Current Research
Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine
Zhang, Y., Gonzalez-Gutierrez, G., Legg, K. A., Edwards, K. A., and GIEDROC, D. P. (2022) BioRxiv, (doi: 10.1101/2022.05.02.490363) (under review)
View: BioRxiv
SifR is an Rrf2-family quinone sensor associated with iron-catechol uptake in Streptococcus pneumoniae D39
Zhang, Y., Martin, J. E., Edmonds, K. A., Winkler, M. E., and GIEDROC, D. P. (2022)
J. Biol Chem, in the press (doi: 10.1016/j.jbc.2022.102046). *Editor’s pick
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Protocol using cysteine persulfide to elucidate chemical reactivity of persulfide sensors
Fakhoury, J. N., Capdevila, D. A. and GIEDROC, D. P. (2022)
STAR Protoc 3, 101424 (doi: 10.1016/j.xpro.2022.101424)
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Zn regulated GTPase metalloprotein activator 1 (ZNG1) regulates zinc homeostasis in vertebrates
Weiss, A., Murdoch, C. C., Edmonds K. A., Jordan, M. R., Monteith, A. J., Perera, Y. R.,
Rodríguez Nassif, A. M., Petoletti, A. M., Beavers, W. N., Krystofiak, E. S., Thalluri, K., Wu, H., DiMarchi, R. D., Chazin, W. J., *GIEDROC, D. P., and *Skaar E. P. (2022)
Cell 185, 1-16 (doi: 10.1016/j.cell.2022.04.011)
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Bacterial hydrophilins promote pathogen desiccation tolerance
Green, E.R., Fakhoury, J.N., Monteith, A. J., Pi, H., GIEDROC, D.P. and Skaar, E.P. (2022)
Cell Host Microbe, S1931-3128(22)00149-4 (doi: 10.1016/j.chom.2022.03.019)
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Functional asymmetry and chemical reactivity of CsoR family persulfide sensors
Fakhoury, J. N., Zhang, Y., Edmonds, K. A., Bringas, M., Luebke, J. L., Gonzalez-Gutierrez, G., Capdevila, D. A., and GIEDROC, D. P. (2021)
Nucl. Acid Res. 49, 12556-12576 (doi: 10.1093/nar/gkab1040)
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COG0523 proteins: A functionally diverse family of transition metal-regulated G3E P-loop GTP hydrolases from bacteria to man
Edmonds, K. A., Jordan, M. R., and GIEDROC, D. P. (2021)
Metallomics 13, mfab046 (doi: 10.1093/mtomcs/mfab046).
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Proteomics Profiling of S-sulfurated Proteins in Acinetobacter baumannii
Walsh, B. J. C., and GIEDROC, D. P. (2021)
Bio Protoc 11, e4000 (doi: 10.21769/BioProtoc.4000)
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Structural basis for persulfide-sensing specificity in a transcriptional regulator
Capdevila, D. A., Walsh, B. J. C., Zhang, Y., Dietrich, C., Gonzalez-Gutierrez, G., and GIEDROC, D. P. (2021)
Nat. Chem. Biol. 17, 65-70 (doi: 10.1038/s41589-020-00671-9)
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Staphylococcus aureus glucose-induced biofilm accessory protein A (GbaA) is a monothiol-dependent electrophile sensor
Ray, A., Edmonds, K. A., Palmer, L. D., Skaar, E. P., and GIEDROC, D. P. (2020)
Biochemistry 59, 2882–2895 (doi: 10.1021/acs.biochem.0c00347).
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The response of Acinetobacter baumannii to hydrogen sulfide reveals two independent persulfide-sensing systems and a connection to biofilm regulation
Walsh, B.J.C., Wang, J., Edmonds, K. A., Palmer, L. D., Zhang, Y., Trinidad, J. C., Skaar, E. P., and GIEDROC, D. P. (2020)
mBio 11, e01254-20 (doi: 10.1128/mBio.01254-20).
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The pneumococcal iron uptake protein A (PiuA) specifically recognizes tetradentate Fe(III) bis– and mono-catechol complexes
Zhang, Y., Edmonds, K. A., Raines, D. J., Murphy, B. A., Wu, H., Guo, C., Nolan, E. M., VanNieuwenhze, M. S., Duhme-Klair, A.-K., GIEDROC, D. P. (2020)
J. Mol. Biol. 432, 5390-5410 (doi: 10.1016/j.jmb.2020.08.005).
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1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the ABC transporter solute binding protein PiuA from Streptococcus pneumoniae
Edmonds, K. A., Zhang, Y., Raines, D. J., Duhme-Klair, A.-K., and GIEDROC, D. P. (2020)
Biomolec. NMR Assign. 14, 233–238 (doi: 10.1007/s12104-020-09952-9).
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Clostridioides difficile senses and hijacks host heme for incorporation into an oxidative stress defense system
Knippel, R. J., Wexler, A. G., Miller, J. M., Beavers, W. N., Weiss, A., de Crécy-Lagard, V., Edmonds, K. A., GIEDROC, D. P. and Skaar, E. P. (2020)
Cell Host Microbe 28, 411-421.e6 (doi: 10.1016/j.chom.2020.05.015)
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Cell-free biosensors for detection of water contaminants
Jung, J. K., Alam, K. K., Verosloff, M. S., Capdevila, D. A., Desmau, M., Clauer, P. R., Lee, J. W., Nguyen, P. Q., Pasten, P. A., Matiasek, S., Gaillard, J.-F., GIEDROC, D. P., Collins, J. J., and Lucks, J. B. (2020)
Nat. Biotech. 38, 1451-1459 (doi.org/10.1038/s41587-020-0571-7).
