메뉴 건너뛰기




Volumn 12, Issue 2, 2009, Pages 138-144

Damage control: regulating defenses against toxic metals and metalloids

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMONY; ARSENIC; CADMIUM; CHROMIUM; COBALT; COPPER; GOLD; LEAD; MERCURY; MERR PROTEIN; METAL; NICKEL; PROTEIN ARSR; REPRESSOR PROTEIN; SELENIUM; SILVER; TELLURIUM; TRANSITION ELEMENT; UNCLASSIFIED DRUG; ZINC;

EID: 63749128999     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2009.02.003     Document Type: Review
Times cited : (56)

References (68)
  • 2
    • 33845230241 scopus 로고    scopus 로고
    • Modern proteomes contain putative imprints of ancient shifts in trace metal geochemistry
    • Dupont C.L., Yang S., Palenik B., and Bourne P.E. Modern proteomes contain putative imprints of ancient shifts in trace metal geochemistry. Proc Natl Acad Sci U S A 103 (2006) 17822-17827
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17822-17827
    • Dupont, C.L.1    Yang, S.2    Palenik, B.3    Bourne, P.E.4
  • 3
    • 17144394461 scopus 로고    scopus 로고
    • Advances in analytical methodology for bioinorganic speciation analysis: metallomics, metalloproteomics and heteroatom-tagged proteomics and metabolomics
    • Szpunar J. Advances in analytical methodology for bioinorganic speciation analysis: metallomics, metalloproteomics and heteroatom-tagged proteomics and metabolomics. Analyst 130 (2005) 442-465
    • (2005) Analyst , vol.130 , pp. 442-465
    • Szpunar, J.1
  • 4
    • 37749006472 scopus 로고    scopus 로고
    • Metalloids: essential, beneficial or toxic? Major intrinsic proteins sort it out
    • Bienert G.P., Sch ̧ssler M.D., and Jahn T.P. Metalloids: essential, beneficial or toxic? Major intrinsic proteins sort it out. Trends Biochem Sci 33 (2008) 20-26
    • (2008) Trends Biochem Sci , vol.33 , pp. 20-26
    • Bienert, G.P.1    Sch ̧ssler, M.D.2    Jahn, T.P.3
  • 5
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Comprehensive state-of-the-art review of metal homeostasis in bacteria.
    • Waldron K.J., and Robinson N.J. How do bacterial cells ensure that metalloproteins get the correct metal?. Nat Rev Microbiol 7 (2009) 25-35. Comprehensive state-of-the-art review of metal homeostasis in bacteria.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 6
    • 34250812094 scopus 로고    scopus 로고
    • Classification of heavy-metal toxicity by human DNA microarray analysis
    • Kawata K., Yokoo H., Shimazaki R., and Okabe S. Classification of heavy-metal toxicity by human DNA microarray analysis. Environ Sci Technol 41 (2007) 3769-3774
    • (2007) Environ Sci Technol , vol.41 , pp. 3769-3774
    • Kawata, K.1    Yokoo, H.2    Shimazaki, R.3    Okabe, S.4
  • 7
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran T.V., and Culotta V.C. Metallochaperones, an intracellular shuttle service for metal ions. J Biol Chem 275 (2000) 25057-25060
    • (2000) J Biol Chem , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 8
    • 34547229278 scopus 로고    scopus 로고
    • Metal sensor proteins: nature's metalloregulated allosteric switches
    • Comprehensive state-of-the-art review of bacterial cytosolic metalloregulators.
    • Giedroc D.P., and Arunkumar A.I. Metal sensor proteins: nature's metalloregulated allosteric switches. Dalton Trans (2007) 3107-3120. Comprehensive state-of-the-art review of bacterial cytosolic metalloregulators.
