温度极端的热力学补偿在B. subtilis与T. 海上氨酸杆切换器中的温度极端
Andrea Marton Menendez1, David J Nesbitt2
1JILA, University of Colorado Boulder and National Institute of Standards and Technology, Boulder, Colorado; Department of Chemistry, University of Colorado Boulder, Boulder, Colorado.
Biophysical journal
|August 2, 2024
概括
在不同的温度下生活的细菌使用类似的 lysine riboswitch 进行基因调节. 这些光环开关适应了它们的结构和动力学,显示了在各种热环境中对氨酸结合和折叠的保存机制.
科学领域:
- 分子生物学分子生物学
- 生物物理学的生物物理.
- 遗传学 是一个遗传学.
背景情况:
- 氨酸核糖开关调节细菌中的基因表达.
- 热友细菌,如T. maritima (~80°C) 和中友细菌,如B. subtilis (~40°C) 使用氨酸核转换器.
- 尽管热环境不同,但这些核糖体交换机在它们的aptamer域中具有结构上的相似性.
研究的目的:
- 调查来自T. maritima和B. subtilis.的氨酸 рибо开关的动力学和热力学适应.
- 为了了解这些带状交换机在极端热环境中如何工作.
- 为了比较联结和形状变化机制.
主要方法:
- 单分子光共振能量转移 (smFRET) 分析.
- 测量折叠和展开速度的动力学研究.
- 取决于温度的范特霍夫和艾灵分析以确定热力学参数.
主要成果:
- 这两种 рибо开关都通过一种诱导适合机制 (bind-then-fold) 结合氨酸.
- 热力学景观显示了对氨酸结合状态的热偏好,热处罚的过渡.
- 折叠/展开速度是相似的,当外推到各自的环境温度 (40°C和80°C).
结论:
- 来自不同热环境的 lysine riboswitch 采用了一种对连接体结合和形状变化的保存机制.
- 基配对和三级结构的适应允许在高热性和中热性条件下实现生物能力.
- 这表明,在多种不同的热中,杆开关功能具有共同的进化策略.
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