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A Mn-sensing riboswitch activates expression of a Mn2+/Ca2+ ATPase transporter in Streptococcus
Martin, J. E., Le, M. T., Bhattarai, N., Capdevila, D. A., Shen, J., Winkler, M. E. and GIEDROC, D. P. (2019)
Nucl. Acids Res. 47, 6885–6899 (doi: 10.1093/nar/gkz494).
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An Acinetobacter baumannii zinc regulated peptidase maintains cell wall integrity during immune-mediated nutrient sequestration
Lonergan, Z. R., Nairn, B. L., Wang, J., Hsu, Y.-P., Hesse, L. E., Beavers, W. N., Chazin, W. J., Trinidad, J. C., VanNieuwenhze, M. S., GIEDROC, D. P., and Skaar, E. P. (2019)
Cell Rep. 26, 2009-2018.e6. (doi:10.1016/j.celrep.2019.01.089).
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Multi-metal restriction by calprotectin impacts de novo flavin biosynthesis in Acinetobacter baumannii
Wang, J., Lonergan, Z. R., Gonzalez-Gutierrez, G., Nairn, B. L., Maxwell, C. N., Zhang, Y., Andreini, C., Karty, J. A., Chazin, W. J., Trinidad, J. C., Skaar, E. P., and GIEDROC, D. P. (2019)
Cell Chem. Biol. 16, 745-755.e7. (doi: 10.1016/j.chembiol.2019.02.011).
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Mechanistic insights into the metal-dependent activation of Zn(II)-dependent metallochaperones
Jordan, M. R., Wang, J., Weiss, A., Skaar, E. P., Capdevila, D. A., and GIEDROC, D. P. (2019)
Inorg. Chem. 58, 13661-13672 (doi: 10.1021/acs.inorgchem.9b01173).
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Thioredoxin profiling of multiple thioredoxin-like proteins in Staphylococcus aureus
Peng, H., Zhang, Y., Trinidad, J. C., & Giedroc, D. P. (2018)
Front. Microbiol. 9, 2385 (doi: 10.3389/fmicb.2018.02385)
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Hydrogen sulfide sensing through reactive sulfur species (RSS) and nitroxyl (HNO) in Enterococcus faecalis
Shen, J., Walsh, B. J. C., Flores-Mireles, A. L., Peng, H., Zhang, Y., Zhang, Y., Trinidad, J. C., Hultgren, S. J., & Giedroc, D. P. (2018)
ACS Chem. Biol. 13, 1610-1620 (doi: 10.1021/acschembio.8b00230)
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Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator
Capdevila, D. A., Huerta, F., Edmonds, K. A, Le, M. T., Wu, H. & GIEDROC, D. P. (2018)
eLife 7, e37268 (doi: 10.7554/eLife.37268)
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Functional role of solvent entropy and conformational entropy of metal binding in dynamically driven allosteric system
Capdevila, D. A., Edmonds, K. A, Campanello, G. C., Wu, H., Gonzalez-Gutierrez G,. & GIEDROC, D. P. (2018)
J Am. Chem. Soc. 140, 9108-9119 (doi: 0.1021/jacs.8b02129)
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Hydrogen sulfide and reactive sulfur species impact S-sulfhydration and global virulence regulation in Staphylococcus aureus
Peng, H., Zhang, Y., Palmer, L, D., Kehl-Fie, T. E., Skaar, E. C., Trinidad, J. C., & Giedroc, D. P. (2017)
ACS Infect. Dis. 3, 744-755 (doi: 10.1021/acsinfecdis.7b00090)
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Sulfide homeostasis and nitroxyl intersect via formation of reactive sulfur species (RSS) in Staphylococcus aureus
Peng, H., Shen, J., Edmonds, K. A., Luebke, J. L., Hickey, A. K., Palmer, L, D., Cheng, F.-M.J., Bruce, K. A., Kehl-Fie, T. E., Skaar, E. C., & Giedroc, D. P. (2017)
mSphere 2, e00082-17 (doi:10.1128/mSphere.00082-17)
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The sulfide-responsive transcriptional repressor SqrR functions as a master regulator of sulfide-dependent photosynthesis
Shimizu, T., Shen, J., Fang, M., Zhang, Y., Hori, K., Trinidad, J. C., Bauer, C. E., Giedroc, D. P. and Masuda, S. (2017)
Proc. Natl. Acad. Sci. U.S.A. 114, 2355-2360 (doi: 10.1073/pnas.1614133114).
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Metal-dependent allosteric activation and inhibition on the same molecular scaffold: The copper sensor CopY from Streptococcus pneumoniae
Glauninger, H., Zhang, Y., Higgins, K. A., Jacobs, A. D., Martin, J. E., Fu, Y., H. Coyne, J. 3rd, Bruce, K. E., Maroney, M. J., Clemmer, D. E., Capdevila, D. A., & GIEDROC, D. P. (2017)
Chem. Sci. 9, 105-118 (doi: 10.1039/c7sc04396a)
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Entropy redistribution controls allostery in a zinc metalloregulatory protein
Capdevila, D. A., Braymer, J. J., Edmonds, K. A., Wu, H., & GIEDROC, D. P. (2017)
Proc. Natl Acad. Sci. USA 114, 4424-4429 (doi: 10.1073/pnas.1620665114)
View: Pubmed
See the Commentary by Josh Wand in Proc Natl Acad Sci USA
The pneumococcal zinc efflux activator SczA protects Streptococcus pneumoniae serotype 2 D39 from intracellular zinc toxicity
Martin, J. E., Edmonds, K. A., Bruce, K. E., Campanello, G. C., Eijkelkamp, B. A., Brazel, E. B., McDevitt, C. A., Winkler, M. E., & GIEDROC, D. P. (2017)
Mol. Microbiol. 104, 636-651 (doi: 10.1111/mmi.13654)
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Perturbation of manganese metabolism disrupts cell division in Streptococcus pneumoniae
Martin, J. E. Lisher, J. P., Winkler, M. E., & GIEDROC, D. P. (2017)
Mol. Microbiol. 104, 334-348 (doi: 10.1111/mmi.13630).
