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Items: 1 to 20 of 95


A single acidic residue can guide binding site selection but does not govern QacR cationic-drug affinity.

Peters KM, Brooks BE, Schumacher MA, Skurray RA, Brennan RG, Brown MH.

PLoS One. 2011 Jan 17;6(1):e15974. doi: 10.1371/journal.pone.0015974.


Biochemical characterization of the multidrug regulator QacR distinguishes residues that are crucial to multidrug binding and induction of qacA transcription.

Peters KM, Sharbeen G, Theis T, Skurray RA, Brown MH.

Biochemistry. 2009 Oct 20;48(41):9794-800. doi: 10.1021/bi901102h.


QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization.

Peters KM, Schuman JT, Skurray RA, Brown MH, Brennan RG, Schumacher MA.

Biochemistry. 2008 Aug 5;47(31):8122-9. doi: 10.1021/bi8008246. Epub 2008 Jul 11.


Multidrug-binding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions.

Brooks BE, Piro KM, Brennan RG.

J Am Chem Soc. 2007 Jul 4;129(26):8389-95. Epub 2007 Jun 13.


Structural mechanisms of QacR induction and multidrug recognition.

Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG.

Science. 2001 Dec 7;294(5549):2158-63.


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

Schumacher MA, Miller MC, Brennan RG.

EMBO J. 2004 Aug 4;23(15):2923-30. Epub 2004 Jul 15.


Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR.

Schumacher MA, Miller MC, Grkovic S, Brown MH, Skurray RA, Brennan RG.

EMBO J. 2002 Mar 1;21(5):1210-8. Erratum in: EMBO J 2002 May 1;21(9):2301.


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

Grkovic S, Brown MH, Schumacher MA, Brennan RG, Skurray RA.

J Bacteriol. 2001 Dec;183(24):7102-9.


Staphylococcal multidrug efflux protein QacA.

Brown MH, Skurray RA.

J Mol Microbiol Biotechnol. 2001 Apr;3(2):163-70. Review.


Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion.

Newberry KJ, Huffman JL, Miller MC, Vazquez-Laslop N, Neyfakh AA, Brennan RG.

J Biol Chem. 2008 Sep 26;283(39):26795-804. doi: 10.1074/jbc.M804191200. Epub 2008 Jul 25.


The molecular mechanisms of allosteric mutations impairing MepR repressor function in multidrug-resistant strains of Staphylococcus aureus.

Birukou I, Tonthat NK, Seo SM, Schindler BD, Kaatz GW, Brennan RG.

MBio. 2013 Aug 27;4(5):e00528-13. doi: 10.1128/mBio.00528-13.


Subdividing repressor function: DNA binding affinity, selectivity, and allostery can be altered by amino acid substitution of nonconserved residues in a LacI/GalR homologue.

Zhan H, Taraban M, Trewhella J, Swint-Kruse L.

Biochemistry. 2008 Aug 5;47(31):8058-69. doi: 10.1021/bi800443k. Epub 2008 Jul 11.


Functional impact of polar and acidic substitutions in the lactose repressor hydrophobic monomer.monomer interface with a buried lysine.

Zhan H, Sun Z, Matthews KS.

Biochemistry. 2009 Feb 17;48(6):1305-14. doi: 10.1021/bi801357f.


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

Grkovic S, Brown MH, Roberts NJ, Paulsen IT, Skurray RA.

J Biol Chem. 1998 Jul 17;273(29):18665-73.


Structural and functional analysis of SmeT, the repressor of the Stenotrophomonas maltophilia multidrug efflux pump SmeDEF.

Hernández A, Maté MJ, Sánchez-Díaz PC, Romero A, Rojo F, Martínez JL.

J Biol Chem. 2009 May 22;284(21):14428-38. doi: 10.1074/jbc.M809221200. Epub 2009 Mar 26.


Transcriptional repression mediated by a TetR family protein, PfmR, from Thermus thermophilus HB8.

Agari Y, Sakamoto K, Kuramitsu S, Shinkai A.

J Bacteriol. 2012 Sep;194(17):4630-41. doi: 10.1128/JB.00668-12. Epub 2012 Jun 29.

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