메뉴 건너뛰기




Volumn 27, Issue 2-3, 2003, Pages 165-181

Zn, Cu and Co in cyanobacteria: Selective control of metal availability

Author keywords

Metallochaperone; Metallothionein; P1 type ATPase; Synechococcus PCC 7942; Synechocystis PCC 6803; Thylakoid copper

Indexed keywords

COBALAMIN; COPPER ION; CYTOCHROME C OXIDASE; ZINC ION;

EID: 0038579428     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(03)00050-0     Document Type: Review
Times cited : (161)

References (114)
  • 2
    • 0030942832 scopus 로고    scopus 로고
    • HIP1 propagates in cyanobacterial DNA via nucleotide substitutions but promotes excision at similar frequencies in Escherichia coli and Synechococcus PCC 7942
    • Robinson P.J., Cranenburgh R.M., Head I.M., Robinson N.J. HIP1 propagates in cyanobacterial DNA via nucleotide substitutions but promotes excision at similar frequencies in Escherichia coli and Synechococcus PCC 7942. Mol. Microbiol. 24:1997;181-189.
    • (1997) Mol. Microbiol. , vol.24 , pp. 181-189
    • Robinson, P.J.1    Cranenburgh, R.M.2    Head, I.M.3    Robinson, N.J.4
  • 6
    • 0035850909 scopus 로고    scopus 로고
    • Oceans. Dis-crediting ocean fertilization
    • Chisholm S.W., Falkowski P.G., Cullen J.J. Oceans. Dis-crediting ocean fertilization. Science. 294:2001;309-310.
    • (2001) Science , vol.294 , pp. 309-310
    • Chisholm, S.W.1    Falkowski, P.G.2    Cullen, J.J.3
  • 7
    • 0038230064 scopus 로고
    • Zinc and plants in rivers and streams
    • Shubert L.E., Ed. Academic Press, London
    • Whitton, B.A. (1980) Zinc and plants in rivers and streams. In: Algae as Ecological Indicators (Shubert L.E., Ed.), pp. 257-280. Academic Press, London.
    • (1980) Algae as Ecological Indicators , pp. 257-280
    • Whitton, B.A.1
  • 8
    • 0003994832 scopus 로고
    • Oxford University Press, Oxford
    • Clark, R.B. (1992) Marine Pollution. Oxford University Press, Oxford.
    • (1992) Marine Pollution
    • Clark, R.B.1
  • 9
    • 0017413212 scopus 로고
    • Influence of zinc on lotic plants. II. Environmental effects on toxicity of zinc to Hormidium rivulare
    • Say P.J., Whitton B.A. Influence of zinc on lotic plants. II. Environmental effects on toxicity of zinc to Hormidium rivulare. Freshwater Biol. 7:1977;377-384.
    • (1977) Freshwater Biol. , vol.7 , pp. 377-384
    • Say, P.J.1    Whitton, B.A.2
  • 10
    • 0003004104 scopus 로고
    • Zinc tolerance in strains of the blue green alga Anacystis nidulans
    • Shehata F.H.A., Whitton B.A. Zinc tolerance in strains of the blue green alga Anacystis nidulans. Br. Phycol. J. 17:1982;5-12.
    • (1982) Br. Phycol. J. , vol.17 , pp. 5-12
    • Shehata, F.H.A.1    Whitton, B.A.2
  • 11
    • 0020097167 scopus 로고
    • Uptake of heavy metals by Plectonema boryanum (Cyanophyceae) into cellular compartments, especially polyphosphate bodies: An X-ray energy dispersive study
    • Jensen T.E., Baxter M., Rachlin J.W., Jani V. Uptake of heavy metals by Plectonema boryanum (Cyanophyceae) into cellular compartments, especially polyphosphate bodies: An X-ray energy dispersive study. Environ. Pollut. (Ser. A). 27:1982;119-127.
    • (1982) Environ. Pollut. (Ser. A) , vol.27 , pp. 119-127
    • Jensen, T.E.1    Baxter, M.2    Rachlin, J.W.3    Jani, V.4
  • 13
    • 0029027150 scopus 로고
    • Molecular identification of an ABC transporter complex for manganese: Analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process
    • Bartsevich V.V., Pakrasi H.B. Molecular identification of an ABC transporter complex for manganese: analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process. EMBO J. 14:1995;1845-1853.
