Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases.
Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases.
复制标题
细菌周质通透酶属于从大肠杆菌到人类的转运蛋白家族：交通ATP酶。
DOI：
10.1111/j.1574-6968.1990.tb04110.x
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发表时间：
1990
影响因子：
11.3
通讯作者：
Shyamala,V
中科院分区：
文献类型：
--
作者：
Ames,GF;Mimura,CS;Shyamala,V
细菌周质转运系统是复杂的渗透酶，由可溶性底物结合受体和含有 2-4 个蛋白质的膜结合复合物组成。最近的进展清楚地表明这些通透酶是通过 ATP 的水解来激发能量的。一些体外系统已经可以对这些渗透酶中起作用的基本参数进行详细研究。几种全能蛋白已被证明可以相互作用，并且运输过程的实际底物已被证明是配体的可溶性受体。该底物对膜复合物的亲和力约为 10 μM。 ATP 参与能量耦合是由膜复合物中的一种蛋白质介导的。对于每种特定的通透酶，该蛋白质是结合 ATP 的保守蛋白质家族的成员。该家族成员之间的相似性很高，并且超出了 ATP 结合的共有基序。有趣的是，在过去的几年中，已经发现了几种真核膜结合蛋白，它们与细菌周质通透酶的保守成分家族具有高度的同源性。大多数这些蛋白质已知或可以推断参与转运过程，例如多药耐药蛋白（MDR）、酵母的STE6基因产物以及可能的囊性纤维化蛋白。这种同源性表明作用机制相似，并且可能具有共同的进化起源。这一令人兴奋的发展将通过使用重叠程序和模型构建来刺激原核和真核研究领域的进展。我们建议将这种通用的渗透酶称为“交通ATP酶”，以将它们与其他类型的运输系统区分开来，并强调它们参与相对于细胞内部的任一方向的多种底物的运输以及它们使用ATP作为能量来源。
Bacterial periplasmic transport systems are complex permeases composed of a soluble substrate-binding receptor and a membrane-bound complex containing 2–4 proteins. Recent developments have clearly demonstrated that these permeases are energized by the hydrolysis of ATP. Several in vitro systems have allowed a detailed study of the essential parameters functioning in these permeases. Several of the compotent proteins have been shown to interact with each other and the actual substrate for the transport process has been shown to be the liganded soluble receptor. The affinity of this substrate for the membrane complex is approximately 10 μM. The involvement of ATP in energy coupling is mediated by one of the proteins in the membrane complex. For each specific permease, this protein is a member of a family of conserved proteins which bind ATP. The similarity between the members of this family is high and extends itself beyond the consensus motifs for ATP binding.Interestingly, over the last few years, several eukaryotic membrane-bound proteins have been discovered which bear a high level of homology to the family of the conserved components of bacterial periplasmic permeases. Most of these proteins are known to, or can be inferred to participate in a transport process, such as in the case of the multidrug resistance protein (MDR), theSTE6gene product of yeast, and possibly the cystic fibrosis protein. This homology suggests a similarity in the mechanism of action and possibly a common evolutionary origin. This exciting deveplopment will stimulate progress in both the prokaryotic and eukaryotic areas of research by the use of overlapping procedures and model building. We propose that this universal class of permeases be called ‘Traffic ATPases’ to distinguish them from other types of transport systems, and to highlight their involvement in the transport of a vast variety of substrate in either direction relative to the cell interior and their use of ATP as energy source.