The High-affinity K+-translocating ATPase Complex from Clostridium acetobutylicum Consists of Six Subunits |
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| Institution: | 1. Laboratoire ORSTOM de Microbiologie des Anaérobies, Université de Provence, CESB/ESILCase 925, 163 Avenue de Luminy, 13288, Marseille Cedex 09, France;2. School of Biomolecular and Biomedical Sciences, Faculty of Science and Technology, Griffith University, Nathan, Brisbane, 4111, Australia;3. Sanofi Recherche, Unité de Microbiologie, BP 137, 31676, Labège Cedex, France;1. Department of Biological Chemistry, UCLA School of Medicine, Los Angeles CA 90095-1737, USA;2. Molecular Biology Institute University of California Los Angeles, CA 90095, USA;1. Hässle Gastrointestinal Research laboratories, Department of Biology, Mölndal, Sweden;2. University of Oulu, Department of Anatomy, Kajaanintie, Finland |
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| Abstract: | The kdp operon of Clostridium acetobutylicum codes for the high affinity K+-translocating Kdp system (P-type ATPase). Beside the three large proteins KdpA, KdpB and KdpC, the kdp operon encodes the two small peptides KdpZ, KdpY and the KdpX protein. The truncation of the clostridial kdpZ and/or the kdpY gene has a significant impact on the growth of an E. coli mutant (TK2205), which is unable to grow at low potassium concentrations. These two genes together with kdpX are essential to maintain the wild-type K+-pump capacity of the clostridial Kdp system. Also the ATPase activity itself, the substrate specifity, and the cation specifity are determined in a major way by KdpZ, KdpY, and KdpX. Thus, this report shows the importance of the KdpZ, KdpY, and KdpX proteins for the Kdp-ATPase and therefore the corresponding operon should now be referred to as kdpZYABCX. |
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