Metal site occupancy and allosteric switching in bacterial metal sensor proteins
Open accessAbstract
All prokaryotes encode a panel of metal sensor or metalloregulatory proteins that govern the expression of genes that allows an organism to quickly adapt to toxicity or deprivation of both biologically essential transition metal ions, e.g., Zn, Cu, Fe, and heavy metal pollutants. As such, metal sensor proteins can be considered arbiters of intracellular transition metal bioavailability and thus potentially control the metallation state of the metalloproteins in the cell. Metal sensor proteins are specialized allosteric proteins that regulate transcription as a result direct binding of one or two cognate metal ions, to the exclusion of all others. In most cases, the binding of the cognate metal ion induces a structural change in a protein oligomer that either activates or inhibits operator DNA binding. A quantitative measure of the degree to which a particular metal drives metalloregulation of operator DNA-binding is the allosteric coupling free energy, ΔGc. In this review, we summarize recent work directed toward understanding metal occupancy and metal selectivity of these allosteric switches in selected families of metal sensor proteins and examine the structural origins of ΔGc in the functional context a thermodynamic "set-point" model of intracellular metal homeostasis.
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Sensitivity is determined by the affinity of the metalloregulator for its cognate ion and the effects of DNA-binding on metal affinity.
“Sensitivity is determined by the affinity of the metalloregulator for its cognate ion and the effects of DNA-binding on metal affinity (thermodynamic coupling), as discussed in detail elsewhere.26,30”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [30]
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Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702 · see citing works
Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis
Outten, C. E., & O'Halloran, A. T. V. (2001) · Science · doi:10.1126/science.1060331 · Cited by 1,489 · see citing works
The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
Lee, J.-W., & Helmann, J. D. (2006) · Nature · doi:10.1038/nature04537 · Cited by 547 · see citing works
Functional specialization within the Fur family of metalloregulators
Lee, J.-W., & Helmann, J. D. (2007) · BioMetals · doi:10.1007/s10534-006-9070-7 · Cited by 432 · see citing works
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
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 Chemical Biology · doi:10.1038/nchembio844 · Cited by 338 · see citing works
Self-citationPohl, E., Haller, J. C., Mijovilovich, A., Meyer‐Klaucke, W., Garman, E., & Vasil, M. L. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03337.x · Cited by 326 · see citing works
Grossoehme, N., Kehl-Fie, T. E., Ma, Z., Adams, K. W., Cowart, D. M., Scott, R. A., Skaar, E. P., & Giedroc, D. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220012 · Cited by 101 · see citing works
Self-citationXiong, A., & Jayaswal, R. K. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.16.4024-4029.1998 · Cited by 100 · see citing works
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Research works printed but not linked: 131
- [1]Reyes-Caballero H Campanello GC Giedroc DP Biophys Chem 156 2011 103 114 21511390 PMC3097251
