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Papers In Press, published online ahead of print March 13, 2005
J. Biol. Chem, 10.1074/jbc.M500783200
Submitted on January 21, 2005
Revised on March 13, 2005
Accepted on March 13, 2005

The multidrug efflux regulator TtgV recognizes a wide range of structurally different effectors in solution and complexed with target DNA. Evidence from isothermal titration calorimetry

Maria- Eugenia Guazzaroni, Tino Krell, Antonia Felipe, Raquel Ruíz, Cuixiang Meng, Xiaodong Zhang, Maria-Trinidad Gallegos, and Juan L. Ramos

Estacion Experimental del Zaidin, CSIC, Granada 18008

Corresponding Author: jlramos{at}eez.csic.es

TtgV modulates the expression of the ttgGHI operon, which encodes an efflux pump that extrudes a wide variety of chemicals including mono- and binuclear aromatic hydrocarbons, aliphatic alcohols and antibiotics of dissimilar chemical structure. Using a ‘lacZ fusion to the ttgG promoter, we show that the most efficient in vivo inducers were 1-naphthol, 2,3-dihydroxynaphthalene, 4-nitrotoluene, benzonitrile and indole. The thermodynamic parameters for the binding of different effector molecules to purified TtgV were determined by isothermal titration calorimetry. For the majority of effectors the interaction was enthalpy driven and counterbalances by unfavourable entropy changes. The TtgV-effector dissociation constants were found to vary between 2 and 890 mu M. There was a relationship between TtgV affinity for the different effectors and their potential to induce gene expression in vivo, indicating that the effector binding constant is a major determinant for efficient efflux pump gene expression. Equilibrium dialysis and isothermal titration calorimetry studies indicated that a TtgV dimer binds 1 effector molecule. No evidence for the simultaneous binding of multiple effectors to TtgV was obtained. The binding of TtgV to a 63 bp DNA fragment containing its cognate operator was tight and entropy driven (KD = 2.4 ± 0.35 nM, delta H=5.5 ± 0.04 kcal/mol). The TtgV-DNA complex was shown to bind 1-napthol with an affinity comparable to the free soluble TtgV protein, KD=4.8 ± 0.19 mu M and 3.0 ± 0.15 mu M, respectively. The biological relevance of this finding is discussed


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