    • (2007) Dalton Trans , pp. 3107-3120
    • Giedroc, D.P.1    Arunkumar, A.I.2
  • 9
    • 0037903225 scopus 로고    scopus 로고
    • Bacterial silver resistance: molecular biology and uses and misuses of silver compounds
    • Silver S. Bacterial silver resistance: molecular biology and uses and misuses of silver compounds. FEMS Microbiol Rev 27 (2003) 341-353
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 341-353
    • Silver, S.1
  • 10
    • 0242418181 scopus 로고    scopus 로고
    • TRASH: a novel metal-binding domain predicted to be involved in heavy-metal sensing, trafficking and resistance
    • Ettema T.J.G., Huynen M.A., de Vos W.M., and van der Oost J. TRASH: a novel metal-binding domain predicted to be involved in heavy-metal sensing, trafficking and resistance. Trends Biochem Sci 28 (2003) 170-173
    • (2003) Trends Biochem Sci , vol.28 , pp. 170-173
    • Ettema, T.J.G.1    Huynen, M.A.2    de Vos, W.M.3    van der Oost, J.4
  • 11
    • 34250821713 scopus 로고    scopus 로고
    • Contribution of extracytoplasmic function sigma factors to transition metal homeostasis in Cupriavidus metallidurans strain CH34
    • A rich resource of new-to-metalloregulation genes.
    • Grosse C., Friedrich S., and Nies D.H. Contribution of extracytoplasmic function sigma factors to transition metal homeostasis in Cupriavidus metallidurans strain CH34. J Mol Microbiol Biotechnol 12 (2007) 227-240. A rich resource of new-to-metalloregulation genes.
    • (2007) J Mol Microbiol Biotechnol , vol.12
    • Grosse, C.1    Friedrich, S.2    Nies, D.H.3
  • 13
    • 63749083011 scopus 로고    scopus 로고
    • Bacterial transport ATPases for monovalent, divalent and trivalent soft metal ions
    • Edited by Kaplan J., Wada Y., and Futai M. (Eds), Wiley-VCH
    • Wong M.D., Fan B., and Rosen B.P. Bacterial transport ATPases for monovalent, divalent and trivalent soft metal ions. In: Edited by Kaplan J., Wada Y., and Futai M. (Eds). Ion-pumping ATPases: Biochemisry, Cell Biology and Pathophysiology (2003), Wiley-VCH
    • (2003) Ion-pumping ATPases: Biochemisry, Cell Biology and Pathophysiology
    • Wong, M.D.1    Fan, B.2    Rosen, B.P.3
  • 14
    • 0036802691 scopus 로고    scopus 로고
    • Arsenate reductases in prokaryotes and eukaryotes
    • Mukhopadhyay R., and Rosen B.P. Arsenate reductases in prokaryotes and eukaryotes. Environ Health Perspect 110 (2002) 745-748
    • (2002) Environ Health Perspect , vol.110 , pp. 745-748
    • Mukhopadhyay, R.1    Rosen, B.P.2
  • 15
    • 33747357184 scopus 로고    scopus 로고
    • Arsenate reduction: thiol cascade chemistry with convergent evolution
    • Messens J., and Silver S. Arsenate reduction: thiol cascade chemistry with convergent evolution. J Mol Biol 362 (2006) 1-17
    • (2006) J Mol Biol , vol.362 , pp. 1-17
    • Messens, J.1    Silver, S.2
  • 16
    • 34447116980 scopus 로고    scopus 로고
    • ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity
    • Lin Y.F., Yang J., and Rosen B.P. ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity. J Biol Chem 282 (2007) 16783-16791
    • (2007) J Biol Chem , vol.282 , pp. 16783-16791
    • Lin, Y.F.1    Yang, J.2    Rosen, B.P.3
  • 17
    • 38349186555 scopus 로고    scopus 로고
    • ArsD: an As(III) metallochaperone for the ArsAB As(III)-translocating ATPase
    • Lin Y.F., Yang J., and Rosen B.P. ArsD: an As(III) metallochaperone for the ArsAB As(III)-translocating ATPase. J Bioenerg Biomembr 39 (2007) 453-458
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 453-458