- [2]Giedroc DP Arunkumar AI Dalton Trans 29 2007 3107 3120 17637984
- [3]Ma Z Jacobsen FE Giedroc DP Chem Rev 109 2009 4644 4681 19788177 PMC2783614
- [4]Busenlehner LS Pennella MA Giedroc DP FEMS Microbiol Rev 27 2003 131 143 12829264
- [5]Osman D Cavet JS Nat Prod Rep 27 2010 668 680 20442958
- [6]Mandal S Chatterjee S Dam B Roy P Das Gupta SK Microbiology 153 2007 80 91 17185537
- [7]Guimaraes BG Barbosa RL Soprano AS Campos BM de Souza TA Tonoli CC Leme AF Murakami MT Benedetti CE J Biol Chem 286 2011 26148 26157 21632538 PMC3138302
- [8]Lee JW Helmann JD Biometals 20 2007 485 499 17216355
- [9]Kloosterman TG van der Kooi-Pol MM Bijlsma JJ Kuipers OP Mol Microbiol 65 2007 1049 1063 17640279
- [10]Kloosterman TG Witwicki RM van der Kooi-Pol MM Bijlsma JJ Kuipers OP J Bacteriol 190 2008 5382 5393 18515418 PMC2493273
- [11]Reyes-Caballero H Guerra AJ Jacobsen FE Kazmierczak KM Cowart D Koppolu UM Scott RA Winkler ME Giedroc DP J Mol Biol 403 2010 197 216 20804771 PMC2949468
- [12]Jacobsen FE Kazmierczak KM Lisher JP Winkler ME Giedroc DP Metallomics 3 2011 38 41 21275153 PMC3061551
- [13]Shafeeq S Kloosterman TG Kuipers OP Metallomics 3 2011 609 618 21603707
- [14]Orth P Schnappinger D Hillen W Saenger W Hinrichs W Nat Struct Biol 7 2000 215 219 10700280
- [15]Kuroda M Hayashi H Ohta T Microbiol Immunol 43 1999 115 125 10229265
- [16]Arunkumar AI Campanello GC Giedroc DP Proc Natl Acad Sci U S A 106 2009 18177 18182 19822742 PMC2775347
- [17]Outten CE Outten FW O'Halloran TV J Biol Chem 274 1999 37517 37524 10608803
- [18]Changela A Chen K Xue Y Holschen J Outten CE O'Halloran TV Mondragon A Science 301 2003 1383 1387 12958362
- [19]Llull D Poquet I Appl Environ Microbiol 70 2004 5398 5406 15345426 PMC520854
- [20]Llull D Son O Blanie S Briffotaux J Morello E Rogniaux H Danot O Poquet I J Bacteriol 193 2011 1919 1929 21317326 PMC3133029
- [21]Panina EM Mironov AA Gelfand MS Proc Natl Acad Sci U S A 100 2003 9912 9917 12904577 PMC187884
- [22]Outten CE O'Halloran TV Science 292 2001 2488 2492 11397910
- [23]Waldron KJ Robinson NJ Nat Rev Microbiol 7 2009 25 35 19079350
- [24]Waldron KJ Rutherford JC Ford D Robinson NJ Nature 460 2009 823 830 19675642
- [26]Eide DJ Biochim Biophys Acta 1763 2006 711 722 16675045
- [27]Krezel A Maret W J Am Chem Soc 129 2007 10911 10921 17696343
- [28]Suhy DA Simon KD Linzer DI O'Halloran TV J Biol Chem 274 1999 9183 9192 10092590
- [29]Maret W J Nutr 133 2003 1460S 1462S 12730443
- [30]Krezel A Maret W J Biol Inorg Chem 11 2006 1049 1062 16924557
- [31]Bozym RA Thompson RB Stoddard AK Fierke CA ACS Chem Biol 1 2006 103 111 17163650
- [32]Vinkenborg JL Nicolson TJ Bellomo EA Koay MS Rutter GA Merkx M Nat Methods 6 2009 737 740 19718032 PMC6101214
- [33]Otvos JD Armitage IM Proc Natl Acad Sci U S A 77 1980 7094 7098 6938956 PMC350447
- [34]Zangger K Oz G Otvos JD Armitage IM Protein Sci 8 1999 2630 2638 10631978 PMC2144227
- [35]Pruteanu M Neher SB Baker TA J Bacteriol 189 2007 3017 3025 17220226 PMC1855835
- [36]Mettert EL Kiley PJ J Mol Biol 354 2005 220 232 16243354
- [37]Pruteanu M Baker TA Res Microbiol 160 2009 677 683 19747971 PMC2783568
- [38]Festa RA Jones MB Butler-Wu S Sinsimer D Gerads R Bishai WR Peterson SN Darwin KH Mol Microbiol 79 2011 133 148 21166899 PMC3052634
- [39]Stoyanov JV Mancini S Lu ZH Mourlane F Poulsen KR Wimmer R Solioz M FEMS Microbiol Lett 302 2010 69 75 19903200
- [40]Grossoehme NE Giedroc DP J Am Chem Soc 131 2009 17860 17870 19995076 PMC2811267
