Kuhn, Misty - San Francisco State University - Department of Chemistry and Biochemistry

个人简介

B.A. (2002), Hanover College Ph.D. (2009), Loyola University Chicago, Chemistry Postdoc (2010), Loyola University Chicago Postdoc (2010-2014), Northwestern University Medical School

研究领域

The overarching goal of our research is to elucidate functions of bacterial enzymes that belong to the large Gcn5-related N-acetyltransferase (GNAT) family. To accomplish this, we use a combination of enzymology, biophysical, and structural biology techniques. Enzymes from this family have diverse functions, which include acylation of a varitey of molecules such as polyamines, antibiotics, peptides, and proteins. These enzymes have been implicated in a vast array of cellular functions and represent a system that is ripe for discovering new insight into mechanisms of antibiotic and herbicide resistance, metabolic regulation, and disease progression. Since most bacterial GNATs remain uncharacterized or have undiscovered functions, there is much to be learned about this family of proteins. Our main focus in the laboratory is to delve deep into the underlying mechanisms of how a conserved structural architecture is used by nature to meticulously catalyze diverse reactions. To do this, we investigate the functions of GNATs from a variety of pathogenic and nonpathogenic bacteria, including Escherichia coli, Vibrio cholerae, Pseudomonas aeruginosa, Acinetobacter and Sinorhizobium meliloti. The hope is that our basic research will lay the foundation for a more in-depth understanding of this family of enzymes and their importance in bacterial metabolism and infectious diseases.

近期论文

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Majorek K.A., Osinski T., Tran D.T., Revilla A., Anderson W.F., Minor W., Kuhn M.L. (2017) Insight into the 3D structure and substrate specificity of previously uncharacterized GNAT superfamily acetyltransferases from pathogenic bacteria. Stogios P.J.*, Kuhn M.L.*, Evdokimova E., Law M., Courvalin P., and Savchenko A. (2016) Structural and biochemical characterization of the Acinetobacter aminoglycoside acetyltransferases AAC(6’)-Ig and AAC(6’)-Ih highlights dramatic functional variety among resistance-conferring enzymes. Kuhn M.L., Alexander E.M., Minasov G., Page H.J., Wawrzak Z., Shuvalova L., Flores K.J., Wilson D.J., Shi C., Aldrich C.C., and Anderson W.F. (2016) Structure of the essential Mtb FadD32 enzyme: a promising drug target for treating tuberculosis. ACS Infect. Filippova E.V.*, Kuhn M.L.*, Osipiuk J., Kiryukhina O., Joachimiak A., Ballicora M.A., and Anderson W.F. (2015) A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed by its dodecameric structure. AbouElfetouh A.*, Kuhn M.L.*, Hu L.I., Scholle M., Sorensen D., Sahu A.K., Becher D., Antelmann H., Mrksich M., Anderson W.F., Gibson B.W., Schilling B., and Wolfe A.J. (2014) The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites. Microbiol. Stogios P.J., Kuhn M.L., Evdokimova E., Courvalin P., Anderson W.F., and Savchenko A. (2014) Potential for reduction of streptogramin A resistance revealed by structural analysis of the VatA acetyltransferase. Majorek K.A., Kuhn M.L., Chruszcz M., Anderson W.F., and Minor W. (2014) Double trouble-buffer selection and His-tag presence may be responsible for non-reproducibility of biomedical experiments. Kuhn M.L.*, Zemaitaitis B*, Hu L.I.*, Sahu A., Sorensen D., Lima B.P., Scholle M., Mrksich M., Anderson W.F., Gibson B., Schilling B and Wolfe A.J. (2014) Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation. Martinez S., Kuhn M.L., Russell J.T., Holz R.C., and Elgren T.E. (2014) Acrylamide production using encapsulated nitrile hydratase from Pseudonocardia thermophila in a sol-gel matrix. Kuhn M.L.*, Prachi P.*, Minasov G., Shuvalova L., Ruan J., Dubrovska I., Winsor J., Giraldi M., Biagini M., Liberatori S., Savino S., Bagnoli F., Anderson W.F., and Grandi G. (2014) Structure and protective efficacy of the Staphylococcus aureus autocleaving protease EpiP. Smith J.M., Warrington N.V., Vierling R.J., Kuhn M.L., Anderson W.F., Koppisch A.T., and Freel Meyers C.L. (2014) Targeting DXP synthase in human pathogens: enzyme inhibition and antimicrobial activity of butylacetylphosphonate. Majorek K.A., Kuhn M.L., Chruszcz M., Anderson W.F., and Minor W. (2013) Structural, functional and inhibition studies of a GNAT superfamily protein PA4794: a new C-terminal lysine protein acetyltransferase from Pseudomonas aeruginosa Hu L.I., Chi B.K., Kuhn M.L., Filippova E.V., Walker-Peddakotla A.J., Basell K., Becher D., Anderson W.F., Antelmann H., and Wolfe A.J. (2013) Acetylation of the response regulator RcsB controls transcription from a small RNA promoter. Figueroa C.M.*, Kuhn M.L.*, Falaschetti C.A., Solamen L., Olsen K.W., Ballicora M.A., and Iglesias A.A. (2013) Unraveling the activation mechanism of the potato tuber ADP-glucose pyrophosphorylase. Gumataotao N., Kuhn M.L., Hajnas N., and Holz R.C. (2013) Identification of an active site bound nitrile hydratase intermediate through single turnover stopped-flow spectroscopy Filippova E.V.*, Weston L.A.*, Kuhn M.L., Geissler B., Gehring A.M., Armoush N., Adkins C.T., Minasov G., Dubrovska I., Shuvalova L., Winsor J.R., Lavis L.D., Satchell K.J.F., Becker D.P., Anderson W.F., and Johnson R.J. (2013) Large-scale structural rearrangement of a serine hydrolase from Francisella tularensis facilitates catalysis. Kuhn M.L.*, Figueroa, C.M.*, Iglesias, A.A., and Ballicora, M.A. (2013) The ancestral activation promiscuity of ADP-glucose pyrophosphorylases from oxygenic photosynthetic organisms. Kuhn M.L., Majorek K.A., Minor W., and Anderson W.F. (2013) Broad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificity. Figueroa, C.M.*, Asencion, M.D.*, Kuhn M.L., McEwen, S., Salerno, G.L., Iglesias, A. A., and Ballicora, M.A. (2012) The Unique Nucleotide Specificity of the Sucrose Synthase from Thermosynechococcus elongates. Machtey M., Kuhn M.L., Flasch, D.A., Aleanzi M., Ballicora M.A., and Iglesias A.A. (2012) Glycogen metabolism in chemo-litho-autotrophic bacteria: distinctive kinetic and regulatory properties of ADP-glucose pyrophosphorylase from Nitrosomonas europaea.