Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli.
Identification of the structural proteins of an ATP-driven potassium transport system in Escherichia coli.
复制标题
大肠杆菌中 ATP 驱动的钾转运系统结构蛋白的鉴定。
DOI：
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发表时间：
1978
影响因子：
11.1
通讯作者：
W. Epstein
中科院分区：
文献类型：
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作者：
L. Laimins;David B. Rhoads;Karlheinz Altendorf;W. Epstein
大肠杆菌 ATP 驱动的 Kdp 钾转运系统的三种结构蛋白 [Rhoads, D. B., Waters, F. B. & Epstein, W. (1976) J. Gen. Physiol. 67, 325-341]已被鉴定并发现位于内膜中。大肠杆菌四个钾转运系统之一中的高亲和力可抑制 Kdp 系统。 Kdp 蛋白在生长的细胞以及被携带 kdp 操纵子的转导噬菌体感染的重度紫外线照射的细胞中都被鉴定出来。尽管之前发现的所有革兰氏阴性细菌的 ATP 驱动转运系统均已显示含有周质蛋白成分，但没有发现此类成分或 Kdp 系统外膜成分的证据。三种内膜蛋白KdpA、KdpB和KdpC的分子量分别测定为47,000、90,000和22,000。
The three structural proteins of the ATP-driven Kdp potassium transport system of Escherichia coli [Rhoads, D. B., Waters, F. B. & Epstein, W. (1976) J. Gen. Physiol. 67, 325-341] have been identified and found to be located in the inner membrane. The high-affinity repressible Kdp system in one of four potassium transport systems in E. coli. The Kdp proteins were identified both in growing cells as well as in heavily UV-irradiated cells infected with transducing phages carrying the kdp operon. Although all previously identified ATP-driven transport systems of Gram-negative bacteria have been shown to contain a periplasmic protein component, no evidence was found for such a component or for an outer membrane component of the Kdp system. The molecular weights of the three inner membrane proteins, KdpA, KdpB, and KdpC, were determined to be 47,000, 90,000 and 22,000, respectively.