ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance.
ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance.
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DOI：
10.1146/annurev.mi.47.100193.001451
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发表时间：
1993
影响因子：
10.5
通讯作者：
C. A. Doige;G. Ames
中科院分区：
文献类型：
--
作者：
C. A. Doige;G. Ames
原核生物的渗透酶是一个被称为交通ATP酶的膜转运蛋白超家族的成员，其包括医学上重要的真核多药耐药（MDR）蛋白和囊性纤维化跨膜调节因子（CFTR）。该超家族的成员具有广泛的序列和结构相似性，特别是在ATP结合基序中，并且被认为使用ATP来激发底物跨生物膜的易位。原核组氨酸通透酶是一个很好的特点，并作为一个方便的模型系统。在这篇综述中，我们强调了一些生物化学和分子生物学的方法来研究这种通透酶的功能和结构组织，并与这些方法的结果是什么是已知的其他交通ATP酶。我们已经确定了我们认为对组氨酸通透酶的功能至关重要的特定区域，并提出真核交通ATP酶中的相应区域对其功能也很重要。鉴于CFTR（可能还有MDR蛋白）是一种离子通道的事实，我们比较了通道和转运蛋白的性质;此外，我们还讨论了交通ATP酶的其他成员也可能具有通道样活性的可能性。
The prokaryotic permeases are members of a superfamily of membrane transporters called traffic ATPases, which includes the medically important eukaryotic multidrug resistance (MDR) protein and cystic fibrosis transmembrane regulator (CFTR). Members of this superfamily have extensive sequence and structural similarity, in particular in an ATP-binding motif, and are believed to use ATP to energize translocation of substrates across biological membranes. The prokaryotic histidine permease is well-characterized and serves as a convenient model system. In this review, we highlight some of the biochemical and molecular biological approaches used to study the functional and architectural organization of this permease and relate the results of these approaches to what is known about other traffic ATPases. We have identified specific regions that we believe critical for the function of the histidine permease and propose that the corresponding regions in the eukaryotic traffic ATPases are also important for their function. In light of the fact that CFTR (and possibly the MDR protein) is an ion channel, we compare the properties of channels and transporters; in addition, we discuss the possibility that other members of the traffic ATPases may also have channel-like activity.