Publications
My bibliography here
Student co-authors marked with an asterisk (*)
2023
Variot C.*, Capule D.*, Arolli X., Baumgartner J.*, Reidl C., Houseman C.*, Ballicora M.A., Becker D.P., and Kuhn M.L. (2023) Mapping roles of active site residues in the acceptor site of the PA3944 Gcn5-related N-acetyltransferase (GNAT) enzyme. Protein Science. 32(8), e4725. PMID: 37418656. doi: 10.1002/pro.4725
Tsimbalyuk S., Shornikov A.*, Srivastav P., Le V.T.B, Warren I.*, Khandokar Y.B., Kuhn M.L.&, and Forwood J.K. (2023) Structural and kinetic characterization of the SpeG spermidine/spermine N-acetyltransferase from methicillin-resistant Staphylococcus aureus USA300. Cells. 12(14), 1829. PMID: 37508494. doi: 10.3390/cells12141829
2022
Jew K.M.*, Le V.T.B., Amaral K.*, Ta A.*, Nguyen May N.M.*, Law M., Adelstein N., and Kuhn M.L. (2022) Investigation of the importance of protein 3D structure for assessing conservation of lysine acetylation sites in protein homologs. Front. Microbiol. 12:805181. PMID: 35173693. doi: 10.3389/fmicb.2021.805181
2021
Le V.T.B.*, Dang J.*, Lim E.Qi*, and Kuhn M.L. (2021) Criticality of a conserved tyrosine residue in the SpeG protein from Escherichia coli. Protein Sci. 30(6), 1264-1269. PMID: 33826189. doi: 10.1002/pro.4078
Ghafoori S.M., Robles A.M.*, Arada A.M.*, Shirmast P., Dranow D.M., Mayclin S.J., Lorimer D.D., Myler P.J., Edwards T.E., Kuhn M.L., and Forwood J.K. (2021) Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1. Sci. Rep. 11(1), 9453. PMID: 33947893. doi: 10.1038/s41598-021-88672-z
Le V.T.B.*, Tsimbalyuk S., Lim E.Qi*, Solis A.*, Gawat D.*, Boeck P.*, Lim E.Qing*, Renolo R.*, Forwood J.K., and Kuhn M.L. (2021) The Vibrio cholerae SpeG spermidine/spermine N-acetyltransferase allosteric loop and B6-B7 structural elements are critical for kinetic activity. Front. Mol. Biosci. 8, 645768. PMID: 33928120. doi: 10.3389/fmolb.2021.645768
Baumgartner J.T.*, Habeeb Mohammad T.S., Czub M.P., Majorek K., Arolli X., Variot C.*, Anonick M., Minor W., Ballicora M.A., Becker D.P., and Kuhn M.L. (2021) Gcn5-related N-acetyltransferases (GNATs) with a catalytic serine residue can play ping-pong too. Front. Mol. Biosci. 8, 646046. PMID: 33912589. doi: 10.3389/fmolb.2021.646046
Young E.C., Baumgartner J.T.*, Karatan E., and Kuhn M.L. (2021) A mutagenic screen reveals NspS residues important for regulation of Vibrio cholerae biofilm formation. Microbiology. 167(3), 001023. PMID: 33502310. doi: 10.1099/mic.0.001023 [Article selected as Editor’s Choice]
2020
Cereijo A.E., Kuhn M.L., Hernández M.A., Ballicora M.A., Iglesias A.A., Alvarez H.M., and Asencion Diez M.D. (2020) Study of duplicated galU genes in Rhodococcus jostii and a putative new metabolic node for glucosamine-1P in rhodococci. Biochim Biophys Acta Gen Subj. 1865(1), 129727. PMID: 32890704. doi: 10.1016/j.bbagen.2020.129727
Tsimbalyuk S., Shornikov A.*, Thi Bich Le V.*, Kuhn M.L., Forwood J.K. (2020) SpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency. J Struct Biol. 210(3), 107506. PMID: 32283314. doi: 10.1016/j.jsb.2020.107506
Alcala A.*, Ramirez G.*, Solis A.*, Kim Y., Tan K., Luna O.*, Nguyen K.*, Vazquez D.*, Ward M.*, Zhou M., Mulligan R., Maltseva N., and Kuhn M.L. (2020) Structural and functional characterization of three Type B and C chloramphenicol acetyltransferases from Vibrio species. Protein Sci. 29(3), 695-710. PMID: 31762145. doi: 10.1002/pro.3793
2019
Christensen D., Baumgartner J.*, Xie X., Jew K.*, Basisty N., Schilling B., Kuhn M.L., and Wolfe A.J. (2019) Protein acetylation in prokaryotes: mechanisms, detection, and relevance. mBio. 10(2), e02708-18. PMID: 30967470. doi: 10.1128/mBio.02708-18
2018
Hu L.I., Filippova E.V., Dang J.*, Pshenichnij S., Ruan J., Kiryukhina O., Anderson W.F., Kuhn M.L., and Wolfe A.J. (2018) The spermidine acetyltransferase SpeG regulates transcription of the small RNA RprA. PLOS One. 13(12), e0207563. PMID: 30562360. doi: 10.1371/journal.pone.0207563