View: Pubmed
Biological and chemical adaptation to endogenous hydrogen peroxide production in Streptococcus pneumoniae D39
Lisher, J. P., Ramos-Montañez, S., Hentchel, K. L. Tsui- T.-H., Winkler, M. E. & GIEDROC, D. P. (2017)
mSphere 2, e00291-16 (doi: 10.1128/mSphere.00291-16)
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Staphylococcus aureus sqr encodes a type II sulfide:quinone oxidoreductase (SQR) and impacts reactive sulfur speciation in cells
Shen, J., Peng, H., Zhang, Y., Trinidad, J. C., & Giedroc, D. P. (2016)
Biochemistry 55, 6524-6534
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The response of Acinetobacter baumannii to zinc starvation
Nairn, B. L., Lonergan, Z. R., Wang, J., Braymer, J. J., Zhang, Y., Calcutt, M. W., Gilston, B. A, Chazin, W. J., de Crécy-Lagard, V., GIEDROC, D. P.*, & Skaar, E. P.* (2016)
Cell Host Microbe 19, 826-836 (doi: 10.1016/j.chom.2016.05.007)
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Functional determinants of metal ion transport and selectivity in paralogous cation diffusion facilitator transporters CzcD and MntE in Streptococcus pneumoniae
Martin, J. E., & GIEDROC, D. P. (2016)
J. Bacteriol. 198, 1066-1076 (doi: 10.1128/JB.00975-15)
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Crystal structure of Clostridium difficile toxin
Rutherford, S. A., Chumber, N. M., Zhang, Z., Lisher, J. P., Farquhar, E., GIEDROC, D. P., Spiller, B. W.., Melnyk, R. A., and Lacy, D. B. (2016)
Nature Microbiol.1, article number 15002 (doi:10.1038/nmicrobiol.2015.2)
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The S2 Cu(I) site in CupA from Streptococcus pneumoniae is required for cellular copper resistance
Fu, Y., Bruce, K., Wu, H. & GIEDROC, D. P. (2016)
Metallomics 8, 61-70 (doi: 10.1039/c5mt00221d)
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Staphylococcus aureus CstB is a novel multidomain persulfide dioxygenase-sulfurtransferase involved in hydrogen sulfide detoxification
Shen, J., Keithly, M. E., Armstrong, R. N., Higgins, K. A., Edmonds, K. A. & Giedroc, D. P. (2015)
Biochemistry 54, 4542-4554 (doi: 10.1021/acs.biochem.5b00584)
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Resolution of stepwise cooperativities of copper binding by the homotetrameric copper-sensitive operon repressor (CsoR): Impact on structure and stability
Jacobs, A.D., Chang, F.-M.J, Morrison, L., Dilger, J.M., Wysocki, V.H., Clemmer, D.E., & GIEDROC, D. P. (2015)
Angew. Chem. Int. Ed. 54, 1-6 (doi: 10.1002/anie.201506349)
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Electrostatic occlusion and quaternary structural ion pairing are key determinants of Cu(I)-mediated allostery in the copper-sensing operon repressor (CsoR)
Chang, F.-M.J., Martin, J.E. & GIEDROC, D. P. (2015)
Biochemistry 54, 2462-2473 (doi: 10.1021/acs.biochem.5b00154)
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Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA
Higgins, K. A., Peng, H., Luebke, J. L., Chang, F.-M. J., & Giedroc, D. P. (2015)
Biochemistry 54, 2385-2398 (doi: 10.1021/acs.biochem.5b00056)
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The CsoR-like sulfurtransferase repressor (CstR) is a persulfide sensor in Staphylococcus aureus.
Luebke, J. L., Shen, J., Bruce, K. E., Kehl-Fie, T. E., Peng, H., Skaar, E. P., & Giedroc, D. P. (2014)
Mol. Microbiol. 94, 1343-1360 (doi: 10.1111/mmi.12835)
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Cu(I)-mediated allosteric switching in a copper-sensing operon repressor (CsoR)
Chang, F.-M. J., Coyne, H.J., Cubillas, C., Vinuesa, P., Fang, X., Ma, Z., Ma, D., Helmann, J.D., Garcia-de los Santos, A., Wang, Y.X., Dann, C.E. & GIEDROC, D. P. (2014)
J. Biol. Chem 289, 19204-19217 (doi: 10.1074/jbc.M114.556704)
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Conversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection
Reeves, B.D., Joshi, N., Campanello, G.C., Hilmer, J.K., Chetia, L., Vance, J.A., Reinschmidt, J.N., Miller, C.G., Dratz, E.A., Singel, D.J., Grieco, P.A. & GIEDROC, D. P. (2014)
Org. Biomol. Chem. 12, 7942-7956 (doi: 10.3389/fcimb.2013.00091)
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Co-ordinate synthesis and protein localization in a bacterial organelle by the action of a penicillin-binding-protein
Hughes, H.V., Lisher, J.P., Hardy, G.G., Kysela, D.T., Arnold, R.J., Brun, Y.V., & GIEDROC, D. P. (2013)
Mol Microbiol 90, 1162-1177 (doi: 10.1111/mmi.12422)
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Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae.
