control of a xylose-inducible promoter without the membrane domain. We performed growth experiments and a Northern blot analysis. Our results show that the kinase function of the cytosolic domain of DesK is temperature-independent, leading to a constitutive expression of the des gene. These findings support the conclusion that the membrane domain of DesK is the temperature-sensing element of the two-component system.

摘要

环境温度降低会导致枯草芽孢杆菌中的脂肪酸去饱和酶Des合成Δ5-不饱和脂肪酸。Des由双组分系统DesKR调控。为了了解DesK的膜结构域和胞质结构域对冷信号的感知和转导机制,我们在没有膜结构域的情况下,在木糖诱导型启动子的控制下反式表达DesK的胞质结构域。我们进行了生长实验和Northern印迹分析。我们的结果表明,DesK胞质结构域的激酶功能与温度无关,导致des基因的组成型表达。这些发现支持了DesK的膜结构域是双组分系统的温度感应元件这一结论。

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