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The ABC transporter MalFGK 2 sequesters the MalT transcription factor at the membrane in the absence of cognate substrate
Author(s) -
Richet Evelyne,
Davidson Amy L.,
Joly Nicolas
Publication year - 2012
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2012.08137.x
Subject(s) - regulon , maltose , transporter , biology , biochemistry , atp binding cassette transporter , efflux , glucose transporter , transcription factor , microbiology and biotechnology , gene , enzyme , insulin , endocrinology
Summary MalK, the cytoplasmic component of the maltose ABC transporter from Escherichia coli is known to control negatively the activity of MalT, the activator of the maltose regulon, through complex formation. Here we further investigate this regulatory process by monitoring MalT activity and performing fluorescence microscopy analyses under various conditions. We establish that, under physiological conditions, the molecular entity that interacts with MalT is not free MalK, but the maltose transporter, MalFGK 2 , which sequesters MalT to the membrane. Furthermore, we provide compelling evidence that the transporter's ability to bind MalT is not constitutive, but strongly diminished when MalFGK 2 is engaged in sugar transport. Notably, the outward‐facing transporter, i.e. the catalytic intermediate, is ineffective in inhibiting MalT compared to the inward‐facing state, i.e. the resting form. Analyses of available genetic and structural data suggest how the interaction between one inactive MalT molecule and MalFGK 2 would be sensitive to the transporter state, thereby allowing MalT release upon maltose entrance. A related mechanism may underpin signalling by other ABC transporters.