    • Lin, Y.F.1    Yang, J.2    Rosen, B.P.3
  • 18
    • 0001775915 scopus 로고    scopus 로고
    • Metalloregulation of soft metal resistance pumps
    • Sarkar B. (Ed), Plenum Press
    • Xu C., and Rosen B.P. Metalloregulation of soft metal resistance pumps. In: Sarkar B. (Ed). Metals and Genetics (1999), Plenum Press 5-19
    • (1999) Metals and Genetics , pp. 5-19
    • Xu, C.1    Rosen, B.P.2
  • 19
    • 20444466105 scopus 로고    scopus 로고
    • Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor
    • Ye J., Kandegedara A., Martin P., and Rosen B.P. Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor. J Bacteriol 187 (2005) 4214-4221
    • (2005) J Bacteriol , vol.187 , pp. 4214-4221
    • Ye, J.1    Kandegedara, A.2    Martin, P.3    Rosen, B.P.4
  • 20
    • 0032536158 scopus 로고    scopus 로고
    • Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins
    • Cook W.J., Kar S.R., Taylor K.B., and Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J Mol Biol 275 (1998) 337-346
    • (1998) J Mol Biol , vol.275 , pp. 337-346
    • Cook, W.J.1    Kar, S.R.2    Taylor, K.B.3    Hall, L.M.4
  • 21
    • 20444447161 scopus 로고    scopus 로고
    • Form and function in metal-dependent transcriptional regulation: dawn of the enlightenment
    • Rensing C. Form and function in metal-dependent transcriptional regulation: dawn of the enlightenment. J Bacteriol 187 (2005) 3909-3912
    • (2005) J Bacteriol , vol.187 , pp. 3909-3912
    • Rensing, C.1
  • 22
    • 0029069508 scopus 로고
    • Metalloregulation of the cyanobacterial smt locus: identification of SmtB binding sites and direct interaction with metals
    • Erbe J.L., Taylor K.B., and Hall L.M. Metalloregulation of the cyanobacterial smt locus: identification of SmtB binding sites and direct interaction with metals. Nucleic Acids Res 23 (1995) 2472-2478
    • (1995) Nucleic Acids Res , vol.23 , pp. 2472-2478
    • Erbe, J.L.1    Taylor, K.B.2    Hall, L.M.3
  • 23
    • 0037174930 scopus 로고    scopus 로고
    • The soft metal ion binding sites in the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor are formed between subunits of the homodimer
    • Wong M.D., Lin Y.F., and Rosen B.P. The soft metal ion binding sites in the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor are formed between subunits of the homodimer. J Biol Chem 277 (2002) 40930-40936
    • (2002) J Biol Chem , vol.277 , pp. 40930-40936
    • Wong, M.D.1    Lin, Y.F.2    Rosen, B.P.3
  • 24
    • 0032833996 scopus 로고    scopus 로고
    • Purification and characterization of MerR, the regulator of the broad-spectrum mercury resistance genes in Streptomyces lividans 1326
    • Rother D., Mattes R., and Altenbuchner J. Purification and characterization of MerR, the regulator of the broad-spectrum mercury resistance genes in Streptomyces lividans 1326. Mol Gen Genet 262 (1999) 154-162
    • (1999) Mol Gen Genet , vol.262 , pp. 154-162
    • Rother, D.1    Mattes, R.2    Altenbuchner, J.3
  • 25
    • 35648990984 scopus 로고    scopus 로고
    • NMR structural analysis of cadmium sensing by winged helix repressor CmtR
    • The first solution structure of a metallated ArsR family member.
    • Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Cavet J.S., Dennison C., Graham A.I., Harvie D.R., and Robinson N.J. NMR structural analysis of cadmium sensing by winged helix repressor CmtR. J Biol Chem 282 (2007) 30181-30188. The first solution structure of a metallated ArsR family member.
