메뉴 건너뛰기




Volumn 161, Issue 2-3, 2009, Pages 920-925

Expressing a bacterial mercuric ion binding protein in plant for phytoremediation of heavy metals

Author keywords

Biosorption; Gram positive bacterial MerP; Heavy metals; Mercuric ion binding protein; Phytoremediation

Indexed keywords

ADSORPTION; BACTERIOLOGY; BIOREMEDIATION; BIOSORPTION; CELL MEMBRANES; CONFOCAL MICROSCOPY; CYTOLOGY; HEAVY METALS; IONS; MERCURY (METAL); MICROSCOPIC EXAMINATION; PLANTS (BOTANY); SORPTION; TURBULENT FLOW;

EID: 56249143073     PISSN: 03043894     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jhazmat.2008.04.079     Document Type: Article
Times cited : (63)

References (30)
  • 1
    • 0033535943 scopus 로고    scopus 로고
    • Phytoremediation of methylmercury pollution: merB expression in Arabidopsis thaliana confers resistance to organomercurials
    • Bizily S.P., Rugh C.L., Summers A.O., and Meagher R.B. Phytoremediation of methylmercury pollution: merB expression in Arabidopsis thaliana confers resistance to organomercurials. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 6808-6813
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6808-6813
    • Bizily, S.P.1    Rugh, C.L.2    Summers, A.O.3    Meagher, R.B.4
  • 2
    • 0028821638 scopus 로고
    • Minamata disease: methylmercury poisoning in Japan caused by environmental pollution
    • Harada M. Minamata disease: methylmercury poisoning in Japan caused by environmental pollution. Crit. Rev. Toxicol. 25 (1995) 1-24
    • (1995) Crit. Rev. Toxicol. , vol.25 , pp. 1-24
    • Harada, M.1
  • 3
    • 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
  • 4
    • 0030975003 scopus 로고    scopus 로고
    • Distribution, diversity and evolution of the bacterial mercury resistance (mer) operon
    • Osborn A.M., Bruce K.D., Strike P., and Ritchie D.A. Distribution, diversity and evolution of the bacterial mercury resistance (mer) operon. FEMS Microbiol. Rev. 19 (1997) 239-262
    • (1997) FEMS Microbiol. Rev. , vol.19 , pp. 239-262
    • Osborn, A.M.1    Bruce, K.D.2    Strike, P.3    Ritchie, D.A.4
  • 5
    • 0033035757 scopus 로고    scopus 로고
    • Structure analysis of a class II transposon encoding the mercury resistance of the Gram-positive bacterium Bacillus megaterium MB1, a strain isolated from Minamata Bay Japan
    • Huang C.C., Narita M., Yamagata T., Itoh Y., and Endo G. Structure analysis of a class II transposon encoding the mercury resistance of the Gram-positive bacterium Bacillus megaterium MB1, a strain isolated from Minamata Bay Japan. Gene 234 (1999) 361-369
    • (1999) Gene , vol.234 , pp. 361-369
    • Huang, C.C.1    Narita, M.2    Yamagata, T.3    Itoh, Y.4    Endo, G.5
  • 6
    • 0032735187 scopus 로고    scopus 로고
    • Identification of three merB genes and characterization of a broad-spectrum mercury resistance module encoded by a class II transposon of Bacillus megaterium strain MB1
    • Huang C.C., Narita M., Yamagata T., and Endo G. Identification of three merB genes and characterization of a broad-spectrum mercury resistance module encoded by a class II transposon of Bacillus megaterium strain MB1. Gene 239 (1999) 361-366
    • (1999) Gene , vol.239 , pp. 361-366
    • Huang, C.C.1    Narita, M.2    Yamagata, T.3    Endo, G.4
  • 7
    • 0037073412 scopus 로고    scopus 로고
    • Characterization of two regulatory genes of the mercury resistance determinants from TnMERI1 by luciferase-based examination
    • Huang C.C., Narita M., Yamagata T., Phung L.T., Endo G., and Silver S. Characterization of two regulatory genes of the mercury resistance determinants from TnMERI1 by luciferase-based examination. Gene 301 (2002) 13-20
    • (2002) Gene , vol.301 , pp. 13-20
    • Huang, C.C.1    Narita, M.2    Yamagata, T.3    Phung, L.T.4    Endo, G.5    Silver, S.6
  • 8
    • 0036320663 scopus 로고    scopus 로고
    • Simultaneous detection and removal of organomercurial compounds by using the genetic expression system of an organomercury lyase from the transposon TnMERI1
    • Narita M., Yamagata T., Ishii H., Huang C.C., and Endo G. Simultaneous detection and removal of organomercurial compounds by using the genetic expression system of an organomercury lyase from the transposon TnMERI1. Appl. Microbiol. Biotechnol. 59 (2002) 86-90