    • (1995) EMBO J. , vol.14 , pp. 1845-1853
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 14
    • 0029975786 scopus 로고    scopus 로고
    • Manganese transport in the cyanobacterium Synechocystis sp. PCC 6803
    • Bartsevich V.V., Pakrasi H.B. Manganese transport in the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 271:1996;26057-26061.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26057-26061
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 15
    • 0037047393 scopus 로고    scopus 로고
    • A two-component signal transduction pathway regulates manganese homeostasis in Synechocystis 6803, a photosynthetic organism
    • Ogawa T., Bao D.H., Katoh H., Shibata M., Pakrasi H.B., Bhattacharyya-Pakrasi M. A two-component signal transduction pathway regulates manganese homeostasis in Synechocystis 6803, a photosynthetic organism. J. Biol. Chem. 277:2002;28981-28986.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28981-28986
    • Ogawa, T.1    Bao, D.H.2    Katoh, H.3    Shibata, M.4    Pakrasi, H.B.5    Bhattacharyya-Pakrasi, M.6
  • 17
    • 0034658505 scopus 로고    scopus 로고
    • The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii
    • Moseley J., Quinn J., Eriksson M., Merchant S. The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. EMBO J. 19:2000;2139-2151.
    • (2000) EMBO J. , vol.19 , pp. 2139-2151
    • Moseley, J.1    Quinn, J.2    Eriksson, M.3    Merchant, S.4
  • 18
    • 0026782111 scopus 로고
    • Copper-mediated regulation of cytochrome c553 and plastocyanin in the cyanobacterium Synechocystis 6803
    • Zhang L., McSpadden B., Pakrasi H.B., Whitmarsh J. Copper-mediated regulation of cytochrome c553 and plastocyanin in the cyanobacterium Synechocystis 6803. J. Biol. Chem. 267:1992;19054-19059.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19054-19059
    • Zhang, L.1    McSpadden, B.2    Pakrasi, H.B.3    Whitmarsh, J.4
  • 19
    • 0025780587 scopus 로고
    • The interactions of duroquinol, dbmib and nqno with the chloroplast cytochrome-bf complex
    • Rich P.R., Madgwick S.A., Moss D.A. The interactions of duroquinol, dbmib and nqno with the chloroplast cytochrome-bf complex. Biochim. Biophys. Acta. 1058:1991;312-328.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 312-328
    • Rich, P.R.1    Madgwick, S.A.2    Moss, D.A.3
  • 20
    • 0001321652 scopus 로고
    • Kinetic-studies of electron-transfer in a hybrid system constructed from the cytochrome bf complex and photosystem-I
    • Rich P.R., Heathcote P., Moss D.A. Kinetic-studies of electron-transfer in a hybrid system constructed from the cytochrome bf complex and photosystem-I. Biochim. Biophys. Acta. 892:1987;138-151.
    • (1987) Biochim. Biophys. Acta , vol.892 , pp. 138-151
    • Rich, P.R.1    Heathcote, P.2    Moss, D.A.3
  • 21
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein
    • Bogsch E., Brink S., Robinson C. Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein. EMBO J. 16:1997;3851-3859.
    • (1997) EMBO J. , vol.16 , pp. 3851-3859
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 22
    • 0002842013 scopus 로고
    • Functional and immunological characterization of both 'mitochondria-like' and 'chloroplast-like' electron/proton transport proteins in isolated and purified cyanobacterial membranes
    • Dworsky A., Mayer B., Regelsberger G., Fromwald S., Peschek G.A. Functional and immunological characterization of both 'mitochondria-like' and 'chloroplast-like' electron/proton transport proteins in isolated and purified cyanobacterial membranes. Bioelectrochem. Bioenerg. 38:1995;35-43.
    • (1995) Bioelectrochem. Bioenerg. , vol.38 , pp. 35-43
    • Dworsky, A.1    Mayer, B.2    Regelsberger, G.3    Fromwald, S.4    Peschek, G.A.5
  • 23
    • 0028360414 scopus 로고
    • A copper-transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus species PCC 7942
    • Kanamaru K., Kashiwagi S., Mizuno T. A copper-transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus species PCC 7942. Mol. Microbiol. 13:1994;369-377.
