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首页> 外文期刊>Journal of bacteriology >Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transducer of Escherichia coli.
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Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transducer of Escherichia coli.

机译：天冬氨酸和麦芽糖结合蛋白与大肠杆菌的焦油趋化信号转导子中的相邻位点相互作用。

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摘要

The Tar protein of Escherichia coli is a chemotactic signal transducer that spans the cytoplasmic membrane and mediates responses to the attractants aspartate and maltose. Aspartate binds directly to Tar, whereas maltose binds to the periplasmic maltose-binding protein, which then interacts with Tar. The Arg-64, Arg-69, and Arg-73 residues of Tar have previously been shown to be involved in aspartate sensing. When lysine residues are introduced at these positions by site-directed mutagenesis, aspartate taxis is disrupted most by substitution at position 64, and maltose taxis is disrupted most by substitution at position 73. To explore the spatial distribution of ligand recognition sites on Tar further, we performed doped-primer mutagenesis in selected regions of the tar gene. A number of mutations that interfere specifically with aspartate taxis (Asp-), maltose taxis (Mal-), or both were identified. Mutations affecting residues 64 to 73 or 149 to 154 in the periplasmic domain of Tar are associated with an Asp- phenotype, whereas mutations affecting residues 73 to 83 or 141 to 150 are associated with a Mal- phenotype. We conclude that aspartate and maltose-binding protein interact with adjacent and partially overlapping regions in the periplasmic domain of Tar to initiate attractant signalling.
机译：大肠杆菌的焦油蛋白是一种趋化信号转导子，横跨细胞质膜并介导对天冬氨酸和麦芽糖引诱剂的反应。天冬氨酸直接与焦油结合，而麦芽糖与周质麦芽糖结合蛋白结合，然后与焦油相互作用。 Tar的Arg-64，Arg-69和Arg-73残基先前已显示参与天冬氨酸感测。当通过定点诱变将赖氨酸残基引入这些位置时，天冬氨酸的出租车在64位被取代破坏最大，麦芽糖的出租车在73位被取代破坏最大。为进一步研究Tar上配体识别位点的空间分布，我们在tar基因的选定区域进行了掺杂引物诱变。鉴定了许多特异性干扰天冬氨酸（Asp-），麦芽糖（Mal-）或两者的突变。影响Tar周质结构域中残基64至73或149至154的突变与Asp表型相关，而影响残基73至83或141至150的突变与Mal表型相关。我们得出的结论是，天冬氨酸和麦芽糖结合蛋白与焦油周质结构域中相邻和部分重叠的区域相互作用，从而引发引诱信号。

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