- [41]Ma Z Cowart DM Ward BP Arnold RJ DiMarchi RD Zhang L George GN Scott RA Giedroc DP J Am Chem Soc 131 2009 18044 18045 19928961 PMC2797707
- [42]Reinhart GD Methods Enzymol 380 2004 187 203 15051338
- [43]Singh VK Xiong A Usgaard TR Chakrabarti S Deora R Misra TK Jayaswal RK Mol Microbiol 33 1999 200 207 10411736
- [44]Xiong A Jayaswal RK J Bacteriol 180 1998 4024 4029 9696746 PMC107394
- [45]Sun Y Wong MD Rosen BP J Biol Chem 276 2001 14955 14960 11278706
- [46]Andrews SC Robinson AK Rodriguez-Quinones F FEMS Microbiol Rev 27 2003 215 237 12829269
- [47]Stoll KE Draper WE Kliegman JI Golynskiy MV Brew-Appiah RA Phillips RK Brown HK Breyer WA Jakubovics NS Jenkinson HF Brennan RG Cohen SM Glasfeld A Biochemistry 48 2009 10308 10320 19795834 PMC3586275
- [48]Pennella MA Arunkumar AI Giedroc DP J Mol Biol 356 2006 1124 1136 16406068
- [49]Busenlehner LS Weng TC Penner-Hahn JE Giedroc DP J Mol Biol 319 2002 685 701 12054863
- [50]Cavet JS Graham AI Meng W Robinson NJ J Biol Chem 278 2003 44560 44566 12939264
- [51]Wang Y Hemmingsen L Giedroc DP Biochemistry 44 2005 8976 8988 15966722
- [52]Ma Z Gabriel SE Helmann JD Nucl Acids Res 2011 in press PMC3241647 21821657
- [53]Popovych N Sun S Ebright RH Kalodimos CG Nat Struct Mol Biol 13 2006 831 838 16906160 PMC2757644
- [54]Lefevre JF Dayie KT Peng JW Wagner G Biochemistry 35 1996 2674 2686 8611573
- [55]Krizova H Zidek L Stone MJ Novotny MV Sklenar V J Biomol NMR 28 2004 369 384 14872128
- [56]Kern D Zuiderweg ER Curr Opin Struct Biol 13 2003 748 757 14675554
- [57]Akke M Curr Opin Struct Biol 12 2002 642 647 12464317
- [58]Englander JJ Louie G McKinnie RE Englander SW J Mol Biol 284 1998 1695 1706 9878380
- [59]Reyes-Caballero H Lee CW Giedroc DP Biochemistry 50 2011 7941 7952 21819125 PMC3225088
- [60]Ma Z Lee JW Helmann JD Nucl Acids Res 39 2011 5036 5044 21398634 PMC3130269
- [61]Grossoehme NE Akilesh S Guerinot ML Wilcox DE Inorg Chem 45 2006 8500 8508 17029360
- [62]Pohl E Holmes RK Hol WG J Mol Biol 285 1999 1145 1156 9887269
- [63]Pohl E Haller JC Mijovilovich A Meyer-Klaucke W Garman E Vasil ML Mol Microbiol 47 2003 903 915 12581348
- [64]Dian C Vitale S Leonard GA Bahlawane C Fauquant C Leduc D Muller C de Reuse H Michaud-Soret I Terradot L Mol Microbiol 79 2011 1260 1275 21208302
- [65]Lucarelli D Russo S Garman E Milano A Meyer-Klaucke W Pohl E J Biol Chem 282 2007 9914 9922 17213192
- [66]Shin JH Jung HJ An YJ Cho YB Cha SS Roe JH Proc Natl Acad Sci U S A 108 2011 5045 5050 21383173 PMC3064357
- [67]Guerra AJ Dann CE III Giedroc DP J Am Chem Soc 2011 in press 10.1021/ja2080532 PMC3246308 22085181 · DOI
- [68]Eicken C Pennella MA Chen X Koshlap KM VanZile ML Sacchettini JC Giedroc DP J Mol Biol 333 2003 683 695 14568530
- [69]Busenlehner LS Giedroc DP J Inorg Biochem 100 2006 1024 1034 16487591
- [70]VanZile ML Cosper NJ Scott RA Giedroc DP Biochemistry 39 2000 11818 11829 10995250
- [71]Lee S Arunkumar AI Chen X Giedroc DP J Am Chem Soc 128 2006 1937 1947 16464095
- [72]Maciag A Dainese E Rodriguez GM Milano A Provvedi R Pasca MR Smith I Palu G Riccardi G Manganelli R J Bacterio l 189 2007 730 740 PMC1797298 17098899
- [73]Diaz-Mireles E Wexler M Sawers G Bellini D Todd JD Johnston AW Microbiology 150 2004 1447 1456 15133106
- [74]Ahn BE Cha J Lee EJ Han AR Thompson CJ Roe JH Mol Microbiol 59 2006 1848 1858 16553888
- [75]An YJ Ahn BE Han AR Kim HM Chung KM Shin JH Cho YB Roe JH Cha SS Nucl Acids Res 2009 3442 3451 19336416 PMC2691836