    • (1994) Mol. Microbiol. , vol.13 , pp. 369-377
    • Kanamaru, K.1    Kashiwagi, S.2    Mizuno, T.3
  • 24
    • 0027937063 scopus 로고
    • P-type ATPase from the cyanobacterium Synechococcus 7942 related to the human Menkes and Wilson disease gene products
    • Phung L.T., Ajlani G., Haselkorn R. P-type ATPase from the cyanobacterium Synechococcus 7942 related to the human Menkes and Wilson disease gene products. Proc. Natl. Acad. Sci. USA. 91:1994;9651-9654.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9651-9654
    • Phung, L.T.1    Ajlani, G.2    Haselkorn, R.3
  • 25
    • 0035827547 scopus 로고    scopus 로고
    • Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803
    • Tottey S., Rich P.R., Rondet S.A., Robinson N.J. Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803. J. Biol. Chem. 276:2001;19999-20004.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19999-20004
    • Tottey, S.1    Rich, P.R.2    Rondet, S.A.3    Robinson, N.J.4
  • 27
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt A., Suter H., Krapf R., Solioz M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268:1993;12775-12779.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 28
    • 0030820818 scopus 로고    scopus 로고
    • Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway
    • Yuan D.S., Dancis A., Klausner R.D. Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway. J. Biol. Chem. 272:1997;25787-25793.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25787-25793
    • Yuan, D.S.1    Dancis, A.2    Klausner, R.D.3
  • 29
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris M.J., Mercer J.F., Culvenor J.G., Lockhart P., Gleeson P.A., Camakaris J. Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J. 15:1996;6084-6095.
    • (1996) EMBO J. , vol.15 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 30
    • 0030803730 scopus 로고    scopus 로고
    • Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae
    • Hung I.H., Suzuki M., Yamaguchi Y., Yuan D.S., Klausner R.D., Gitlin J.D. Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 272:1997;21461-21466.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21461-21466
    • Hung, I.H.1    Suzuki, M.2    Yamaguchi, Y.3    Yuan, D.S.4    Klausner, R.D.5    Gitlin, J.D.6
  • 31
    • 0037085443 scopus 로고    scopus 로고
    • A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer and alternative sites for copper acquisition
    • Tottey S., Rondet S.A., Borrelly G.P., Robinson P.J., Rich P.R., Robinson N.J. A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer and alternative sites for copper acquisition. J. Biol. Chem. 277:2002;5490-5497.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5490-5497
    • Tottey, S.1    Rondet, S.A.2    Borrelly, G.P.3    Robinson, P.J.4    Rich, P.R.5    Robinson, N.J.6
  • 33
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae T.D., Schmidt P.J., Pufahl R.A., Culotta V.C., O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science. 284:1999;805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 34
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten C.E., O'Halloran T.V. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science. 292:2001;2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 35
    • 0035117191 scopus 로고    scopus 로고
    • Copper delivery by metallochaperone proteins
    • Rosenzweig A.C. Copper delivery by metallochaperone proteins. Acc. Chem. Res. 34:2001;119-128.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 119-128
    • Rosenzweig, A.C.1
  • 36
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran T.V., 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
  • 38
    • 0030877175 scopus 로고    scopus 로고
    • Metallocenter assembly in nickel-containing enzymes
    • Hausinger R.P. Metallocenter assembly in nickel-containing enzymes. J. Biol. Inorg. Chem. 2:1997;279-286.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 279-286
    • Hausinger, R.P.1
  • 39
    • 0038203196 scopus 로고    scopus 로고
    • Nickel uptake and utilisation by microrganisms
    • Mulrooney S.B., Hausinger R.P. Nickel uptake and utilisation by microrganisms. FEMS Microbiol. Rev. 27:2003;000-000.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 000-000
    • Mulrooney, S.B.1    Hausinger, R.P.2
  • 41
    • 0031796990 scopus 로고    scopus 로고
    • Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: The 'phantom' subunit and the possible role of Lys7p
    • Lyons T.J., Nerissian A., Goto J.J., Zhu H., Gralla E.B., Valentine J.S. Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: the 'phantom' subunit and the possible role of Lys7p. J. Biol. Inorg. Chem. 3:1998;650-662.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 650-662
    • Lyons, T.J.1    Nerissian, A.2    Goto, J.J.3    Zhu, H.4    Gralla, E.B.5    Valentine, J.S.6
  • 44
    • 0031452147 scopus 로고    scopus 로고
    • Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle
    • Beers J., Glerum D.M., Tzagoloff A. Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle. J. Biol. Chem. 272:1997;33191-33196.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33191-33196
    • Beers, J.1    Glerum, D.M.2    Tzagoloff, A.3
  • 45
    • 0035936586 scopus 로고    scopus 로고
    • The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex
    • Heaton D.N., George G.N., Garrison G., Winge D.R. The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. Biochemistry. 40:2001;743-751.
