Receptor structure in the bacterial sensing system.
Receptor structure in the bacterial sensing system.
复制标题
细菌传感系统中的受体结构。
DOI：
10.1073/pnas.77.12.7157
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发表时间：
1980
影响因子：
11.1
通讯作者：
KoshlandJr,DE
中科院分区：
文献类型：
--
作者：
Wang,EA;KoshlandJr,DE
在细菌趋化过程中，天冬氨酸和丝氨酸的主要受体是由tar和tsr基因编码的60000道尔顿蛋白。证据是：(i)重组DNA技术在不同水平上过量生产焦油基因产物会导致天冬氨酸结合的比例增加；（ii）天冬氨酸结合与[3H]甲基标记的焦油基因产物相结合；（iii）针对tar和tsr蛋白片段的抗体沉淀出一种单种蛋白（60,000道尔顿），保留了结合能力和[3H]羧甲基标签。部分纯化的焦油基因产物可以重组成人工囊泡，并保留天冬氨酸结合和天冬氨酸敏感的甲基化和去甲基化。这些结果表明，天冬氨酸和丝氨酸受体是单多肽链的跨膜蛋白，受体识别位点在膜外，共价甲基化位点在膜内。
The primary receptors for aspartate and serine in bacterial chemotaxis have been shown to be the 60,000-dalton proteins encoded by the tar and tsr genes. The evidence is: (i) overproduction of the tar gene product at various levels by recombinant DNA techniques produces proportionate increases in aspartate binding; (ii) aspartate binding copurifies with [3H]methyl-labeled tar gene product; (iii) antibody to tar and tsr protein fragments precipitates a single species of protein (60,000 daltons) which retains binding capacity and [3H]carboxymethyl label. Partially purified tar gene product can be reconstituted into artificial vesicles and retains aspartate binding and aspartate-sensitive methylation and demethylation. These results show that the aspartate and serine receptors are transmembrane proteins of a single polypeptide chain with the receptor recognition site on the outside of the membrane and the covalent methylation site on the inside.