Lisher, J. P, Higgins, K. A., Maroney, M. J., & GIEDROC, D. P. (2013)
Biochemistry 52,7689-7701 (doi: 10.1021/bi401132w)
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Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Chakravorty, D. K, Wang, B., Lee, C. W., Guerra, A .J., GIEDROC, D. P., & Merz, K. M. Jr. (2013)
J. Biomol. NMR 56, 125-137.
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Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus
Luebke, J. L., Arnold, R. A. & Giedroc, D. P. (2013)
Metallomics 5, 335-342 (doi: 10.1039/c3mt20205d)
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A new structural paradigm in copper resistance in Streptococcus pneumoniae.
Fu, Y., Tsui, H .-C., Bruce, K. E., Sham, L. T., Higgins, K. A., Lisher, J .P., Kazmierczak, K. M., Maroney, M. J., Dann, C. E. 3rd, Winkler, M. E., & GIEDROC, D. P. (2013)
Nat. Chem. Biol. 9, 177-183.
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Allosteric inhibition of a zinc-sensing transcriptional repressor: Insights into the arsenic repressor (ArsR) family.
Campanello, G. C., Ma, Z., Grossoehme, N. E., Guerra, A. J., Ward, B. P., Dimarchi, R. D., Ye, Y,, Dann, C. E., 3rd, & GIEDROC, D. P. (2013)
J. Mol. Biol. 425, 1143-1157.
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Energetics of zinc-mediated interactions in the allosteric pathways of metal sensor proteins.
Chakravorty, D. K., Parker, T. M., Guerra, A. J., Sherrill, C. D., GIEDROC, D. P., & Merz, K. M. Jr. (2013)
J. Am. Chem. Soc. 135, 30-33.
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Backbone resonance assignments of the homotetrameric (48 kD) copper sensor CsoR from Geobacillus thermodenitrificans in the apo- and Cu(I)-bound states: insights into copper-mediated allostery.
Coyne, H. J., 3rd., & GIEDROC, D. P. (2012)
Biomol. NMR Assign. 7, 279-283 (doi: 10.1007/s12104-012-9428-4)
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(1)H, (13)C, and (15)N resonance assignments of NmtR, a Ni(II)/Co(II) metalloregulatory protein of Mycobacterium tuberculosis.
Lee, C. W., & GIEDROC, D. P. (2012)
Biomol. NMR Assign. 7, 145-148 (doi: 10.1007/s12104-012-9397-7)
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Solution structure of Mycobacterium tuberculosis NmtR in the apo state: insights into Ni(II)-mediated allostery.
Lee, C. W., Chakravorty, D. K., Chang, F. M., Reyes-Caballero, H., Ye, Y., Merz, K. M., Jr., GIEDROC, D. P. (2012)
Biochemistry 51, 2619-2629.
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Simulations of allosteric motions in the zinc sensor CzrA.
Chakravorty, D., Wang, B., Lee, C. W., GIEDROC, D. P., & Merz, K.M., Jr. (2012)
J. Am. Chem. Soc. 134, 3367-3376.
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Backbone and sterospecific methyl side chain resonance assignments of the homodimeric zinc sensor AdcR (32 kDa) in the apo- and Zn(II)-bound states.
Guerra, A. J.., & GIEDROC, D. P. (2012)
Biomol. NMR Assign. 8, 11-14 (doi: 10.1007/s12104-012-9442-6)
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Control of copper resistance and inorganic sulfur metabolism by paralogous regulators in Staphylococcus aureus
Grossoehme, N., Kehl-Fie, T.E., Ma, Z., Adams, K.W., Cowart, D.M., Scott, R.A., Skaar, E.P., & Giedroc, D.P. (2011)
J. Biol. Chem. 286, 13522-13531
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Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR.
Reyes-Caballero, H., Lee, C. W., & GIEDROC, D. P. (2011)
Biochemistry 50, 7941-7952.
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Control of copper resistance and inorganic sulfur metabolism by paralogous regulators in Staphylococcus aureus.
Grossoehme, N. E., Kehl-Fie, T. E., Ma, Z., Adams, K. W., Cowart, D. M., Scott, R. A., Skaar, E. P. ,& GIEDROC, D. P. (2011)
J. Biol. Chem. 286, 13522-13531.
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Interplay between manganese and zinc homeostasis in the human pathogen Streptococcus pneumoniae.
Jacobsen, F. E., Kazmierczak, K. M., Lisher, J. P., Winkler, M. E., & GIEDROC, D. P. (2011)
Metallomics 3, 38-41.
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Crystal structure of the zinc-dependent MarR family transcriptional regulator AdcR in the Zn(II)-bound state.
Guerra, A. J., Dann, C. E., III, & GIEDROC, D. P. (2011)
J. Am. Chem. Soc. 133, 19614-19617.
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Ratiometric pulse-chase amidination mass spectrometry as a probe of biomolecular complex formation.
Chang, F.-M., Lauber, M. A., Running, W. E., Reilly, J. P., & GIEDROC, D. P. (2011)
Anal. Chem. 83, 9092–9099.
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The CRR1 Nutritional Copper Sensor in Chlamydomonas Contains Two Distinct Metal-Responsive Domains.