    • (2001) Biochemistry , vol.40 , pp. 743-751
    • Heaton, D.N.1    George, G.N.2    Garrison, G.3    Winge, D.R.4
  • 46
    • 0030910597 scopus 로고    scopus 로고
    • A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport
    • Lin S.J., Pufahl R.A., Dancis A., O'Halloran T.V., Culotta V.C. A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J. Biol. Chem. 272:1997;9215-9220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9215-9220
    • Lin, S.J.1    Pufahl, R.A.2    Dancis, A.3    O'Halloran, T.V.4    Culotta, V.C.5
  • 47
    • 0030671295 scopus 로고    scopus 로고
    • Delivering copper inside yeast and human cells
    • Valentine J.S., Gralla E.B. Delivering copper inside yeast and human cells. Science. 278:1997;817-818.
    • (1997) Science , vol.278 , pp. 817-818
    • Valentine, J.S.1    Gralla, E.B.2
  • 48
    • 0035913995 scopus 로고    scopus 로고
    • Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance
    • Multhaup G., Strausak D., Bissig K.-D., Solioz M. Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance. Biochem. Biophys. Res. Commun. 288:2001;172-177.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 172-177
    • Multhaup, G.1    Strausak, D.2    Bissig, K.-D.3    Solioz, M.4
  • 50
    • 0037035530 scopus 로고    scopus 로고
    • Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: Metal coordination environments and protein interactions
    • Cobine P.A., George G.N., Jones C.E., Wickramasinghe W.A., Solioz M., Dameron C.T. Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions. Biochemistry. 41:2002;5822-5829.
    • (2002) Biochemistry , vol.41 , pp. 5822-5829
    • Cobine, P.A.1    George, G.N.2    Jones, C.E.3    Wickramasinghe, W.A.4    Solioz, M.5    Dameron, C.T.6
  • 51
    • 0028938093 scopus 로고
    • Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae
    • Odermatt A., Solioz M. Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae. J. Biol. Chem. 270:1995;4349-4354.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4349-4354
    • Odermatt, A.1    Solioz, M.2
  • 52
    • 0036403247 scopus 로고    scopus 로고
    • Bacterial copper transport
    • Lu Z.H., Solioz M. Bacterial copper transport. Adv. Protein Chem. 60:2002;93-121.
    • (2002) Adv. Protein Chem. , vol.60 , pp. 93-121
    • Lu, Z.H.1    Solioz, M.2
  • 53
    • 0035914375 scopus 로고    scopus 로고
    • Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase
    • Torres A.S., Petri V., Rae T.D., O'Halloran T.V. Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase. J. Biol. Chem. 276:2001;38410-38416.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38410-38416
    • Torres, A.S.1    Petri, V.2    Rae, T.D.3    O'Halloran, T.V.4
  • 54
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb A.L., Torres A.S., O'Halloran T.V., Rosenzweig A.C. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat. Struct. Biol. 8:2001;751-755.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 56
    • 0035798652 scopus 로고    scopus 로고
    • Characterization of the binding interface between the copper metallochaperone Atx1 and the first cytosolic domain of Ccc2 ATPase
    • Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Huffman D.L., O'Halloran T.V. Characterization of the binding interface between the copper metallochaperone Atx1 and the first cytosolic domain of Ccc2 ATPase. J. Biol. Chem. 276:2001;41365-41376.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41365-41376
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 57
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • Huffman D.L., O'Halloran T.V. Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2. J. Biol. Chem. 275:2000;18611-18614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 58
    • 0035910261 scopus 로고    scopus 로고
    • The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
    • Tsivkovskii R., MacArthur B.C., Lutsenko S. The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner. J. Biol. Chem. 276:2001;2234-2242.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2234-2242
    • Tsivkovskii, R.1    MacArthur, B.C.2    Lutsenko, S.3
  • 59
    • 0034637471 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
    • Patzer S.I., Hantke K. The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J. Biol. Chem. 275:2000;24321-24332.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24321-24332
    • Patzer, S.I.1    Hantke, K.2
  • 60
    • 0008218838 scopus 로고    scopus 로고
    • Metal metabolism and toxicity: Repetitive DNA
    • Whitton, B.A. and Potts, M., Eds. Kluwer Academic, Dordrecht
    • Robinson, N.J., Rutherford, J.C., Pocock, M.R. and Cavet, J.S. (2000) Metal metabolism and toxicity: Repetitive DNA. In: The Ecology of Cyanobacteria (Whitton, B.A. and Potts, M., Eds.), pp. 443-463. Kluwer Academic, Dordrecht.