    • (2007) J Biol Chem , vol.282 , pp. 30181-30188
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Ciofi-Baffoni, S.4    Cavet, J.S.5    Dennison, C.6    Graham, A.I.7    Harvie, D.R.8    Robinson, N.J.9
  • 26
    • 34547547068 scopus 로고    scopus 로고
    • Identifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coils
    • Touw D.S., Nordman C.E., Stuckey J.A., and Pecoraro V.L. Identifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coils. Proc Natl Acad Sci U S A 104 (2007) 11969-11974
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11969-11974
    • Touw, D.S.1    Nordman, C.E.2    Stuckey, J.A.3    Pecoraro, V.L.4
  • 27
    • 54449094012 scopus 로고    scopus 로고
    • Evolution of metal(loid) binding sites in transcriptional regulators
    • Structural and biochemical analyses demonstrate the protean qualities of the ArsR family.
    • Ordonez E., Thiyagarajan S., Cook J.D., Stemmler T.L., Gil J.A., Mateos L.M., and Rosen B.P. Evolution of metal(loid) binding sites in transcriptional regulators. J Biol Chem 283 (2008) 25706-25714. Structural and biochemical analyses demonstrate the protean qualities of the ArsR family.
    • (2008) J Biol Chem , vol.283 , pp. 25706-25714
    • Ordonez, E.1    Thiyagarajan, S.2    Cook, J.D.3    Stemmler, T.L.4    Gil, J.A.5    Mateos, L.M.6    Rosen, B.P.7
  • 28
    • 36349027677 scopus 로고    scopus 로고
    • Convergent evolution of a new arsenic binding site in the ArsR/SmtB family of metalloregulators
    • Qin J., Fu H.L., Ye J., Bencze K.Z., Stemmler T.L., Rawlings D.E., and Rosen B.P. Convergent evolution of a new arsenic binding site in the ArsR/SmtB family of metalloregulators. J Biol Chem 282 (2007) 34346-34355
    • (2007) J Biol Chem , vol.282 , pp. 34346-34355
    • Qin, J.1    Fu, H.L.2    Ye, J.3    Bencze, K.Z.4    Stemmler, T.L.5    Rawlings, D.E.6    Rosen, B.P.7
  • 30
    • 0038240633 scopus 로고    scopus 로고
    • Bacterial mercury resistance from atoms to ecosystems
    • Barkay T., Miller S.M., and Summers A.O. Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev 27 (2003) 355-384
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 355-384
    • Barkay, T.1    Miller, S.M.2    Summers, A.O.3
  • 32
    • 0345849436 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Ptashne M., and Gann A. Genes & Signals (2002), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2002) Genes & Signals
    • Ptashne, M.1    Gann, A.2
  • 33
    • 0024508489 scopus 로고
    • Transcriptional switching by the metalloregulatory MerR protein: initial characterization of DNA and mercury (II) binding activities
    • Shewchuk L.M., Verdine G.L., and Walsh C.T. Transcriptional switching by the metalloregulatory MerR protein: initial characterization of DNA and mercury (II) binding activities. Biochemistry 28 (1989) 2331-2339
    • (1989) Biochemistry , vol.28 , pp. 2331-2339
    • Shewchuk, L.M.1    Verdine, G.L.2    Walsh, C.T.3
  • 35
    • 2942628401 scopus 로고    scopus 로고
    • Characterization of the MerD protein from Ralstonia metallidurans CH34: a possible role in bacterial mercury resistance by switching off the induction of the mer operon
    • Champier L., Duarte V., Michaud-Soret I., and Coves J. Characterization of the MerD protein from Ralstonia metallidurans CH34: a possible role in bacterial mercury resistance by switching off the induction of the mer operon. Mol Microbiol 52 (2004) 1475-1485
    • (2004) Mol Microbiol , vol.52 , pp. 1475-1485
    • Champier, L.1    Duarte, V.2    Michaud-Soret, I.3    Coves, J.4
  • 37
    • 34447108172 scopus 로고    scopus 로고
    • 19F-NMR reveals metal- and operator-induced allostery in MerR
    • Indentification of the interprotomer allosteric signally path and first demonstration of operator modulation of regulator metal binding site.
