Proton-dependent multidrug efflux systems.
- I. Paulsen, M. Brown, R. Skurray
- BiologyMicrobiological reviews
- 1 December 1996
Whether the normal physiological role of the multidrug efflux systems is to protect the cell from toxic compounds or whether they fulfil primary functions unrelated to drug resistance and only efflux multiple drugs fortuitously or opportunistically is discussed.
Analysis of the sequence and gene products of the transfer region of the F sex factor.
- L. Frost, K. Ippen-Ihler, R. Skurray
- Biology, ChemistryMicrobiological reviews
- 1 June 1994
This review will concentrate on the genes required for bacterial conjugation that are encoded within the transfer region (or regions) of conjugative plasmids, which has been the paradigm for conjugations since it was discovered nearly 50 years ago.
Structural basis for cooperative DNA binding by two dimers of the multidrug‐binding protein QacR
- M. Schumacher, Marshall C. Miller, S. Grkovic, Melissa H. Brown, R. Skurray, R. Brennan
- Biology, ChemistryEMBO Journal
- 1 March 2002
The data reveal that the DNA recognition mode of QacR is distinct from TetR and involves the binding of a pair ofQacR dimers, and the inferred cooperativity does not arise from cross‐dimer protein–protein contacts, but from the global undertwisting and major groove widening elicited by thebinding of two Qac R dimers.
Regulation of Bacterial Drug Export Systems
- S. Grkovic, Melissa H. Brown, R. Skurray
- BiologyMicrobiology and Molecular Biology Reviews
- 1 December 2002
Many regulatory systems are ill-adapted for detecting the presence of toxic pump substrates and instead are likely to respond to alternative signals related to unidentified physiological roles of the transporter, resulting in regulatory mutations that result in drug transporter overexpression and concomitant elevated antimicrobial resistance.
Structural Mechanisms of QacR Induction and Multidrug Recognition
- M. Schumacher, Marshall C. Miller, S. Grkovic, Melissa H. Brown, R. Skurray, R. Brennan
- Biology, ChemistryScience
- 7 December 2001
The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we…
Multidrug resistance proteins QacA and QacB from Staphylococcus aureus: membrane topology and identification of residues involved in substrate specificity.
- I. Paulsen, M. Brown, T. Littlejohn, B. A. Mitchell, R. Skurray
- BiologyProceedings of the National Academy of Sciences…
- 16 April 1996
QacA represents the first membrane transport protein shown to contain 14 transmembrane segments, and confirms that the major facilitator superfamily contains a family of proteins with 14 trans Membranes segments.
The multidrug efflux protein NorM is a prototype of a new family of transporters
- Melissa H. Brown, I. Paulsen, R. Skurray
- BiologyMolecular Microbiology
- 1 January 1999
The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs
- I. Paulsen, R. Skurray, L. Grinius
- Biology, ChemistryMolecular Microbiology
- 1 March 1996
Hydropathy and residue distribution analyses of this family suggest a structural model in which the polypeptide chain spans the membrane four times as mildly amphipathic α‐helices, and a possible mechanistic model of drug efflux.
Antimicrobial resistance of Staphylococcus aureus: genetic basis.
- B. Lyon, R. Skurray
- Biology, MedicineMicrobiological reviews
- 1 March 1987
This work has shown clear trends in the emergence of multiresislant S. aureus-related resistance as well as in the development of novel mechanisms for this resistance.
QacR Is a Repressor Protein That Regulates Expression of theStaphylococcus aureus Multidrug Efflux Pump QacA*
- S. Grkovic, Melissa H. Brown, N. Roberts, I. Paulsen, R. Skurray
- BiologyJournal of Biological Chemistry
- 17 July 1998
Adding of diverse QacA substrates was shown to induce qacA expression in vivo, as well as inhibit binding of QacR to operator DNA in vitro, by using gel-mobility shift assays, which appears to interact directly with structurally dissimilar inducing compounds that are substrates of the Qac a multidrug efflux pump.
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