    • (2000) The Ecology of Cyanobacteria , pp. 443-463
    • Robinson, N.J.1    Rutherford, J.C.2    Pocock, M.R.3    Cavet, J.S.4
  • 63
    • 0027434568 scopus 로고
    • Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions
    • Huckle J.W., Morby A.P., Turner J.S., Robinson N.J. Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions. Mol. Microbiol. 7:1993;177-187.
    • (1993) Mol. Microbiol. , vol.7 , pp. 177-187
    • Huckle, J.W.1    Morby, A.P.2    Turner, J.S.3    Robinson, N.J.4
  • 64
    • 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., 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
  • 65
    • 0027247583 scopus 로고
    • SmtB is a metal regulated repressor of the cyanobacterial metallothionein gene smtA: Identification of a Zn inhibited DNA-protein complex
    • Morby A.P., Turner J.S., Huckle J.W., Robinson N.J. SmtB is a metal regulated repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 21:1993;921-925.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 921-925
    • Morby, A.P.1    Turner, J.S.2    Huckle, J.W.3    Robinson, N.J.4
  • 66
    • 0029662326 scopus 로고    scopus 로고
    • 2+-sensing by the cyanobacterial metallothionein repressor SmtB: Different motifs mediate metal-induced protein-DNA dissociation
    • 2+-sensing by the cyanobacterial metallothionein repressor SmtB: different motifs mediate metal-induced protein-DNA dissociation. Nucleic Acids Res. 24:1996;3714-3721.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3714-3721
    • Turner, J.S.1    Glands, P.D.2    Samson, A.C.R.3    Robinson, N.J.4
  • 68
    • 0029261948 scopus 로고
    • 2+-tolerant cyanobacteria with a modified metallothionein divergon: Further analysis of the function and regulation of smt
    • 2+-tolerant cyanobacteria with a modified metallothionein divergon: Further analysis of the function and regulation of smt. J. Ind. Microbiol. 14:1995;259-264.
    • (1995) J. Ind. Microbiol. , vol.14 , pp. 259-264
    • Turner, J.S.1    Robinson, N.J.2    Gupta, A.3
  • 70
    • 0002093183 scopus 로고    scopus 로고
    • Metallothionein gene regulation in cyanobacteria
    • Silver, S. and Walden, W., Eds. Chapman and Hall, London
    • Robinson, N.J., Bird, A.J. and Turner, J.S. (1998) Metallothionein gene regulation in cyanobacteria. In: Metal Ions in Gene Regulation (Silver, S. and Walden, W., Eds.), pp. 372-397. Chapman and Hall, London.
    • (1998) Metal Ions in Gene Regulation , pp. 372-397
    • Robinson, N.J.1    Bird, A.J.2    Turner, J.S.3
  • 72
    • 0029004281 scopus 로고
    • Cyanobacterial metallothioneins: Biochemistry and molecular genetics
    • Turner J.S., Robinson N.J. Cyanobacterial metallothioneins: biochemistry and molecular genetics. J. Ind. Microbiol. 14:1995;119-125.
    • (1995) J. Ind. Microbiol. , vol.14 , pp. 119-125
    • Turner, J.S.1    Robinson, N.J.2
  • 73
    • 0023889538 scopus 로고
    • Primary- and secondary-structural analysis of a unique prokaryotic metallothionein from a Synechococcus sp. cyanobacterium
    • Olafson R.W., McCubbin W.D., Kay C.M. Primary- and secondary-structural analysis of a unique prokaryotic metallothionein from a Synechococcus sp. cyanobacterium. Biochem. J. 251:1988;691-699.
