tailieunhanh - Báo cáo khoa học: A differential scanning calorimetry study of tetracycline repressor

Tetracycline repressor (TetR), which constitutes the most commonmechanismof bacterial resistance to an antibiotic, is a homodimeric protein composed of two identical sub-units, each of which contains a domain possessing a helix– turn–helix motif and a domain responsible for binding tetra-cycline. Binding of tetracycline in the protein pocket is accompanied by conformational changes in TetR, which abolish the specific interaction between the protein and DNA. | Eur. J. Biochem. 270 4564-4573 2003 FEBS 2003 doi A differential scanning calorimetry study of tetracycline repressor Sylwia Kẹdracka-Krok and Zygmunt Wasylewski Department of Physical Biochemistry Faculty of Biotechnology Jagiellonian University Krakow Poland Tetracycline repressor TetR which constitutes the most common mechanism of bacterial resistance to an antibiotic is a homodimeric protein composed of two identical subunits each of which contains a domain possessing a helixturn-helix motif and a domain responsible for binding tetracycline. Binding of tetracycline in the protein pocket is accompanied by conformational changes in TetR which abolish the specific interaction between the protein and DNA. Differential scanning calorimetry DSC and CD measurements performed at pH were used to observe the thermal denaturation of TetR in the absence and presence of tetracycline. The DSC results show that in the absence of tetracycline the thermally induced transitions of TetR can be described as an irreversible process strongly dependent on scan rate and indicating that the protein denaturation is under kinetic control described by the simple kinetic scheme N2 - D2 where k is a first-order kinetic constant N is the native state and D is the denatured state. On the other hand analysis of the scan rate effect on the transitions of TetR in the presence of tetracycline shows that thermal unfolding of the protein can be described by the two-state model N2 U2 D. In the proposed model TetR in the presence of tetracycline undergoes co-operative unfolding characterized by an enthalpy change AHcil 1067 kJ-mol-1 and an entropy change AS kJ-mol-1 . Keywords circular dichroism differential scanning calorimetry tetracycline repressor tetracycline thermal denaturation. Resistance to tetracycline Tc which is the most common form of antibiotic resistance in Gram-negative bacteria is based on the activation of the drug efflux through the .

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