Selected Publications Highlighting Brennan Laboratory Research
Schumacher, M.A.*, Balani, P.; Min, J., Chinnam, N.b., Hansen, S., Vulic, M., Lewis,K.*, Brennan R.G.* (*co-corresponding authors). HipBA-promoter structures reveal the basis of heritable multidrug tolerance. Nature (2015) Cuthbert, B. J., Brennan R.G.* and Schumacher, M.A.* (*co-corresponding authors). Structural and biochemical characterization of the Francisella tularensis pathogenicity regulator, macrophage locus protein A (MglA). PloS One (2015) Schindler, B.D., Seo, S.M., Birukou,I., Brennan, R.G., Kaatz, G.W. Mutations Within the mepA Operator Affect Binding of the MepR Regulatory Protein and its Induction by MepA Substrates in Staphylococcus aureus. J. Bacteriol. (2015) Reniere, M., Whiteley, A.T., Hamilton, K.L., John, S., Lauer, P., Brennan R.G. , Portnoy, D.A. Glutathione activates virulence gene expression of an intracellular pathogen. Nature (2015). Tschowri, N, Schumacher, M.A., Schlimpert, S., Chinnam, N.b., Findlay, K., Brennan R.G. and Buttner, M. Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development. Cell (2014). Kovach, A.R., Hoff, K.E., Canty, J.T., Orans, J. and Brennan R.G. Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes. RNA, (2014). Birukou, I., Seo, S. M., Kaatz, G.W. and Brennan R.G. . Structural mechanism of transcription regulation of the Staphylococcus aureus multidrug efflux operon mepRA by the MarR family repressor MepR. Nucleic Acids Res., (2014). Robinson K.E., Orans J., Kovach A.R., Link T.M., Brennan RG . Mapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenching. Nucleic Acids Res., (2014). Birukou I., Tonthat N.K., Seo S.M., Schindler B.D., Kaatz G.W., Brennan R.G. . The molecular mechanisms of allosteric mutations impairing MepR repressor function in multidrug resistant strains of Staphylococcus aureus. mBio, (2013). Schindler, B.D., Seo, S.M., Jacinto, P.L., Kumaraswami, M., Brennan, R.G. and Kaatz, G.W. Functional Consequences of Substitution Mutations in MepR, a Repressor of the Staphylococcus aureus MepA Multidrug Efflux Pump Gene. J. Bacteriol., (2013). Rajagopalan, S., Teeter, S., Brennan, R.G., Philips, K. and Kiley, P. Studies of IscR indicate a novel mechanism for metal-dependent regulation of DNA binding specificity. Nat. Struct. Mol. Biol., (2013). Xie, T.-X., Zhou, G., Zhao, M., Sano, D., Jasser, S.A., Brennan, R.G. and Myers, J.N.M. Serine substitution of Proline at Codon 151 of TP53 Confers Gain of Function Activity Leading to Anoikis Resistance and Tumor Progression of Head and Neck Cancer Cells. The Laryngoscope, (2013). Schumacher, M.A.*, Min, J., Link, T.M., Xu, W., Ahn, Y.-H., Kurie, J.M., Evdokimov, A., Lewis, K. and Brennan, R.G*. (*co-corresponding authors). Role of unusual P-loop ejection and autophosphorylation in HipA-mediated persistence and multidrug tolerance. Cell Reports, (2012). Horstmann, N, Orans, J., Valentin-Hansen, P., Shelburne III, S.A. and Brennan, R.G. Structural mechanism of Staphylococcus aureus Hfq binding to an RNA A-tract. Nucleic Acids Res. (2012). Hansen, S., Vulic, M., Min, J., Yen, T.-J., Schumacher, M.A., Brennan, R.G. and Lewis K. Regulation of the Escherichia coli HipBA Toxin-Antitoxin System by Proteolysis. PLoS ONE 7: e39185.doi:10.1371/journal pone.0039185 (2012). Horstmann, N., Sahasrabhojane, P., Suber, B., Kumaraswami, M., Olsen R.J., Flores, A., Musser, J.M., Brennan, R.G. and Shelburne S.A., 3rd. Distinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesis. PLoS Pathog. 2011 Oct;7 (10):e1002311. Kumaraswami, M., Schuman, J.T., Seo, S.M., Kaatz, G.W. and Brennan, R.G. Structural and Biochemical Characterization of MepR, a Multidrug binding Transcription Regulator of the Staphylococcus aureus Multidrug Efflux Pump MepA. Nucleic Acids Res. 37:1211–1224 (2009). Schumacher, M.A.*, Piro, K.M., Xu, W., Hansen, S., Lewis, K., and Brennan, R.G.* (*co-corresponding authors) Molecular Mechanisms of HipA Mediated Multidrug Tolerance and its Neutralization by HipB. Science 323: 396-401 (2009). Newberry, K.J., Huffman, J.L., Miller, M.C., Vazquez-Laslop, Neyfakh, A.A., and Brennan, R.G. Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion. J. Biol. Chem. 283:26796-26804 (2008). Newberry, K.J., Fuangthong, M., Panmanee W., Mongkolsuk, S. and Brennan, R.G. Structural Mechanism of Organic Hydroperoxide Induction of the Transcription Regulator OhrR. Mol. Cell 128:652-664 (2007). Hong, M., Fuangthong, M., Helmann, J.D. and Brennan, R.G. Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol. Cell 20:131-141 (2005). Schumacher, M.A., Allen, G.S., Diel, M., Seidel, G., Hillen, W. and Brennan, R.G. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118:731-741 (2004). Schumacher, M.A., Miller, R.F., Møller, T., Valentin-Hansen, P. and Brennan, R.G. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex; a bacterial Sm-like protein. EMBO J. 21:3546-3556 (2002). Schumacher, M.A., Miller, M.C. and Brennan, R.G. Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein. EMBO J. 23:2923-2930 (2004). Schumacher, M.A., Miller, M.C., Grkovic, S, Brown, M.H., Skurray, R.A. and Brennan, R.G. Structural Mechanisms of QacR Induction and Multidrug Recognition. Science 294:2158-2163 (2001). Zheleznova Heldwein, E.E. and Brennan, R.G. Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409:378-382 (2001). Zheleznova, E.E., Markham, P.N., Neyfakh, A.A. and Brennan, R.G. Structural Basis of Multidrug Recognition by BmrR, a Transcription Activator of a Multidrug Transporter. Cell 96:353-362 (1999). Schumacher, M.A., Choi, K.Y., Zalkin, H. and Brennan, R.G. Crystal Structure of the LacI Member, PurR, Bound to DNA: Minor Groove Binding by a-Helices. Science 266:763-770 (1994).