(Q46378444)

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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

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

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 (English)

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

María-Trinidad Gallegos

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

Juan Luis Ramos Martín

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

María-Eugenia Guazzaroni

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María-Eugenia Guazzaroni

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Antonia Felipe

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

Raquel Ruiz

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

Cuixiang Meng

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21 December 2017

http://europepmc.org/abstract/MED/15767250

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13 March 2005

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21 December 2017

http://europepmc.org/abstract/MED/15767250

Journal of Biological Chemistry

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21 December 2017

http://europepmc.org/abstract/MED/15767250

280

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21 December 2017

http://europepmc.org/abstract/MED/15767250

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21 December 2017

http://europepmc.org/abstract/MED/15767250

20887-20893

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Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

Mechanisms of solvent tolerance in gram-negative bacteria

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Isolation and expansion of the catabolic potential of a Pseudomonas putida strain able to grow in the presence of high concentrations of aromatic hydrocarbons

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Multidrug efflux pumps of gram-negative bacteria

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Solvent-exposed residues in the Tet repressor (TetR) four-helix bundle contribute to subunit recognition and dimer stability.

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Three efflux pumps are required to provide efficient tolerance to toluene in Pseudomonas putida DOT-T1E

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Biotransformation in double-phase systems: physiological responses of Pseudomonas putida DOT-T1E to a double phase made of aliphatic alcohols and biosynthesis of substituted catechols

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21 January 2018

In vivo and in vitro evidence that TtgV is the specific regulator of the TtgGHI multidrug and solvent efflux pump of Pseudomonas putida.

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21 January 2018

TtgV bound to a complex operator site represses transcription of the promoter for the multidrug and solvent extrusion TtgGHI pump.

1 reference

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21 January 2018

Expression of the TOL plasmid xylS gene in Pseudomonas putida occurs from a alpha 70-dependent promoter or from alpha 70- and alpha 54-dependent tandem promoters according to the compound used for growth

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21 January 2018

Antibiotic-dependent induction of Pseudomonas putida DOT-T1E TtgABC efflux pump is mediated by the drug binding repressor TtgR.

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21 January 2018

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

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21 January 2018

The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers.

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21 January 2018

Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization

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Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein

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Structural mechanisms of QacR induction and multidrug recognition

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Effects exerted by transcriptional regulator PcaU from Acinetobacter sp. strain ADP1.

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QacR is a repressor protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA.

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Crystal structure of the transcription activator BmrR bound to DNA and a drug

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Gene regulation by tetracyclines. Constraints of resistance regulation in bacteria shape TetR for application in eukaryotes

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Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance

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Characterization of the role of side-chain interactions in the binding of ligands to apo trp repressor: pH dependence studies.

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Interactions of the QacR multidrug-binding protein with structurally diverse ligands: implications for the evolution of the binding pocket.

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Fatty acyl-CoA binding domain of the transcription factor FadR. Characterization by deletion, affinity labeling, and isothermal titration calorimetry

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21 January 2018

Identifiers

10.1074/JBC.M500783200

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

1 reference

Europe PubMed Central

21 December 2017

http://europepmc.org/abstract/MED/15767250

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