Sommer, F,. Kropat, J., Malasarn, D., Grossoehme, N. E., Chen, X., GIEDROC, D. P., Merchant, S. S. (2010)
Plant Cell 22, 4098-4113.
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The metalloregulatory zinc site in Streptococcus pneumoniae AdcR, a zinc-activated MarR family repressor.
Reyes-Caballero, H., Guerra, A. J., Jacobsen, F. E., Kazmierczak, K. M., Cowart, D., Koppolu, U. M., Scott, R. A., Winkler, M. E., & GIEDROC, D. P. (2010)
J. Mol. Biol. 403, 197-216.
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Elucidation of the functional metal binding profile of a Cd(II)/Pb(II) sensor CmtR(Sc).
Wang, Y., Kendall, J., Cavet, J. S., & GIEDROC, D. P. (2010)
Streptomyces coelicolor. Biochemistry 49, 6617-6626.
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Molecular insights into the metal selectivity of the Cu(I)-sensing repressor CsoR from Bacillus subtilis.
Ma, Z., Cowart, D., Scott, R. A. & GIEDROC, D. P. (2009)
Biochemistry 48, 3325-3334.
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Structure of Thermotoga maritima TM0439: Implications for the mechanism of bacterial GntR transcription regulators with Zn2+-binding FCD domains.
Zheng, M., Cooper, D. R., Grossoehme, N. E., Yu, M., Hung, L. W., Cieslik, M., Derewenda, U., Lesley, S. A, Wilson, I. A., GIEDROC, D. P., Derewenda, Z. S. (2009)
Acta Cryst 65, 356-365.
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Solution structure of a paradigm ArsR family sensor in the DNA bound state.
Arunkumar, A. I., Campanello, G. C. & GIEDROC, D. P. (2009)
Proc. Natl. Acad. Sci. U. S. A. 106, 18177-18182.
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Energetics of allosteric negative coupling in the zinc sensor S. aureus CzrA.
Grossoehme, N. E., & GIEDROC, D. P. (2009)
J. Am. Chem. Soc. 131, 17860-17870.
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Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor.
Ma, Z., Cowart, D. M, Ward, B. P., Arnold, R. J., DiMarchi, R. D., Zhang, L., George, G. N., Scott, R. A., & GIEDROC, D. P. (2009)
J. Am. Chem. Soc. 131, 18044-18045.
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A Cu(I)-sensing ArsR family metal sensor protein with a relaxed metal selectivity profile.
Liu, T., Chen, X., Ma, Z., Shokes, J., Hemmingsen, L, Scott, R. A., Giedroc, D. P. (2008)
Biochemistry 47, 10564-10575.
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Copper sensing by Drosophila metal-responsive transcription factor-1 requires a Cu(I)4-S6 cluster.
Chen, X., Hua, H., Balamurugan, K., Kong, X., Wang, L., George, G. N., Georgiev, O., Schaffner, W. and Giedroc, D. P. (2008)
Nucl. Acids Res., 36, 3128-3138.
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Multiple metal-binding domains enhance the Zn(II) selectivity of the divalent metal ion transporter AztA.
Liu, T., Reyes, H., Li, C., Li, C., Scott, R. A., & Giedroc, D. P. (2007)
Biochemistry 46, 11057-11068.
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Resonance assignments of the metal sensor CzrA in the apo-, Zn2- and DNA-bound (42 kDa) states.
Arunkumar, A. I., Pennella, M. A., Kong, X., and Giedroc, D. P. (2007)
Biomol. NMR Assign 1, 99-101.
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CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator.
Liu, T., Ramesh, A., Ma, Z, Ward, S. K., Zhang, L., George, G. N., Talaat, A. M., Sacchettini, J. C., & Giedroc, D. P. (2007)
Nature Chem. Biol. 3, 60-68.
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Individual Metal Ligands Play Distinct Functional Roles in the Zinc Sensor Staphylococcus aureus CzrA.
Pennella, M.A., Arunkumar, A.I., & Giedroc, D. P. (2006)
J. Mol. Biol. 356, 1124-1136.
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Structural Insights into Homo- and Heterotropic Allosteric Coupling in the Zinc Sensor S. aureus CzrA from Covalently Fused Dimers.
Lee, S., Arunkumar, A.I., Chen, X., & Giedroc, D. P. (2006)
J. Am. Chem. Soc. 128, 1937-1947.
View: PubMed
Kinetics of Metal Binding by the Toxic Metal-Sensing Transcriptional Repressor S. aureus pI258 CadC.
Busenlehner, L. S., and Giedroc, D. P. (2006)
J. Inorg. Biochem. 100, 1024-1034.
View: PubMed
A Zn(II)/Pb(II)/Cd(II)-Inducible Operon from Anabaena is Regulated by AztR, an alpha3N ArsR/SmtB-family Metalloregulator.
Liu, T., Golden, J. W., & Giedroc, D. P. (2005)
Biochemistry 44, 8673-8683.
View: PubMed
Structural and Functional Characterization of M. tuberculosis CmtR, a Pb(II)/Cd(II)-sensing SmtB/ArsR Metalloregulatory Repressor.
Wang, Y., & Hemmingsen, L., & Giedroc, D. P. (2005)
Biochemistry 44, 8976-8988.
View: PubMed
A Novel Cyanobacterial SmtB/ArsR Family Metalloregulator Regulates a CPx-ATPase and a Metallothionein in Response to both Cu(I)/Ag(I) and Zn(II)/Cd(II).