- [76]Lee JW Helmann JD Nature 440 2006 363 367 16541078
- [77]Jacquamet L Traore DA Ferrer JL Proux O Testemale D Hazemann JL Nazarenko E El Ghazouani A Caux-Thang C Duarte V Latour JM Mol Microbiol 73 2009 20 31 19508285
- [78]Small SK Puri S O'Brian MR Biometals 22 2009 89 97 19093075 PMC2659648
- [79]Hibbing ME Fuqua C J Bacteriol 193 2011 3461 3472 21602352 PMC3133315
- [80]Traore DA El Ghazouani A Jacquamet L Borel F Ferrer JL Lascoux D Ravanat JL Jaquinod M Blondin G Caux-Thang C Duarte V Latour JM Nat Chem Biol 5 2009 53 59 19079268
- [81]Traore DA El Ghazouani A Ilango S Dupuy J Jacquamet L Ferrer JL Caux-Thang C Duarte V Latour JM Mol Microbiol 61 2006 1211 1219 16925555
- [82]Outten CE Tobin DA Penner-Hahn JE O'Halloran TV Biochemistry 40 2001 10417 10423 11523983
- [83]Carrington PE Chivers PT Al-Mjeni F Sauer RT Maroney MJ Nat Struct Biol 10 2003 126 130 12524532
- [84]Pennella MA Shokes JE Cosper NJ Scott RA Giedroc DP Proc Natl Acad Sci U S A 100 2003 3713 3718 12651949 PMC152987
- [85]Giedroc DP Mol Microbiol 73 2009 1 4 19508286 PMC2765198
- [86]Ma Z Cowart DM Scott RA Giedroc DP Biochemistry 48 2009 3325 3334 19249860 PMC2728441
- [87]Bradley MJ Chivers PT Baker NA J Mol Biol 378 2008 1155 1173 18433769 PMC2478562
- [88]Sindhikara DJ Roitberg AE Merz KM Jr Biochemistry 48 2009 12024 12033 19891498 PMC2795120
- [89]Chakravorty DK Wang B Lee CW Giedroc DP Merz KM J Am Chem Soc 2011 in press PMC3288340 22007899
- [90]Watanabe S Kita A Kobayashi K Miki K Proc Natl Acad Sci U S A 105 2008 4121 4126 18334645 PMC2393793
- [91]Liu T Ramesh A Ma Z Ward SK Zhang L George GN Talaat AM Sacchettini JC Giedroc DP Nat Chem Biol 3 2007 60 68 17143269
- [92]Corbett D Schuler S Glenn S Andrew PW Cavet JS Roberts IS Mol Microbiol 2011 21564342
- [93]Iwig JS Rowe JL Chivers PT Mol Microbiol 62 2006 252 262 16956381
- [94]Iwig JS Leitch S Herbst RW Maroney MJ Chivers PT J Am Chem Soc 130 2008 7592 7606 18505253 PMC2435081
- [95]Grossoehme N Kehl-Fie TE Ma Z Adams KW Cowart DM Scott RA Skaar EP Giedroc DP J Biol Chem 286 2011 13522 13531 21339296 PMC3075698
- [96]Campbell DR Chapman KE Waldron KJ Tottey S Kendall S Cavallaro G Andreini C Hinds J Stoker NG Robinson NJ Cavet JS J Biol Chem 282 2007 32298 32310 17726022 PMC3145109
- [97]Wu J Rosen BP J Biol Chem 268 1993 52 58 8416957
- [98]Morby AP Turner JS Huckle JW Robinson NJ Nucl Acids Res 21 1993 921 925 8451191 PMC309225
- [99]Harvie DR Andreini C Cavallaro G Meng W Connolly BA Yoshida K Fujita Y Harwood CR Radford DS Tottey S Cavet JS Robinson NJ Mol Microbiol 59 2006 1341 1356 16430705
- [100]Cavet JS Meng W Pennella MA Appelhoff RJ Giedroc DP Robinson NJ J Biol Chem 277 2002 38441 38448 12163508
- [102]Banci L Bertini I Cantini F Ciofi-Baffoni S Cavet JS Dennison C Graham AI Harvie DR Robinson NJ J Biol Chem 282 2007 30181 30188 17599915
- [103]Ye J Kandegedara A Martin P Rosen BP J Bacteriol 187 2005 4214 4221 15937183 PMC1151749
- [104]Barondeau DP Kassmann CJ Bruns CK Tainer JA Getzoff ED Biochemistry 43 2004 8038 8047 15209499
- [105]Sankararamakrishnan R Verma S Kumar S Proteins 58 2005 211 221 15508143
- [106]Chung KC Cao L Dias AV Pickering IJ George GN Zamble DB J Am Chem Soc 130 2008 14056 14057 18834129
- [107]West AL St John F Lopes PE MacKerell AD Jr Pozharski E Michel SL J Am Chem Soc 132 2010 14447 14456 20863122 PMC2958704