    • Song L., Teng Q., Brewer J., Phillips R.S., and Summers A.O. 19F-NMR reveals metal- and operator-induced allostery in MerR. J Mol Biol 371 (2007) 79-92. Indentification of the interprotomer allosteric signally path and first demonstration of operator modulation of regulator metal binding site.
    • (2007) J Mol Biol , vol.371 , pp. 79-92
    • Song, L.1    Teng, Q.2    Brewer, J.3    Phillips, R.S.4    Summers, A.O.5
  • 38
    • 0032612908 scopus 로고    scopus 로고
    • Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response
    • Demple B., Hidalgo E., and Ding H. Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response. Biochem Soc Symp 64 (1999) 119-128
    • (1999) Biochem Soc Symp , vol.64 , pp. 119-128
    • Demple, B.1    Hidalgo, E.2    Ding, H.3
  • 39
    • 41649117130 scopus 로고    scopus 로고
    • DNA binding shifts the redox potential of the transcription factor SoxR
    • Second demonstration of operator DNA modulation of a regulator's metal binding site.
    • Gorodetsky A.A., Dietrich L.E., Lee P.E., Demple B., Newman D.K., and Barton J.K. DNA binding shifts the redox potential of the transcription factor SoxR. Proc Natl Acad Sci U S A 105 (2008) 3684-3689. Second demonstration of operator DNA modulation of a regulator's metal binding site.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3684-3689
    • Gorodetsky, A.A.1    Dietrich, L.E.2    Lee, P.E.3    Demple, B.4    Newman, D.K.5    Barton, J.K.6
  • 40
    • 68449099013 scopus 로고    scopus 로고
    • Lead(II) resistance in Cupriavidus metallidurans CH34: interplay between plasmid and chromosomally-located functions
    • in press, doi:10.1007/s10482-008-9289-0
    • Taghavi S., Lesaulnier C., Monchy S., Wattiez R., Mergeay M., and van der Lelie D. Lead(II) resistance in Cupriavidus metallidurans CH34: interplay between plasmid and chromosomally-located functions. Antonie Van Leeuwenhoek (2009) in press, doi:10.1007/s10482-008-9289-0
    • (2009) Antonie Van Leeuwenhoek
    • Taghavi, S.1    Lesaulnier, C.2    Monchy, S.3    Wattiez, R.4    Mergeay, M.5    van der Lelie, D.6
  • 43
    • 43749099051 scopus 로고    scopus 로고
    • Expression, purification, and crystallization and preliminary X-ray crystallographic analysis of CnrX from Cupriavidus metallidurans CH34
    • Kim K.H., Jung E.J., Im H., Lelie D.V., and Kim E.E. Expression, purification, and crystallization and preliminary X-ray crystallographic analysis of CnrX from Cupriavidus metallidurans CH34. J Microbiol Biotechnol 18 (2008) 43-47
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 43-47
    • Kim, K.H.1    Jung, E.J.2    Im, H.3    Lelie, D.V.4    Kim, E.E.5
  • 46
    • 0141591471 scopus 로고    scopus 로고
    • Genetic identification of a respiratory arsenate reductase
    • Saltikov C.W., and Newman D.K. Genetic identification of a respiratory arsenate reductase. Proc Natl Acad Sci U S A 100 (2003) 10983-10988
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10983-10988
    • Saltikov, C.W.1    Newman, D.K.2
  • 47
    • 0038220925 scopus 로고    scopus 로고
    • The ars detoxification system is advantageous but not required for As(V) respiration by the genetically tractable Shewanella species strain ANA-3
