influence of quaternary cation compound on the size of the escherichia coli small multidrug resistance protein, emre

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ID: 215634
2018
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Abstract
EmrE is a member of the small multidrug resistance (SMR) protein family in Escherichia coli. It confers resistance to a wide variety of quaternary cation compounds (QCCs) as an efflux transporter driven by the transmembrane proton motive force. We have expressed hexahistidinyl (His6) – myc epitope tagged EmrE, extracted it from membrane preparations using the detergent n-dodecyl-β-D-maltopyranoside (DDM), and purified it using nickel-affinity chromatography. The size of the EmrE protein, in DDM environment, was then examined in the presence and absence of a range of structurally different QCC ligands that varied in their chemical structure, charge and shape. We used dynamic light scattering and showed that the size and oligomeric state distributions are dependent on the type of QCC. We also followed changes in the Trp fluorescence and determined apparent dissociation constants (Kd). Overall, our in vitro analyses of epitope tagged EmrE demonstrated subtle but significant differences in the size distributions with different QCC ligands bound. Keywords: Small multidrug resistance (SMR) protein, EmrE, Integral membrane protein folding, Quaternary ammonium compounds (QAC), Quaternary cation compounds (QCC), Ligand binding, Hexahistidine (His6) tag, Structural plasticity, Dynamic light scattering
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qazi2018biochemistryinfluence Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;S. Junaid S. Qazi;Raymond J. Turner
Journal addictive behaviors reports
Year 2018
DOI
DOI not found
URL
http://www.sciencedirect.com/science/article/pii/S2405580818300293
Keywords
biology (general)biochemistry

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