    • (1988) Biochem. J. , vol.251 , pp. 691-699
    • Olafson, R.W.1    McCubbin, W.D.2    Kay, C.M.3
  • 76
    • 0026353521 scopus 로고
    • Overview of metallothioneins
    • Kägi J.H.R. Overview of metallothioneins. Methods Enzymol. 205:1991;613-626.
    • (1991) Methods Enzymol. , vol.205 , pp. 613-626
    • Kägi, J.H.R.1
  • 77
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter R.D. The elusive function of metallothioneins. Proc. Natl. Acad. Sci. USA. 95:1998;8428-8430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 78
    • 0035713724 scopus 로고    scopus 로고
    • The 'metal transcription factor' MTF-1: Biological facts and medical implications
    • Lichtlen P., Schaffner W. The 'metal transcription factor' MTF-1: biological facts and medical implications. Swiss Med. Wkly. 131:2001;647-652.
    • (2001) Swiss Med. Wkly. , vol.131 , pp. 647-652
    • Lichtlen, P.1    Schaffner, W.2
  • 79
    • 0026353520 scopus 로고
    • Determination of the three-dimensional structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution
    • Wüthrich K. Determination of the three-dimensional structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution. Methods Enzymol. 205:1991;502-520.
    • (1991) Methods Enzymol. , vol.205 , pp. 502-520
    • Wüthrich, K.1
  • 80
    • 0026349826 scopus 로고
    • X-ray structure of metallothionein
    • Robbins A.H., Stout C.D. X-ray structure of metallothionein. Methods Enzymol. 205:1991;485-502.
    • (1991) Methods Enzymol. , vol.205 , pp. 485-502
    • Robbins, A.H.1    Stout, C.D.2
  • 81
    • 0026647117 scopus 로고
    • Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy
    • Messerle B.A., Schaffer A., Vasak M., Kägi J.H., Wüthrich K. Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy. J. Mol. Biol. 225:1992;433-443.
    • (1992) J. Mol. Biol. , vol.225 , pp. 433-443
    • Messerle, B.A.1    Schaffer, A.2    Vasak, M.3    Kägi, J.H.4    Wüthrich, K.5
  • 85
    • 0032468144 scopus 로고    scopus 로고
    • NMR spectroscopic studies of I=1/2 metal ions in biological systems
    • Öz G., Pountney D.A., Armitage I.M. NMR spectroscopic studies of I=1/2 metal ions in biological systems. Biochem. Cell Biol. 76:1998;223-234.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 223-234
    • Öz, G.1    Pountney, D.A.2    Armitage, I.M.3
  • 87
    • 0027108653 scopus 로고
    • DNA transcription. Zinc standard for economy
    • Luisi B. DNA transcription. Zinc standard for economy. Nature. 356:1992;378-380.
    • (1992) Nature , vol.356 , pp. 378-380
    • Luisi, B.1
  • 90
    • 0031740406 scopus 로고    scopus 로고
    • Measurement of nitric oxide-mediated effects on zinc homeostasis and zinc finger transcription factors
    • Kröncke K.-D., Kolb-Bachofen V. Measurement of nitric oxide-mediated effects on zinc homeostasis and zinc finger transcription factors. Methods Enzymol. 301:1999;126-135.
    • (1999) Methods Enzymol. , vol.301 , pp. 126-135
    • Kröncke, K.-D.1    Kolb-Bachofen, V.2
  • 91
    • 0037954792 scopus 로고    scopus 로고
    • Inactivation of zinc finger transcription factors provides a mechanism for a gene regulatory role of nitric oxide
    • Kröncke K.-D., Carlberg C. Inactivation of zinc finger transcription factors provides a mechanism for a gene regulatory role of nitric oxide. FASEB J. 14:2000;166-173.
    • (2000) FASEB J. , vol.14 , pp. 166-173
    • Kröncke, K.-D.1    Carlberg, C.2
  • 94
    • 0033571671 scopus 로고    scopus 로고
    • 2+ release from metallothionein by destroying zinc-sulfur clusters without concomitant formation of S-nitrosothiol
    • 2+ release from metallothionein by destroying zinc-sulfur clusters without concomitant formation of S-nitrosothiol. Biochem. J. 344:1999;253-258.