Liu, T., Nakashima, S., Hirose, K., Shibasaka, M., Katsuhara, M., Ezaki, B., Giedroc, D. P., & Kasamo, K. (2004)
J. Biol. Chem. 279, 17810-17818.
View: PubMed
A Novel Cysteine Cluster in Human MTF-1 is Required for Heavy Metal-induced Transcriptional Activation in vivo.
Chen, X., Zhang, B., Harmon, P. M., Schaffner, W., Peterson, D. O., & Giedroc, D. P. (2004)
J. Biol. Chem. 279, 4515-4522.
View: PubMed
Ratiometric Pulsed Alkylation-Mass Spectrometry as a Probe of Thiolate Reactivity in Different Metalloderivatives of S. aureus pI258 CadC.
Apuy, J. A., Busenlehner, L. S., Russell, D. H., & Giedroc, D. P. (2004)
Biochemistry 43, 3824-3834.
View: PubMed
A Metal-Ligand mediated Intersubunit Allosteric Switch in Related SmtB/ArsR Zinc Sensor Proteins.
Eicken, C., Pennella, M. A., Chen, X., Koshlap, K., VanZile, M. L., Sacchettini, J. C., & Giedroc, D. P. (2003)
J. Mol. Biol. 333, 683-695.
View: PubMed
Structural Elements of Metal Selectivity in Metal Sensor Proteins.
Pennella, M. A., Shokes, J. E., Cosper, N. J., Scott, R. A., & Giedroc, D. P. (2003)
Proc. Natl. Acad. Sci. USA 100, 3713-3718.
View: PubMed
A Nickel-Cobalt Sensing ArsR-SmtB Family Repressor: Contributions of the Cytosol and Effector Binding Sites to Metal Selectivity.
Cavet, J. S., Meng, W., Pennella, M. A., Appelhoff, R. J., Giedroc, D. P., & Robinson, N. J. (2002)
J. Biol. Chem. 277, 38441-38448.
View: PubMed
Allosteric Negative Regulation of smt O/P Binding of the Zinc Sensor, SmtB, by Metal Ions: A Coupled Equilibrium Analysis.
VanZile, M. L., Chen, X., & Giedroc, D. P. (2002)
Biochemistry 41, 9776-9786.
View: PubMed
Structural and Functional Characterization of a Metalloregulatory Bi(III) Site in S. aureus pI258 CadC.
Busenlehner, L. S., Apuy, J. L., & Giedroc, D. P. (2002)
J. Biol. Inorg. Chem. 7, 551-559.
View: PubMed
Elucidation of Primary (alpha3N) and Vestigial (alpha5) Heavy Metal Binding Sites in S. aureus pI258 CadC: Evolutionary Implications for Metal Ion Selectivity of ArsR/SmtB Metal Sensor Proteins.
Busenlehner, L. S., Weng, T. -C., Penner-Hahn, J. E. & Giedroc, D. P. (2002)
J. Mol. Biol. 319, 685-701.
View: PubMed
Structural Characterization of Distinct alpha3N and alpha5 Metal Sites in the Cyanobacterial Zinc Sensor SmtB.
VanZile, M.L., Chen, X., & Giedroc, D.P. (2002)
Biochemistry 41, 9765-9775.
View: PubMed
Spectroscopic Properties of the Metalloregulatory Cd(II) and Pb(II) Sites of S. aureus pI258 CadC.
Busenlehner, L. S., Cosper, N. J., Scott, R. A., Rosen, B. P., Wong, M. D. & Giedroc, D. P. (2001)
Biochemistry 40, 4426-4436.
View: PubMed
Conformational Heterogeneity in the C-Terminal Zinc Fingers of Human MTF-1: An NMR and Zinc Binding Study.
Giedroc, D. P., Chen, X., Pennella, M. A., & LiWang, A. (2001)
J. Biol. Chem. 276, 42322-42332.
View: PubMed
Ratiometric Pulsed-Alkylation Mass Spectrometry of the Cysteine Pairs in Individual Zinc Fingers of MRE-Binding Transcription Factor-1 (MTF-1) as a Probe of Zinc Chelate Stability.
Apuy, J. L., Chen, X., Baldwin, T. O., Russell, D. H., & Giedroc, D. P. (2001)
Biochemistry 40, 15164-15175.
View: PubMed
Metal-Response Element-Binding Transcription Factor-1 (MTF-1): Structure, Function and Regulation.
Giedroc, D. P., Chen, X., & Apuy, J. L.. (2001)
Antiox. Redox Signal. 3, 577-596 (invited review).
View: PubMed
The Zinc Metalloregulatory Protein, Synechococcus PCC7942 SmtB, Binds a Single Zinc Ion per Monomer with High Affinity in a Tetrahedral Coordination Geometry.
VanZile, M. L., Cosper, N., Scott, R. A. & Giedroc, D. P. (2000)
Biochemistry 39, 11818-11829.
View: PubMed
MRE-Binding Transcription Factor-1: Weak Zinc-Binding Finger Domains 5 and 6 Modulate the Structure, Affinity and Specificity of the Metal-Response Element Complex.
Chen, X., Chu, M., & Giedroc, D. P. (1999)
Biochemistry 38, 12915-12925.
View: PubMed
Structural and Functional Heterogeneity Among the Zinc-Fingers of Human MRE-Binding Transcription Factor-1 (MTF-1).
Chen, X., Agarwal, A., & Giedroc, D. P. (1998)
Biochemistry 37, 11152-11161.