Czub M., Zhang B.*, Chiarelli M., Majorek K., Joe L.*, Porebski P., Revilla A.*, Wu W., Becker D.P., Minor W., and Kuhn M.L. (2018) A Gcn5-related N-acetyltransferase (GNAT) capable of acetylating polymyxin B and colistin antibiotics in vitro. Biochemistry. 57(51), 7011-7020. PMID: 30499668. doi: 10.1021/acs.biochem.8b00946
Figueroa C.M., Kuhn M.L., Hill B.L., Iglesias A.A., and Ballicora M.A. (2018) Resurrecting the regulatory properties of the Ostreococcus tauri ADP-glucose pyrophosphorylase large subunit. Front. Plant Sci. 9, 1564. PMID: 30425723. doi: 10.3389/fpls.2018.01564
Ferrero D.M.L., Diez M.D.A., Kuhn M.L., Falaschetti C.A.*, Piattoni C.V., Iglesias A.A., and Ballicora M.A. (2018) On the roles of wheat endosperm ADP-glucose pyrophosphorylase subunits. Front. Plant Sci. 9, 1498. PMID: 30459778. doi: 10.3389/fpls.2018.01498
Christensen D.B., Meyer J.G., Baumgartner J.T.*, Sahu A.K., Nalson W.C., Payne S.H., Kuhn M.L., Schilling B., and Wolfe A.J. (2018) Identification of novel protein lysine acetyltransferases in Escherichia coli. mBio. 9(5), e01905-18. PMID: 30352934. doi: 10.1128/mBio.01905-18
Handing K.B., Niedzialkowska E., Shabalin I.G., Kuhn M.L., Zheng H., and Minor W. (2018) Characterizing metal binding sites in proteins with X-ray crystallography. Nat. Protoc. 13(5), 1062-1090. PMID: 29674755. doi: 10.1038/nprot.2018.018
Gokey T.*, Halavaty A.S., Minasov G., Anderson W.F., and Kuhn M.L. (2018) Structure of the Bacillus anthracis dTDP-L-rhamnose biosynthetic pathway enzyme: dTDP-a-D-glucose 4,6-dehydratase, RfbB. J. Struct. Biol. 202(2), 175-181. PMID: 29331609. doi: 10.1016/j.jsb.2018.01.006
2017
Law A.*, Stergioulis A.*, Halavaty A.S., Minasov G., Anderson W.F., and Kuhn M.L. (2017) Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductases (RfbD). Acta Cryst. F73, 644-650. PMID: 29199984. doi: 10.1107/S2053230X17015746
Shornikov A.*, Tran H.*, Macias J.*, Halavaty A.S., Minasov G., Anderson W.F., and Kuhn M.L. (2017) Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose 3,5-epimerase (RfbC). Acta Cryst. F73, 664-671. PMID: 29199987. doi: 10.1107/S2053230X17015849
Baumgartner J.*, Lee J.*, Halavaty A.S., Minasov, G., Anderson W.F., and Kuhn M.L. (2017) Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme glucose-1-phosphate thymidylyltransferase (RfbA). Acta Cryst. F73, 621-628. PMID: 29095156. doi: 10.1107/S2053230X17015357
Reidl C., Majorek K.A., Dang J.*, Tran D.*, Jew K.*, Law M.*, Payne Y., Minor W., Becker D.P., and Kuhn M.L. (2017) Generating enzyme and radical-mediated bisubstrates as tools for investigating Gcn5-related N-acetyltransferases. FEBS Lett. 591(15) 2348-2361. PMID: 28703494. doi: 10.1002/1873-3468.12753
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. Biochim Biophys Acta. 1865(1) 55-64. PMID: 27783928. doi: 10.1016/j.bbapap.2016.10.011
Stogios P.J., Kuhn M.L., Evdokimova E., Law M.*, Courvalin P., and Savchenko A. (2017) Structural and biochemical characterization of the Acinetobacter aminoglycoside acetyltransferases AAC(6’)-Ig and AAC(6’)-Ih highlights dramatic functional variety among resistance-conferring enzymes. ACS Infect. Dis. 3(2) 132-143. PMID: 27785912. doi: 10.1021/acsinfecdis.6b00058
2016
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. Dis. 2(8) 579-591. PMID: 27547819. doi: 10.1021/acsinfecdis.6b00082
2015
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. J. Mol. Biol. 427(6) PartB 1316-1334. PMID: 25623305. doi: 10.1016/j.jmb.2015.01.009
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. (2015) The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites. Microbiol. Open 4(1) 66-83. PMID: 25417765. doi: 10.1002/mbo3.223
2014
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. Antimicrob. Agents Chemother. 58(12) 7083-7092. PMID: 25223995. doi: 10.1128/AAC.03743-14
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. Protein Sci. 23(10) 1359-1368. PMID: 25044180. doi: 10.1002/pro.2520
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. PLOS ONE 9(4):e94816. PMID: 24756028. doi: 10.1371/journal.pone.0094816
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. J. Mol. Catal. B: Enzym (100) 19-24. doi:10.1016/j.molcatb.2013.11.014
