Orelle Cédric, Schmitt Lutz, Jault Jean-Michel
University of Lyon, CNRS, UMR5086 'Molecular Microbiology and Structural Biochemistry', IBCP, 7 Passage du Vercors, F-69367, Lyon, France.
Institute of Biochemistry, Heinrich Heine University, Universitätsstrasse 1, 40225 Düsseldorf, Germany.
Trends Microbiol. 2023 Mar;31(3):233-241. doi: 10.1016/j.tim.2022.09.005. Epub 2022 Sep 30.
Microorganisms need to constantly exchange with their habitat to capture nutrients and expel toxic compounds. The ATP-binding cassette (ABC) transporters, a family of membrane proteins especially abundant in microorganisms, are at the core of these processes. Due to their extraordinary ability to expel structurally unrelated compounds, some transporters play a protective role in different organisms. Yet, the downside of these multidrug transporters is their entanglement in the resistance to therapeutic treatments. Intriguingly, some multidrug ABC transporters show a high level of ATPase activity, even in the absence of transported substrates. Although this basal ATPase activity might seem a waste, we surmise that this inherent capacity allows multidrug transporters to promptly translocate any bound drug before it penetrates into the cell.
微生物需要不断与它们的生存环境进行物质交换，以获取营养并排出有毒化合物。ATP结合盒（ABC）转运蛋白是一类在微生物中特别丰富的膜蛋白家族，处于这些过程的核心位置。由于它们具有排出结构不相关化合物的非凡能力，一些转运蛋白在不同生物体中发挥着保护作用。然而，这些多药转运蛋白的缺点是它们与对治疗的耐药性有关。有趣的是，一些多药ABC转运蛋白即使在没有转运底物的情况下也表现出高水平的ATP酶活性。尽管这种基础ATP酶活性看似是一种浪费，但我们推测这种内在能力使多药转运蛋白能够在任何结合的药物渗入细胞之前迅速将其转运出去。
