Oosawa K, Hess J F, Simon M I
Division of Biology, California Institute of Technology, Pasadena 91125.
Cell. 1988 Apr 8;53(1):89-96. doi: 10.1016/0092-8674(88)90490-4.
To examine the correlation between CheA phosphorylation and bacterial chemotaxis, cheA mutations leading to defects in chemotaxis were mapped and characterized. Mutant CheA proteins were tested in vitro for phosphorylation and were grouped into four classes: nonphosphorylated, partially phosphorylated, phosphorylated but not dephosphorylated by CheB and CheY, and phosphorylated and dephosphorylated. Nearly all the mutants were found to be defective in an aspect of phosphorylation. Furthermore, the mutant phenotypes were found to cluster in different regions of the cheA gene. We suggest that the CheA protein has three functional domains: one for interaction with CheB and CheY, a second for regulating phosphorylation and controlling the stability of the protein, and a third for receiving input signals regulating CheA activity.
为了研究CheA磷酸化与细菌趋化性之间的相关性，对导致趋化性缺陷的cheA突变进行了定位和表征。在体外测试突变型CheA蛋白的磷酸化情况，并将其分为四类：未磷酸化、部分磷酸化、被CheB和CheY磷酸化但未去磷酸化、以及磷酸化且去磷酸化。几乎所有突变体在磷酸化方面都存在缺陷。此外，发现突变体表型聚集在cheA基因的不同区域。我们认为CheA蛋白有三个功能结构域：一个用于与CheB和CheY相互作用，第二个用于调节磷酸化并控制蛋白质的稳定性，第三个用于接收调节CheA活性的输入信号。