    • Saltikov C.W., Cifuentes A., Venkateswaran K., and Newman D.K. The ars detoxification system is advantageous but not required for As(V) respiration by the genetically tractable Shewanella species strain ANA-3. Appl Environ Microbiol 69 (2003) 2800-2809
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2800-2809
    • Saltikov, C.W.1    Cifuentes, A.2    Venkateswaran, K.3    Newman, D.K.4
  • 49
    • 33746105720 scopus 로고    scopus 로고
    • Identification of genes and proteins involved in the pleiotropic response to arsenic stress in Caenibacter arsenoxydans, a metalloresistant beta-proteobacterium with an unsequenced genome
    • Carapito C., Muller D., Turlin E., Koechler S., Danchin A., Van Dorsselaer A., Leize-Wagner E., Bertin P.N., and Lett M.C. Identification of genes and proteins involved in the pleiotropic response to arsenic stress in Caenibacter arsenoxydans, a metalloresistant beta-proteobacterium with an unsequenced genome. Biochimie 88 (2006) 595-606
    • (2006) Biochimie , vol.88 , pp. 595-606
    • Carapito, C.1    Muller, D.2    Turlin, E.3    Koechler, S.4    Danchin, A.5    Van Dorsselaer, A.6    Leize-Wagner, E.7    Bertin, P.N.8    Lett, M.C.9
  • 50
    • 33144480276 scopus 로고    scopus 로고
    • Arsenic detoxification and evolution of trimethylarsine gas by a microbial arsenite S-adenosylmethionine methyltransferase
    • Qin J., Rosen B.P., Zhang Y., Wang G., Franke S., and Rensing C. Arsenic detoxification and evolution of trimethylarsine gas by a microbial arsenite S-adenosylmethionine methyltransferase. Proc Natl Acad Sci U S A 103 (2006) 2075-2080
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2075-2080
    • Qin, J.1    Rosen, B.P.2    Zhang, Y.3    Wang, G.4    Franke, S.5    Rensing, C.6
  • 52
    • 48349127075 scopus 로고    scopus 로고
    • Enterobacter cloacae SLD1a-1 gains a selective advantage from selenate reduction when growing in nitrate-depleted anaerobic environments
    • Leaver J.T., Richardson D.J., and Butler C.S. Enterobacter cloacae SLD1a-1 gains a selective advantage from selenate reduction when growing in nitrate-depleted anaerobic environments. J Ind Microbiol Biotechnol 35 (2008) 867-873
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 867-873
    • Leaver, J.T.1    Richardson, D.J.2    Butler, C.S.3
  • 53
    • 33644862744 scopus 로고    scopus 로고
    • Expression of the ubiE gene of Geobacillus stearothermophilus V in Escherichia coli K-12 mediates the evolution of selenium compounds into the headspace of selenite- and selenate-amended cultures
    • Swearingen Jr. J.W., Fuentes D.E., Araya M.A., Plishker M.F., Saavedra C.P., Chasteen T.G., and Vasquez C.C. Expression of the ubiE gene of Geobacillus stearothermophilus V in Escherichia coli K-12 mediates the evolution of selenium compounds into the headspace of selenite- and selenate-amended cultures. Appl Environ Microbiol 72 (2006) 963-967
    • (2006) Appl Environ Microbiol , vol.72 , pp. 963-967
    • Swearingen Jr., J.W.1    Fuentes, D.E.2    Araya, M.A.3    Plishker, M.F.4    Saavedra, C.P.5    Chasteen, T.G.6    Vasquez, C.C.7
  • 54
    • 46249109847 scopus 로고    scopus 로고
    • Trends in selenium utilization in marine microbial world revealed through the analysis of the global ocean sampling (GOS) project