    • (1999) Biochem. J. , vol.344 , pp. 253-258
    • Aravindakumar, C.T.1    Ceulemans, J.2    De Ley, M.3
  • 95
    • 0037118631 scopus 로고    scopus 로고
    • Nitric oxide releases intracellular zinc from prokaryotic metallothionein in Escherichia coli
    • Binet M.R., Cruz-Ramos H., Laver J., Hughes M.N., Poole R.K. Nitric oxide releases intracellular zinc from prokaryotic metallothionein in Escherichia coli. FEMS Microbiol. Lett. 213:2002;121-126.
    • (2002) FEMS Microbiol. Lett. , vol.213 , pp. 121-126
    • Binet, M.R.1    Cruz-Ramos, H.2    Laver, J.3    Hughes, M.N.4    Poole, R.K.5
  • 96
    • 0026773382 scopus 로고
    • Amplification and rearrangement of a prokaryotic metallothionein locus smt in Synechococcus PCC 6301 selected for tolerance to cadmium
    • Gupta A., Whitton B.A., Morby A.P., Huckle J.W., Robinson N.J. Amplification and rearrangement of a prokaryotic metallothionein locus smt in Synechococcus PCC 6301 selected for tolerance to cadmium. Proc. R. Soc. Lond. B. 248:1992;273-281.
    • (1992) Proc. R. Soc. Lond. B , vol.248 , pp. 273-281
    • Gupta, A.1    Whitton, B.A.2    Morby, A.P.3    Huckle, J.W.4    Robinson, N.J.5
  • 97
    • 0027441545 scopus 로고
    • Deletion within the metallothionein locus of Cd-tolerant Synechococcus PCC 6301 involving a highly iterated palindrome (HIP1)
    • Gupta A., Morby A.P., Turner J.S., Whitton B.A., Robinson N.J. Deletion within the metallothionein locus of Cd-tolerant Synechococcus PCC 6301 involving a highly iterated palindrome (HIP1). Mol. Microbiol. 7:1993;189-195.
    • (1993) Mol. Microbiol. , vol.7 , pp. 189-195
    • Gupta, A.1    Morby, A.P.2    Turner, J.S.3    Whitton, B.A.4    Robinson, N.J.5
  • 99
    • 0021241613 scopus 로고
    • Cadmium-resistant Pseudomonas putida synthesizes novel cadmium binding proteins
    • Higham D.P., Sadler P.J., Scawen M.D. Cadmium-resistant Pseudomonas putida synthesizes novel cadmium binding proteins. Science. 225:1984;1043-1046.
    • (1984) Science , vol.225 , pp. 1043-1046
    • Higham, D.P.1    Sadler, P.J.2    Scawen, M.D.3
  • 100
    • 0026954828 scopus 로고
    • Nucleotide sequence of a metallothionein gene of the thermophilic cyanobacterium Synechococcus vulcanus
    • Shimizu T.T., Hiyam T., Ikeuchi M., Inoue Y. Nucleotide sequence of a metallothionein gene of the thermophilic cyanobacterium Synechococcus vulcanus. Plant Mol. Biol. 20:1992;565-567.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 565-567
    • Shimizu, T.T.1    Hiyam, T.2    Ikeuchi, M.3    Inoue, Y.4
  • 101
    • 0001024754 scopus 로고    scopus 로고
    • Reactions of electrophilic reagents that target the thiolate groups of metallothionein clusters: Preferential reaction of the α-domain with 5,5′-dithio-bis (2-nitrobenzoate) (DTNB) and aurothiolmalate (AuSTm)
    • Muñoz A., Petering D.H., Shaw C.F. Reactions of electrophilic reagents that target the thiolate groups of metallothionein clusters: Preferential reaction of the α-domain with 5,5′-dithio-bis (2-nitrobenzoate) (DTNB) and aurothiolmalate (AuSTm). Inorg. Chem. 38:1999;5655-5659.