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 86-90
    • Narita, M.1    Yamagata, T.2    Ishii, H.3    Huang, C.C.4    Endo, G.5
  • 10
    • 1642344946 scopus 로고    scopus 로고
    • Dissemination of TnMERI1-like mercury resistance transposons among Bacillus isolated from worldwide environmental samples
    • Narita M., Matsui K., Huang C.C., Kawabata Z., and Endo G. Dissemination of TnMERI1-like mercury resistance transposons among Bacillus isolated from worldwide environmental samples. FEMS Ecol. 48 (2004) 47-55
    • (2004) FEMS Ecol. , vol.48 , pp. 47-55
    • Narita, M.1    Matsui, K.2    Huang, C.C.3    Kawabata, Z.4    Endo, G.5
  • 11
    • 0035253627 scopus 로고    scopus 로고
    • Metal-binding proteins and peptides in bioremediation and phytoremediation of heavy metals
    • Mejare M., and Bulow L. Metal-binding proteins and peptides in bioremediation and phytoremediation of heavy metals. Trends Biotechnol. 19 (2001) 67-73
    • (2001) Trends Biotechnol. , vol.19 , pp. 67-73
    • Mejare, M.1    Bulow, L.2
  • 12
    • 0031684013 scopus 로고    scopus 로고
    • Development of bacterium-based heavy metal biosorbents: enhanced uptake of cadmium and mercury by Escherichia coli expressing a metal binding motif
    • Pazirandeh M., Wells B.M., and Ryan R.L. Development of bacterium-based heavy metal biosorbents: enhanced uptake of cadmium and mercury by Escherichia coli expressing a metal binding motif. Appl. Environ. Microbiol. 64 (1998) 4068-4072
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4068-4072
    • Pazirandeh, M.1    Wells, B.M.2    Ryan, R.L.3
  • 13
    • 0023253810 scopus 로고
    • Role of the merT and merP gene products of transposon Tn501 in the induction and expression of resistance to mercuric ions
    • Lund P.A., and Brown N.L. Role of the merT and merP gene products of transposon Tn501 in the induction and expression of resistance to mercuric ions. Gene 52 (1987) 207-214
    • (1987) Gene , vol.52 , pp. 207-214
    • Lund, P.A.1    Brown, N.L.2
  • 14
    • 0026608566 scopus 로고
    • Purification and properties of the mercuric-ion-binding protein MerP
    • Sahlman L., and Jonsson B.H. Purification and properties of the mercuric-ion-binding protein MerP. Eur. J. Biochem. 205 (1992) 375-381
    • (1992) Eur. J. Biochem. , vol.205 , pp. 375-381
    • Sahlman, L.1    Jonsson, B.H.2
  • 15
    • 0031907875 scopus 로고    scopus 로고
    • Genes for all metals-a bacterial view of the Period Table
    • Silver S. Genes for all metals-a bacterial view of the Period Table. J. Industr. Microbiol. Biotech. 20 (1998) 1-12
    • (1998) J. Industr. Microbiol. Biotech. , vol.20 , pp. 1-12
    • Silver, S.1
  • 16
    • 0030199612 scopus 로고    scopus 로고
    • CPx-type ATPases: a class of P-type ATPases that pump heavy metals
    • Solioz M., and Vulpe C. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21 (1996) 237-241
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 17
    • 0033584955 scopus 로고    scopus 로고
    • Reactivity of the two essential cysteine residues of the periplasmic mercuric ion-binding protein MerP
    • Powlowski J., and Sahlman L. Reactivity of the two essential cysteine residues of the periplasmic mercuric ion-binding protein MerP. J. Biol. Chem. 274 (1999) 33320-33326
    • (1999) J. Biol. Chem. , vol.274 , pp. 33320-33326
    • Powlowski, J.1    Sahlman, L.2
  • 19
    • 0041429290 scopus 로고    scopus 로고
    • Polypeptides for heavy-metal biosorption: capacity and specificity of two heterogeneous MerP proteins
    • Huang C.C., Su C.C., Hsieh J.L., Tseng C.P., Lin P.J., and Chang J.S. Polypeptides for heavy-metal biosorption: capacity and specificity of two heterogeneous MerP proteins. Enzyme Microb. Technol. 33 (2003) 379-385
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 379-385
    • Huang, C.C.1    Su, C.C.2    Hsieh, J.L.3    Tseng, C.P.4    Lin, P.J.5    Chang, J.S.6
  • 20
    • 0142214658 scopus 로고    scopus 로고
    • Functional expression of a bacterial heavy metal transporter in Arabidopsis enhances resistance to and decreases uptake of heavy metals
    • Lee J., Bae H., Jeong J., Lee J.Y., Yang Y.Y., Hwang I., Martinoia E., and Lee Y. Functional expression of a bacterial heavy metal transporter in Arabidopsis enhances resistance to and decreases uptake of heavy metals. Plant Physiol. 133 (2003) 589-596