    • Zhang Y., and Gladyshev V.N. Trends in selenium utilization in marine microbial world revealed through the analysis of the global ocean sampling (GOS) project. PLoS Genet 4 (2008) e1000095
    • (2008) PLoS Genet , vol.4
    • Zhang, Y.1    Gladyshev, V.N.2
  • 55
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance
    • Busenlehner L.S., Pennella M.A., and Giedroc D.P. The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol Rev 27 (2003) 131-143
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 56
    • 0001476958 scopus 로고
    • Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium-efflux ATPase
    • Nucifora G., Chu L., Misra T.K., and Silver S. Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium-efflux ATPase. Proc Natl Acad Sci U S A 86 (1989) 3544-3548
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3544-3548
    • Nucifora, G.1    Chu, L.2    Misra, T.K.3    Silver, S.4
  • 57
    • 0036321752 scopus 로고    scopus 로고
    • Membrane topolocy of the pI258 CadA Cd(II)/Pb(II)/Zn(II)-translocating P-type ATPase
    • Tsai K.J., Lin Y.F., Wong M.D., Yang H.H.C., Fu H.L., and Rosen B.P. Membrane topolocy of the pI258 CadA Cd(II)/Pb(II)/Zn(II)-translocating P-type ATPase. J Bionerg Biomembr 34 (2002) 147-156
    • (2002) J Bionerg Biomembr , vol.34 , pp. 147-156
    • Tsai, K.J.1    Lin, Y.F.2    Wong, M.D.3    Yang, H.H.C.4    Fu, H.L.5    Rosen, B.P.6
  • 58
    • 0242582330 scopus 로고    scopus 로고
    • A cadmium-lead-sensing ArsR-SmtB repressor with novel sensory sites. Complementary metal discrimination by NmtR AND CmtR in a common cytosol
    • Cavet J.S., Graham A.I., Meng W., and Robinson N.J. A cadmium-lead-sensing ArsR-SmtB repressor with novel sensory sites. Complementary metal discrimination by NmtR AND CmtR in a common cytosol. J Biol Chem 278 (2003) 44560-44566
    • (2003) J Biol Chem , vol.278 , pp. 44560-44566
    • Cavet, J.S.1    Graham, A.I.2    Meng, W.3    Robinson, N.J.4
  • 59
    • 21744460226 scopus 로고    scopus 로고
    • Structural and functional characterization of Mycobacterium tuberculosis CmtR, a PbII/CdII-sensing SmtB/ArsR metalloregulatory repressor
    • Wang Y., Hemmingsen L., and Giedroc D.P. Structural and functional characterization of Mycobacterium tuberculosis CmtR, a PbII/CdII-sensing SmtB/ArsR metalloregulatory repressor. Biochemistry 44 (2005) 8976-8988
    • (2005) Biochemistry , vol.44 , pp. 8976-8988
    • Wang, Y.1    Hemmingsen, L.2    Giedroc, D.P.3
  • 60
    • 53249086198 scopus 로고    scopus 로고
    • 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., and Giedroc D.P. A Cu(I)-sensing ArsR family metal sensor protein with a relaxed metal selectivity profile. Biochemistry 47 (2008) 10564-10575
    • (2008) Biochemistry , vol.47 , pp. 10564-10575
    • Liu, T.1    Chen, X.2    Ma, Z.3    Shokes, J.4    Hemmingsen, L.5    Scott, R.A.6    Giedroc, D.P.7
  • 61
    • 0035320841 scopus 로고    scopus 로고
    • Chromosomal locus for cadmium resistance in Pseudomonas putida consisting of a cadmium-transporting ATPase and a MerR family response regulator
    • Lee S.W., Glickmann E., and Cooksey D.A. Chromosomal locus for cadmium resistance in Pseudomonas putida consisting of a cadmium-transporting ATPase and a MerR family response regulator. Appl Environ Microbiol 67 (2001) 1437-1444
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1437-1444