View: PubMed
Reviews
Molecular evolution of transition metal bioavailability at the host-pathogen interface
Antelo, G. T., Vila, A. J., GIEDROC, D. P. and Capdevila, D. A. (2021)
Trends Microbiol. 29, 441-457 (doi: 10.1016/j.tim.2020.08.001.)
View: PubMed
H2S and reactive sulfur signaling at the host bacterial pathogen interface
Walsh, B. J. C. and GIEDROC, D. P. (2020)
J. Biol. Chem. 295, 13150-13168 (doi: 10.1074/jbc.REV120.011304)
View: PubMed
Iron acquisition by bacterial pathogens: Beyond tris-catecholate complexes
Zhang, Y., Sen, S., and GIEDROC, D. P. (2020)
ChemBioChem 21, 1955-1967 (doi: 10.1002/cbic.201900778)
View: PubMed
Multi-metal nutrient restriction at the host-microbial pathogen interface
Jordan, M. R., Wang, J., Capdevila, D. A., and GIEDROC, D. P. (2020)
Curr. Opin. Microbiol. 55, 17-25 (doi: 10.1016/j.mib.2020.01.010).
View: PubMed
Metal Ion Homeostasis
In Comprehensive Coordination Chemistry III (Li, Y., Que, L. eds.),
Wang, J., Capdevila, D. A., and GIEDROC, D. P. (2020)
Elsevier, Ltd., Oxford, UK (doi: 10.1016/B978-0-12-409547-2.14675-X).
Hydrogen sulfide signaling and enzymology
In Comprehensive Natural Products III: Chemistry and Biology, Vol 4, pp. 430–473 (Liu, H.-W., Begley, T., eds.)
Walsh, B. J. C., Brito, J. A., and GIEDROC, D. P. (2020)
Elsevier, Ltd., Oxford, UK
View: PubMed
A new player in bacterial sulfide-inducible transcriptional regulation
GIEDROC, D. P. (2017)
Mol. Microbiol. 105, 347-352 (doi: 10.1111/mmi.13726)
View: PubMed
Metallochaperones and metalloregulation in bacteria
Capdevila, D. A., Edmonds, K. A., & GIEDROC, D. P. (2017)
Essays Biochem. 61, 177-200 (doi: 10.1042/EBC20160076)
View: PubMed
Mammalian copper biology: Hitting the pause button in celebration of three pioneers and four decades of discovery (Commentary)
La Fontaine, S., Burke, R., & GIEDROC, D. P. (2016)
Metallomics 8, 810-812 (doi: 10.1039/c6mt90035f)
View: PubMed
Bacterial strategies to maintain zinc metallostasis at the host-pathogen interface
Capdevila, D. A., Wang, J. and GIEDROC, D. P. (2016)
J Biol Chem. 291, 20858-20868 (doi: 10.1074/jbc.R116.742023)
View: PubMed
Cysteine sulfur chemistry in transcriptional regulators at the host-bacterial pathogen interface
Luebke, J. L., & GIEDROC, D. P. (2015)
Biochemistry 54, 3235-3249 (doi: 10.1021/acs.biochem.5b00085)
View: PubMed
Recent developments in copper and zinc homeostasis in bacterial pathogens
Braymer, J. J. & GIEDROC, D. P. (2014)
Curr. Opin. Chem. Biol. 19, 59-66 (doi: 10.1016/j.cbpa.2013.12.021)
View: PubMed
Copper transport and trafficking at the host-bacterial pathogen interface
Fu, Y., Chang, F.-M. J. & GIEDROC, D. P. (2014)
Acc Chem. Res. 47, 3605-3613 (doi: 10.1021/ar500300n)
View: PubMed
Insights into protein allostery in the CsoR/RcnR family of transcriptional repressors
Higgins, K. A. & GIEDROC, D. P. (2014)
Chem. Lett. (Japan) 43, 20-25
View: PubMed
Manganese acquisition and homeostasis at the host-pathogen interface
Lisher, J. P. & GIEDROC, D. P. (2013)
Front Cell Infect Microbiol. 3 (doi: 10.3389/fcimb.2013.00091)
View: PubMed
Metal specificity of metallosensors
Higgins, K. A. & GIEDROC, D. P. (2013)
In Metals in Cells (Culotta, V. & Scott, R. S., eds.), Chichester, UK. John Wiley & Sons, Ltd, pp. 209-224.
View: Online Publishing
Illuminating allostery in metal-sensing transcriptional regulators.
Grossoehme, N. E. & GIEDROC, D. P. (2012)
Methods Mol. Biol. 875, 165-192.
View: PubMed
Allosteric coupling between transition metal-binding sites in homooligomeric metal sensor proteins.
Grossoehme, N. E. & GIEDROC, D. P. (2012)
Methods Mol. Biol. 796, 31-51.
View: PubMed
Metal site occupancy and allosteric switching in bacterial metal sensor proteins.
Guerra, A. J., & GIEDROC, D. P. (2012)
Arch. Biochem. Biophys. 519, 210-222.
View: PubMed
Metalloregulatory proteins: Metal selectivity and allosteric switching.
Reyes-Caballero, H., Campanello, G. C., & GIEDROC, D. P. (2011)
Biophys. Chem. 156, 103-114. (Invited Perspective)
View: PubMed
Hydrogen peroxide sensing in Bacillus subtilis: it is all about the (metallo)regulator.
GIEDROC, D. P. (2009)
Mol. Micro. 73, 1-4 (Invited commentary)
View: PubMed
Coordination chemistry of bacterial metal transport and sensing.
Ma, Z, Jacobsen, F. E., & GIEDROC, D. P. (2009)
Chem. Rev.109, 4644-4681.