    • (2003) Plant Physiol. , vol.133 , pp. 589-596
    • Lee, J.1    Bae, H.2    Jeong, J.3    Lee, J.Y.4    Yang, Y.Y.5    Hwang, I.6    Martinoia, E.7    Lee, Y.8
  • 21
    • 0029919514 scopus 로고    scopus 로고
    • Mercuric ion reduction and resistance in transgenic Arabidopsis thaliana plants expressing a modified bacterial merA gene
    • Rugh C.L., Wilde H.D., Stack N.M., Thompson D.M., Summers A.O., and Meagher R.B. Mercuric ion reduction and resistance in transgenic Arabidopsis thaliana plants expressing a modified bacterial merA gene. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 3182-3187
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3182-3187
    • Rugh, C.L.1    Wilde, H.D.2    Stack, N.M.3    Thompson, D.M.4    Summers, A.O.5    Meagher, R.B.6
  • 22
    • 0031758183 scopus 로고    scopus 로고
    • Development of transgenic yellow poplar for mercury phytoremediation
    • Rugh C.L., Senecoff J.F., Meagher R.B., and Merkle S.A. Development of transgenic yellow poplar for mercury phytoremediation. Nat. Biotechnol. 16 (1998) 925-928
    • (1998) Nat. Biotechnol. , vol.16 , pp. 925-928
    • Rugh, C.L.1    Senecoff, J.F.2    Meagher, R.B.3    Merkle, S.A.4
  • 23
    • 0033951201 scopus 로고    scopus 로고
    • Phytodetoxification of hazardous organomercurials by genetically engineered plants
    • Bizily S.P., Rugh C.L., and Meagher R.B. Phytodetoxification of hazardous organomercurials by genetically engineered plants. Nat. Biotechnol. 18 (2000) 213-217
    • (2000) Nat. Biotechnol. , vol.18 , pp. 213-217
    • Bizily, S.P.1    Rugh, C.L.2    Meagher, R.B.3
  • 24
    • 0037321362 scopus 로고    scopus 로고
    • Subcellular targeting of methylmercury lyase enhances its specific activity for organic mercury detoxification in plants
    • Bizily S.P., Kim T., Kandasamy M.K., and Meagher R.B. Subcellular targeting of methylmercury lyase enhances its specific activity for organic mercury detoxification in plants. Plant Physiol. 131 (2003) 463-471
    • (2003) Plant Physiol. , vol.131 , pp. 463-471
    • Bizily, S.P.1    Kim, T.2    Kandasamy, M.K.3    Meagher, R.B.4
  • 25
    • 0037700822 scopus 로고    scopus 로고
    • Phytoremediation of organomercurial compounds via chloroplast genetic engineering
    • Ruiz O.N., Hussein H.S., Terry N., and Daniell H. Phytoremediation of organomercurial compounds via chloroplast genetic engineering. Plant Physiol. 132 (2003) 1344-1352
    • (2003) Plant Physiol. , vol.132 , pp. 1344-1352
    • Ruiz, O.N.1    Hussein, H.S.2    Terry, N.3    Daniell, H.4
  • 26
    • 0025376570 scopus 로고
    • Isolation of an efficient actin promoter for use in rice transformation
    • McElroy D., Zhang W., Cao J., and Wu R. Isolation of an efficient actin promoter for use in rice transformation. Plant Cell 2 (1990) 163-171
    • (1990) Plant Cell , vol.2 , pp. 163-171
    • McElroy, D.1    Zhang, W.2    Cao, J.3    Wu, R.4
  • 27
    • 69949124194 scopus 로고
    • Efficient transformation of Agrobacterium spp. by high voltage electroporation
    • Shen W.J., and Forde B.G. Efficient transformation of Agrobacterium spp. by high voltage electroporation. Nucleic Acids Res. 17 (1989) 8385
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8385
    • Shen, W.J.1    Forde, B.G.2
  • 28
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough S.J., and Bent A.F. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16 (1998) 735-743
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 29
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions
    • Jauh G.Y., Phillips T.E., and Rogers J.C. Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 11 (1999) 1867-1882
    • (1999) Plant Cell , vol.11 , pp. 1867-1882
    • Jauh, G.Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 30
    • 1142273243 scopus 로고    scopus 로고
    • Rapid estimation of lipids in oleaginous fungi and yeasts using Nile red fluorescence
    • Kimura K., Yamaoka M., and Kamisaka Y. Rapid estimation of lipids in oleaginous fungi and yeasts using Nile red fluorescence. J. Microbiol. Methods 56 (2004) 331-338
    • (2004) J. Microbiol. Methods , vol.56 , pp. 331-338
    • Kimura, K.1    Yamaoka, M.2    Kamisaka, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.