    • Lee, S.W.1    Glickmann, E.2    Cooksey, D.A.3
  • 62
    • 35448961704 scopus 로고    scopus 로고
    • GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon
    • Pontel L.B., Audero M.E., Espariz M., Checa S.K., and Soncini F.C. GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon. Mol Microbiol 66 (2007) 814-825
    • (2007) Mol Microbiol , vol.66 , pp. 814-825
    • Pontel, L.B.1    Audero, M.E.2    Espariz, M.3    Checa, S.K.4    Soncini, F.C.5
  • 63
    • 0034811821 scopus 로고    scopus 로고
    • Cloning and functional analysis of the pbr lead resistance determinant of Ralstonia metallidurans CH34
    • Borremans B., Hobman J.L., Provoost A., Brown N.L., and van Der Lelie D. Cloning and functional analysis of the pbr lead resistance determinant of Ralstonia metallidurans CH34. J Bacteriol 183 (2001) 5651-5658
    • (2001) J Bacteriol , vol.183 , pp. 5651-5658
    • Borremans, B.1    Hobman, J.L.2    Provoost, A.3    Brown, N.L.4    van Der Lelie, D.5
  • 64
    • 47349108178 scopus 로고    scopus 로고
    • Expression of chromate resistance genes from Shewanella sp. strain ANA-3 in Escherichia coli
    • Aguilar-Barajas E., Paluscio E., Cervantes C., and Rensing C. Expression of chromate resistance genes from Shewanella sp. strain ANA-3 in Escherichia coli. FEMS Microbiol Lett 285 (2008) 97-100
    • (2008) FEMS Microbiol Lett , vol.285 , pp. 97-100
    • Aguilar-Barajas, E.1    Paluscio, E.2    Cervantes, C.3    Rensing, C.4
  • 65
    • 51849150398 scopus 로고    scopus 로고
    • Transcriptome analysis reveals response regulator SO2426-mediated gene expression in Shewanella oneidensis MR-1 under chromate challenge
    • Chourey K., Wei W., Wan X.F., and Thompson D.K. Transcriptome analysis reveals response regulator SO2426-mediated gene expression in Shewanella oneidensis MR-1 under chromate challenge. BMC Genomics 9 (2008) 395
    • (2008) BMC Genomics , vol.9 , pp. 395
    • Chourey, K.1    Wei, W.2    Wan, X.F.3    Thompson, D.K.4
  • 66
    • 55749085128 scopus 로고    scopus 로고
    • The chromate-inducible chrBACF operon from the transposable element TnOtChr confers resistance to chromium(VI) and superoxide
    • Branco R., Chung A.P., Johnston T., Gurel V., Morais P., and Zhitkovich A. The chromate-inducible chrBACF operon from the transposable element TnOtChr confers resistance to chromium(VI) and superoxide. J Bacteriol 190 (2008) 6996-7003
    • (2008) J Bacteriol , vol.190 , pp. 6996-7003
    • Branco, R.1    Chung, A.P.2    Johnston, T.3    Gurel, V.4    Morais, P.5    Zhitkovich, A.6
  • 67
    • 68449097696 scopus 로고    scopus 로고
    • Cupriavidus metallidurans: evolution of a metal-resistant bacterium
    • in press, doi:10.1007/s10482-008-9284-5
    • von Rozycki T., and Nies D.H. Cupriavidus metallidurans: evolution of a metal-resistant bacterium. Antonie Van Leeuwenhoek (2009) in press, doi:10.1007/s10482-008-9284-5
    • (2009) Antonie Van Leeuwenhoek
    • von Rozycki, T.1    Nies, D.H.2
  • 68
    • 0033105190 scopus 로고    scopus 로고
    • Bacterial tellurite resistance
    • Taylor D.E. Bacterial tellurite resistance. Trends Microbiol 7 (1999) 111-115
    • (1999) Trends Microbiol , vol.7 , pp. 111-115
    • Taylor, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.