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. FASEB J. 28: 1780-93. PMID: 24421400. doi: 10.1096/fj.13-241737
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. J. Antibiotics (67) 77-83. PMID: 24169798. doi: 10.1038/ja.2013.105
2013
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. J. Biol. Chem. (288) 30223-35. PMID: 24003232. doi: 10.1074/jbc.M113.501353
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. J. Bacteriol. 195 (18) 4174-4186. PMID: 23852870. doi: 10.1128/JB.00383-13
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. PLOS ONE 8(6) e66824. PMID: 23826149. doi: 10.1371/journal.pone.0066824
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. J. Biol. Chem. (288) 15532-15536. PMID: 23589282. doi: 10.1074/jbc.M112.398909
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. J. Biol. Chem. (288) 10522-10535. PMID: 23430251. doi: 10.1074/jbc.M112.446625
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. BMC Evol. Biol. 13:51. PMID: 23433303. doi: 10.1186/1471-2148-13-51
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. Protein Sci. 22(2) 222-230. PMID: 23184347. doi: 10.1002/pro.2199
Figueroa, C.M., Asencion, M.D., Kuhn M.L., McEwen, S.*, Salerno, G.L., Iglesias, A. A., and Ballicora, M.A. (2013) The Unique Nucleotide Specificity of the Sucrose Synthase from Thermosynechococcus elongates. FEBS Lett. 587 (2), 165-169. PMID: 23196182. doi: 10.1016/j.febslet.2012.11.011
2012
Machtey M., Kuhn M.L., Flasch, D.A.*, Aleanzi M., Ballicora M.A., and Iglesias A.A. (2012) Insights into glycogen metabolism in chemo-litho-autotrophic bacteria: distinctive kinetic and regulatory properties of ADP-glucose pyrophosphorylase from Nitrosomonas europaea. J. Bacteriol. 294 (22), 6056-6065. PMID: 22961847. doi: 10.1128/JB.00810-12
Makowska-Grzyska M., Kim Y., Wu R., Wilton R., Gollapalli D., Wang X., Zhang R., Jedrzejczak R., Mack J., Maltseva N., Mulligan R., Binkowski T., Gornicki P., Kuhn M.L., Anderson W., Hedstrom L., and Joachimiak A. (2012) Bacillus anthracis IMP dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate- and product-bound complexes. Biochemistry 51 (31), 6148-6163. PMID: 22788966. doi: 10.1021/bi300511w
Kuhn M.L., Martinez, S.*, Gumataotao, N.*, Bornscheuer, U., Liu, D., and Holz, R.C. (2012) The Fe-type nitrile hydratase from Comomonas testosteroni Ni1 does not require an activator accessory protein for expression in Escherichia coli. Biochem. Biophys. Res. Commun. 424 (3), 365-370. PMID: 22713452. doi: 10.1016/j.bbrc.2012.06.036
2010
Kuhn M.L., Figueroa C.M., Aleanzi M., Olsen K.W., Iglesias A.A., and Ballicora M.A. (2010) Bi-national and interdisciplinary course in enzyme engineering. Biochem. Mol. Biol. Edu. 38 (6), 370-379. PMID: 21567865. doi: 10.1002/bmb.20438
2009
Kuhn M.L., Falaschetti C.A.*, and Ballicora M.A. (2009) The Ostreococcus tauri ADP-glucose pyrophosphorylase reveals alternative paths for the evolution of subunit roles. J. Biol. Chem. (284) 34092-34102. PMID: 19737928. doi: 10.1074/jbc.M109.037614
2008
Ventriglia T., Kuhn M.L., Ruiz M.T., Ribeiro-Pedro M., Valverde F., Ballicora M.A., Preiss J., Romero J.M. (2008) Two Arabidopsis ADP-Glucose Pyrophosphorylase Large Subunits (APL1 and APL2) Are Catalytic. Plant Physiol. (148) 65-76. PMID: 18614708. doi: 10.1104/pp.108.122846
2006
Natasha T., Kuhn M., Kelly O. & Rittling S.R. (2006) Override of the osteoclast defect in osteopontin-deficient mice by metastatic tumor growth in the bone. Am. J. Pathol. (168) 551-561. PMID: 16436669. doi: 10.2353/ajpath.2006.050480
2005
Kuhn M., Shah S., Natasha T. & Rittling S.R. (2005) A mouse model of breast cancer metastasis to the choroid of the eye. Clin. Exp. Metastasis (22) 685-690. PMID: 16708307. doi: 10.1007/s10585-006-9012-3
2003
Guo X., Condra M., Kimura K., Berth G., Dautzenberg H. & Dubin P.L. (2003) Determination of molecular weight of heparin by size exclusion chromatography with universal calibration. Anal. Biochem. (312) 33-39. PMID: 12479832. doi: 10.1016/s0003-2697(02)00428-1