Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases.
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 component 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 microM. 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), the STE6 gene 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 development 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 substrates in either direction relative to the cell interior and their use of ATP as energy source.
Ames
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GF
Division of Biochemistry and Molecular Biology, University of California, Berkeley 94720.
Mimura
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CS
Shyamala
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D000251:Adenosine Triphosphatases / Q000145:classification / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000145:classification / Q000378:metabolism*; D001693:Biological Transport, Active; D002352:Carrier Proteins / Q000145:classification / Q000502:physiology; D003550:Cystic Fibrosis / Q000378:metabolism; D004331:Drosophila melanogaster / Q000378:metabolism; D004352:Drug Resistance, Microbial; D004734:Energy Metabolism; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D000072235:Mating Factor; D008565:Membrane Proteins / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000145:classification / Q000502:physiology*; D008954:Models, Biological; D010455:Peptides / Q000378:metabolism; D010802:Phylogeny; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D013379:Substrate Specificity
D001426:Bacterial Proteins; D002352:Carrier Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D010455:Peptides; D000072235:Mating Factor; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases