Metallostasis in Bacterial Pathogens

Metallostasis: Transition Metal Homeostasis in Bacterial Pathogens

In this project, our goal is to understand the molecular mechanisms of how cells regulate the intracellular bioavailability of essential transition metal ions, notably Cu, Mn and Zn among others. This process, termed metal homeostasis and resistance, represents an important battleground in human host-bacterial pathogen interactions since these ions may be limiting or in excess, both detrimental to the survival of the invading microbe. Metal sensor proteins bind specific DNA sequences and regulate the expression of homeostasis genes in response to specific metal ions. Recent studies involve the use of ion mobility mass spectrometry and methyl-NMR dynamics approaches to elucidate mechanisms of allosteric regulation in metallosensors, and understanding the physiological response of Acinetobacter baumanni to host-imposed Zn limitation, Fe limitation and Mn toxicity in Streptococcus pneumoniae using a variety of analytical approaches.

Reviews and Perspectives


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., in the press (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., in the press  (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, in the press (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., available online (
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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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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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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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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) 

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)
View: Pubmed

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).
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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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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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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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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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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 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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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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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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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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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.
View: PubMed

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.

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.
View:  SpringerLink

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.
View:  PubMed

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.
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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


Molecular evolution of transition metal bioavailability at the host-pathogen interface
Antelo, G. T., Vila, A. J., GIEDROC, D. P. and Capdevila, D. A. (2020)
Trends Microbiol., in the press (doi: 10.1016/j.tim.2020.08.001.)

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).

Metallochaperones and metalloregulation in bacteria
Capdevila, D. A., Edmonds, K. A., & GIEDROC, D. P. (2017)
Essays Biochem., in the press (doi: 10.1042/EBC20160076)

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

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

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

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

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