Hunke S, Döse S, Schneider E
Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, Institut für Biologie, Germany.
Biochem Biophys Res Commun. 1995 Nov 13;216(2):589-94. doi: 10.1006/bbrc.1995.2663.
Vanadate and Bafilomycin A1 were shown to inhibit the ATPase activity of the reconstituted binding protein-dependent ATP-binding Cassette (ABC) transporter for maltose (MalFGK2) of Salmonella typhimurium in the micromolar range. This is in sharp contrast to the recent finding that the isolated ATPase subunit MalK was insensitive to both compounds. Our data provide the first experimental evidence for the view that functional coupling of the ATPase domain of an ABC transporter to the membrane-integral domains is crucial for conferring sensitivity to vanadate and bafilomycin A1. Possible consequences for the mode of action of ABC transport proteins are discussed.
已证明钒酸盐和巴弗洛霉素A1在微摩尔范围内可抑制鼠伤寒沙门氏菌麦芽糖（MalFGK2）重组结合蛋白依赖性ATP结合盒（ABC）转运蛋白的ATP酶活性。这与最近发现的分离的ATP酶亚基MalK对这两种化合物均不敏感形成鲜明对比。我们的数据为以下观点提供了首个实验证据：ABC转运蛋白的ATP酶结构域与膜整合结构域的功能偶联对于赋予对钒酸盐和巴弗洛霉素A1的敏感性至关重要。文中还讨论了ABC转运蛋白作用模式可能产生的后果。