    • (1999) Inorg. Chem. , vol.38 , pp. 5655-5659
    • Muñoz, A.1    Petering, D.H.2    Shaw, C.F.3
  • 102
    • 0034646226 scopus 로고    scopus 로고
    • Zinc transfer potentials of the alpha- and beta-clusters of metallothionein are affected by domain interactions in the whole molecule
    • Jiang L.J., Vasák M., Vallee B.L., Maret W. Zinc transfer potentials of the alpha- and beta-clusters of metallothionein are affected by domain interactions in the whole molecule. Proc. Natl. Acad. Sci. USA. 97:2000;2503-2508.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2503-2508
    • Jiang, L.J.1    Vasák, M.2    Vallee, B.L.3    Maret, W.4
  • 103
    • 0032168014 scopus 로고    scopus 로고
    • An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter
    • Thelwell C., Robinson N.J., Turner-Cavet J.S. An SmtB-like repressor from Synechocystis PCC 6803 regulates a zinc exporter. Proc. Natl. Acad. Sci. USA. 95:1998;10728-10733.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10728-10733
    • Thelwell, C.1    Robinson, N.J.2    Turner-Cavet, J.S.3
  • 104
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6    Miyajima, N.7    Hirosawa, M.8    Sugiura, M.9    Sasamoto, S.10
  • 105
    • 0033520471 scopus 로고    scopus 로고
    • Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase
    • Rutherford J.C., Cavet J.S., Robinson N.J. Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase. J. Biol. Chem. 274:1999;25827-25832.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25827-25832
    • Rutherford, J.C.1    Cavet, J.S.2    Robinson, N.J.3
  • 106
    • 0343986363 scopus 로고    scopus 로고
    • A gene cluster involved in metal homeostasis in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Garcia-Dominguez M., Lopez-Maury L., Florencio F.J., Reyes J.C. A gene cluster involved in metal homeostasis in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 182:2000;1507-1514.
    • (2000) J. Bacteriol. , vol.182 , pp. 1507-1514
    • Garcia-Dominguez, M.1    Lopez-Maury, L.2    Florencio, F.J.3    Reyes, J.C.4
  • 107
    • 0036041795 scopus 로고    scopus 로고
    • A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis
    • Gaballa A., Helmann J.D. A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis. Mol. Microbiol. 45:2002;997-1005.
    • (2002) Mol. Microbiol. , vol.45 , pp. 997-1005
    • Gaballa, A.1    Helmann, J.D.2
  • 108
    • 0037033056 scopus 로고    scopus 로고
    • Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase
    • in press
    • Fan, B. and Rosen, B.P. (2002) Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. J. Biol. Chem. (in press).
    • (2002) J. Biol. Chem.
    • Fan, B.1    Rosen, B.P.2
  • 109
    • 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., Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: A model for metalloregulatory proteins. J. Mol. Biol. 275:1998;337-347.
    • (1998) J. Mol. Biol. , vol.275 , pp. 337-347
    • Cook, W.J.1    Kar, S.R.2    Taylor, K.B.3    Hall, L.M.4
  • 110
    • 0037064122 scopus 로고    scopus 로고
    • A nickel-cobalt-sensing ArsR-SmtB family repressor: Contributions of 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. A nickel-cobalt-sensing ArsR-SmtB family repressor: Contributions of cytosol and effector binding sites to metal selectivity. J. Biol. Chem. 277:2002;38441-38448.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38441-38448
    • Cavet, J.S.1    Meng, W.2    Pennella, M.A.3    Appelhoff, R.J.4    Giedroc, D.P.5    Robinson, N.J.6
  • 112
    • 0026542504 scopus 로고
    • The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate
    • Thibaut D., Couder M., Famechon A., Debussche L., Cameron B., Crouzet J., Blanche F. The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate. J. Bacteriol. 174:1992;1043-1049.
    • (1992) J. Bacteriol. , vol.174 , pp. 1043-1049
    • Thibaut, D.1    Couder, M.2    Famechon, A.3    Debussche, L.4    Cameron, B.5    Crouzet, J.6    Blanche, F.7
  • 113
    • 0035986679 scopus 로고    scopus 로고
    • Metallochaperones: Bind and deliver
    • Rosenzweig A.C. Metallochaperones: Bind and deliver. Chem. Biol. 9:2002;673-677.
    • (2002) Chem. Biol. , vol.9 , pp. 673-677
    • Rosenzweig, A.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.