- [108]Schreiter ER Wang SC Zamble DB Drennan CL Proc Natl Acad Sci U S A 103 2006 13676 13681 16945905 PMC1564233
- [109]Phillips CM Nerenberg PS Drennan CL Stultz CM J Am Chem Soc 131 2009 10220 10228 19621966 PMC3579654
- [110]Phillips CM Schreiter ER Stultz CM Drennan CL Biochemistry 49 2010 7830 7838 20704276 PMC2934763
- [111]Borremans B Hobman JL Provoost A Brown NL van Der Lelie D J Bacteriol 183 2001 5651 5658 11544228 PMC95457
- [112]Chen P Greenberg B Taghavi S Romano C van der Lelie D He C Angew Chem Int Ed Engl 44 2005 2715 2719 15800869
- [113]Lund PA Ford SJ Brown NL J Gen Microbiol 132 Pt 2 1986 465 480 3011964
- [114]Ralston DM O'Halloran TV Proc Natl Acad Sci U S A 87 1990 3846 3850 2187194 PMC54000
- [115]Hobman JL Wilkie J Brown NL Biometals 18 2005 429 436 16158235
- [116]Dosanjh NS West AL Michel SL Biochemistry 48 2009 527 536 19119856
- [117]van Vliet AH Ernst FD Kusters JG Trends Microbiol 12 2004 489 494 15488389
- [118]Dosanjh NS Michel SL Curr Opin Chem Biol 10 2006 123 130 16504569
- [119]Ernst FD Stoof J Horrevoets WM Kuipers EJ Kusters JG van Vliet AH Infect Immun 74 2006 6821 6828 17015456 PMC1698083
- [120]Dosanjh NS Hammerbacher NA Michel SL Biochemistry 46 2007 2520 2529 17291009
- [121]Dian C Schauer K Kapp U McSweeney SM Labigne A Terradot L J Mol Biol 361 2006 715 730 16872629
- [122]Benini S Cianci M Ciurli S Dalton Trans 40 2011 7831 7833 21725560
- [123]Wen Y Feng J Scott DR Marcus EA Sachs G J Bacteriol 191 2009 449 460 18978046 PMC2620809
- [124]Tottey S Harvie DR Robinson NJ Acc Chem Res 38 2005 775 783 16231873
- [125]Kell DB Arch Toxicol 84 2010 825 889 20967426 PMC2988997
- [126]Burkhead JL Gray LW Lutsenko S Biometals 24 2011 455 466 21380607 PMC3106420
- [127]Whitmire JM Gancz H Merrell DS Curr Med Chem 14 2007 469 478 17305547
- [128]Flo TH Smith KD Sato S Rodriguez DJ Holmes MA Strong RK Akira S Aderem A Nature 432 2004 917 921 15531878
- [129]Corbin BD Seeley EH Raab A Feldmann J Miller MR Torres VJ Anderson KL Dattilo BM Dunman PM Gerads R Caprioli RM Nacken W Chazin WJ Skaar EP Science 319 2008 962 965 18276893
- [130]Kehl-Fie TE Chitayat S Hood MI Damo S Restrepo N Garcia C Munro KA Chazin WJ Skaar EP Cell Host Microbe 10 2011 158 164 21843872 PMC3157011
- [131]Nobles CL Maresso AW Metallomics 3 2011 788 796 21725569
- [132]Kehl-Fie TE Skaar EP Curr Opin Chem Biol 14 2010 218 224 20015678 PMC2847644
- [133]Wang SC Dias AV Bloom SL Zamble DB Biochemistry 43 2004 10018 10028 15287729
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- Authors
- Guerra, A. J., & Giedroc, D. P.
- Affiliations
- Indiana University Bloomington (US)
- Corresponding author
- Giedroc, David P.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 519
- Issue
- 2
- Pages
- 210-222
- ISSN
- 0003-9861 (ISSN-L)
- PMC
- PMC3312040
- OpenAlex
- W2085328815
- Cited by
- 77
- References
- 9
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 3 · 2022: 3 · 2021: 1 · 2020: 1 · 2019: 7 · 2018: 5 · 2017: 8 · 2016: 7 · 2015: 9 · 2014: 11 · 2013: 7 · 2012: 4
- FWCI
- 0.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- US National Institutes of Health (GM042569)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- metalloregulation, metal ion selectivity, transition metal homeostasis, transcriptional regulation, DNA binding, metalloproteins, bacterial metal homeostasis
- MeSH terms
- Allosteric Regulation, Bacteria, Bacterial Proteins, DNA, Bacterial, Metals
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