COMPUTER-SIMULATION OF THE PHOSPHORYLATION CASCADE CONTROLLING BACTERIAL CHEMOTAXIS
COMPUTER-SIMULATION OF THE PHOSPHORYLATION CASCADE CONTROLLING BACTERIAL CHEMOTAXIS
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DOI：
10.1091/mbc.4.5.469
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发表时间：
1993-05-01
影响因子：
3.3
通讯作者：
SIMON, MI
中科院分区：
文献类型：
--
作者：
BRAY, D;BOURRET, RB;SIMON, MI
我们已经开发了一个计算机程序，模拟介导的快速（非适应性）大肠杆菌细菌的趋化反应的细胞内反应的引诱剂天冬氨酸和排斥Ni 2+离子。该模型由代表所涉及的分子组分的模块化单元构建，在可能的情况下，每个模块化单元被分配一个已知的细胞内浓度和酶促速率常数值。这些成分被连接成一个耦合的生化反应网络，该网络基于广泛接受的机制的汇编，但包含几个新的功能。计算机马达显示出与实际细菌相同的运行，翻滚和暂停模式，并以与活细菌相同的方式对天冬氨酸或Ni 2+浓度的突然变化做出反应。模拟的网络准确地再现了30多个突变体的表型，其中趋化途径的组分被删除和/或过量表达，并显示出对天冬氨酸浓度阶跃变化的快速响应，类似于活细菌。模拟和真实的细菌在某些突变体的表型和对天冬氨酸的趋化反应的增益之间的差异表明在体内信号处理途径中存在另外的尚未确定的相互作用。
We have developed a computer program that simulates the intracellular reactions mediating the rapid (nonadaptive) chemotactic response of Escherichia coli bacteria to the attractant aspartate and the repellent Ni2+ ions. The model is built from modular units representing the molecular components involved, which are each assigned a known value of intracellular concentration and enzymatic rate constant wherever possible. The components are linked into a network of coupled biochemical reactions based on a compilation of widely accepted mechanisms but incorporating several novel features. The computer motor shows the same pattern of runs, tumbles and pauses seen in actual bacteria and responds in the same way as living bacteria to sudden changes in concentration of aspartate or Ni2+. The simulated network accurately reproduces the phenotype of more than 30 mutants in which components of the chemotactic pathway are deleted and/or expressed in excess amounts and shows a rapidity of response to a step change in aspartate concentration similar to living bacteria. Discrepancies between the simulation and real bacteria in the phenotype of certain mutants and in the gain of the chemotactic response to aspartate suggest the existence of additional as yet unidentified interactions in the in vivo signal processing pathway.