View: PubMed
Metal Sensor Proteins: Nature’s metalloregulated allosteric switches.
Giedroc, D. P. and Arunkumar, A. I. (2007)
Dalton Trans., 3107-3120 (Invited Perspective).
View: PubMed
Structural Determinants of Metal Selectivity in Prokaryotic Metal-Responsive Transcriptional Regulators.
Pennella, M. A., & Giedroc, D. P. (2005)
Biometals 18, 413-428 (invited review).
View: PubMed
The SmtB/ArsR Family of Metalloregulatory Transcriptional Repressors: Structural Insights into Prokaryotic Metal Resistance.
Busenlehner, L. S., Pennella, M. A., & Giedroc, D. P. (2003)
FEMS Microbiol. Rev. 27, 131-144 (invited review).
View: PubMed
Past RNA Research and Other Projects
SHAPE analysis of the RNA seconday structure of the Mouse Hepatitis Virus 5′ untranslated region and N-terminal nsp1 coding sequences
Yang, D., Liu, P., Wudeck, E.V., LEIBOWITZ, J.L., & GIEDROC, D. P. (2015)
Virology. 475, 15-27 (doi: 10.1016/j.virol.2014.11.001)
View: PubMed
Solution structure of mouse hepatitis virus (MHV) nsp3a and determinants of the interaction with MHV nucleocapsid (N) protein
Keane, S. C. & GIEDROC, D. P. (2013) (doi: 10.1128/JVI.03112-12)
J. Virol. 87, 3502-3515
View: PubMed
(1)H, (13)C, (15)N resonance assignments of murine hepatitis virus nonstructural protein 3a.
Keane, S. C. & GIEDROC, D. P. (2012)
Biomol. NMR Assign.8, 15-17 (doi: 10.1007/s12104-012-9443-5)
View: PubMed
Functional transcriptional regulatory sequence (TRS) RNA binding and helix destabilizing determinants of the murine hepatitis virus (MHV) nucleocapsid (N) protein.
Keane, S. C., Liu, P., Leibowitz, J. L. & GIEDROC, D. P. (2012)
J. Biol. Chem. 287, 7063-7073.
View: PubMed
A conserved RNA pseudoknot in a putative molecular switch domain of the 3′-untranslated region of coronaviruses is only marginally stable.
Stammler, S. N., Cao, S., Chen, S. J., & GIEDROC, D. P. (2011)
RNA 17, 1747-1759.
View: PubMed
Mouse hepatitis virus stem-loop 4 functions as a spacer element required to drive subgenomic RNA synthesis.
Yang, D., Liu, P., GIEDROC, D. P., & Leibowitz, J. L. (2011)
J. Virol. 85, 9199-9209.
View: PubMed
The solution structure of coronaviral stem-loop 2 (SL2) reveals a canonical CUYG tetraloop fold.
Lee, C. W., Li, L.,& GIEDROC, D. P. (2011)
FEBS Lett. 585, 1049-1053.
View: PubMed
Mouse hepatitis virus stem-loop 2 adopts an uYNMG(U)a-like tetraloop structure that is highly functionally tolerant of base substitutions.
Lui, P., Li, L., Keane, S. C., Yang, D., Leibowitz, J. L. & GIEDROC, D. P. (2009)
J. Virol. 83, 12084-12093.
View: PubMed
Coronavirus N protein N-terminal domain (NTD) specifically binds the transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA duplexes.
Grossoehme, N. E., Li, L., Keane, S. C., Liu, P., Dann, C. E., III, Leibowitz, J. L., & GIEDROC, D. P. (2009)
J. Mol. Biol. 394, 544-557.
View: PubMed
Structural lability in stem-loop 1 drives a 5′ UTR-3′ UTR interaction in coronavirus replication.
Li, L., Kang, H., Liu, P., Makkinje, N., Williamson, S. T., Leibowitz, J. L., and Giedroc, D. P. (2008)
J. Mol. Biol. 377, 790-803.
View: PubMed
A U-turn motif-containing stem-loop in the coronavirus 5′ untranslated region (UTR) plays a functional role in replication.
Liu, P., Li, L., Millership, J. J., Leibowitz, J. L., & Giedroc, D. P. (2007)
RNA 13, 763-780.
View: PubMed
Cis-acting stem-loops in the 5′ untranslated region of the severe acute respiratory syndrome coronavirus can substitute for their MHV counterparts.
Kang, H., Feng, M., Schroeder, M. E., Giedroc, D. P., & Leibowitz, J. L. (2006)
J. Virol. 80, 10600-10614.
View: PubMed
Coming Soon!
Structure of the large extracellular loop of FtsX and its interaction with the essential peptidoglycan hydrolase PcsB in Streptococcus pneumoniae
Rued, B. E., Alcorlo, M., Edmonds, K. A., Martínez-Caballero, S., Straume, D., Fu, Y., Bruce, K. E., Wu, H., Håvarstein, L. S., Hermoso, J. A., Winkler, M. E., & Giedroc, D. P. (2018)
mBio 10, e02622-18 (doi: 10.1128/mBio.02622-18).
View: PubMed
1H, 13C, 15N resonance assignments of the extracellular loop 1 domain (ECL1) of Streptococcus pneumoniae D39 FtsX, an essential cell division protein
Fu, Y., Bruce, K. E., Rued, B., Winkler, M. E., & Giedroc, D. P. (2016)
Biomol. NMR Assign. 10, 89-92 (doi: 10.1007/s12104-015-9644-9)
View: PubMed