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Volumn 82, Issue 4, 2011, Pages 792-796

How iron is transported into magnetosomes

Author keywords

[No Author keywords available]

Indexed keywords

CATION TRANSPORT PROTEIN; HETERODIMER; IRON; MAGNETITE; PROTEIN MAMB; PROTEIN MAMM; UNCLASSIFIED DRUG;

EID: 80855143751     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07864.x     Document Type: Note
Times cited : (14)

References (24)
  • 1
    • 7744220357 scopus 로고    scopus 로고
    • Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans and Escherichia coli
    • Anton, A., Weltrowski, A., Haney, J.H., Franke, S., Grass, G., Rensing, C., and Nies, D.H. (2004) Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans and Escherichia coli. J Bacteriol 186: 7499-7507.
    • (2004) J Bacteriol , vol.186 , pp. 7499-7507
    • Anton, A.1    Weltrowski, A.2    Haney, J.H.3    Franke, S.4    Grass, G.5    Rensing, C.6    Nies, D.H.7
  • 2
    • 2342429689 scopus 로고    scopus 로고
    • Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP
    • Chao, Y., and Fu, D. (2004) Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP. J Biol Chem 279: 17173-17180.
    • (2004) J Biol Chem , vol.279 , pp. 17173-17180
    • Chao, Y.1    Fu, D.2
  • 4
    • 0034945014 scopus 로고    scopus 로고
    • ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli
    • Grass, G., Fan, B., Rosen, B.P., Franke, S., Nies, D.H., and Rensing, C. (2001) ZitB (YbgR), a member of the cation diffusion facilitator family, is an additional zinc transporter in Escherichia coli. J Bacteriol 183: 4664-4667.
    • (2001) J Bacteriol , vol.183 , pp. 4664-4667
    • Grass, G.1    Fan, B.2    Rosen, B.P.3    Franke, S.4    Nies, D.H.5    Rensing, C.6
  • 5
    • 14244251491 scopus 로고    scopus 로고
    • The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum
    • Grass, G., Franke, S., Taudte, N., Nies, D.H., Kucharski, L.M., Maguire, M.E., and Rensing, C. (2005a) The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum. J Bacteriol 187: 1604-1611.
    • (2005) J Bacteriol , vol.187 , pp. 1604-1611
    • Grass, G.1    Franke, S.2    Taudte, N.3    Nies, D.H.4    Kucharski, L.M.5    Maguire, M.E.6    Rensing, C.7
  • 6
    • 12444299959 scopus 로고    scopus 로고
    • FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress
    • Grass, G., Otto, M., Fricke, B., Haney, C.J., Rensing, C., Nies, D.H., and Munkelt, D. (2005b) FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress. Arch Microbiol 183: 9-18.
    • (2005) Arch Microbiol , vol.183 , pp. 9-18
    • Grass, G.1    Otto, M.2    Fricke, B.3    Haney, C.J.4    Rensing, C.5    Nies, D.H.6    Munkelt, D.7
  • 7
    • 0024741152 scopus 로고
    • Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae
    • Kamizomo, A., Nishizawa, M., Teranishi, A., Murata, K., and Kimura, A. (1989) Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae. Mol Gen Genet 219: 161-167.
    • (1989) Mol Gen Genet , vol.219 , pp. 161-167
    • Kamizomo, A.1    Nishizawa, M.2    Teranishi, A.3    Murata, K.4    Kimura, A.5
  • 8
    • 79960149723 scopus 로고    scopus 로고
    • Characterization of a dipartite iron-uptake system from uropathogenic Escherichia coli strain F11
    • Koch, D., Chan, A.C., Murphy, M.E., Lilie, H., Grass, G., and Nies, D.H. (2011) Characterization of a dipartite iron-uptake system from uropathogenic Escherichia coli strain F11. J Biol Chem 286: 25317-25330.
    • (2011) J Biol Chem , vol.286 , pp. 25317-25330
    • Koch, D.1    Chan, A.C.2    Murphy, M.E.3    Lilie, H.4    Grass, G.5    Nies, D.H.6
  • 9
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili, A., Li, Z., Newman, D.K., and Jensen, G.J. (2006) Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311: 242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 10
    • 79955723752 scopus 로고    scopus 로고
    • The HtrA/DegP family protease MamE is a bifunctional protein with roles in magnetosome protein localization and magnetite biomineralization
    • Komeili, A., Quinlan, A., Murat, D., and Vali, H. (2011) The HtrA/DegP family protease MamE is a bifunctional protein with roles in magnetosome protein localization and magnetite biomineralization. Mol Microbiol 80: 1075-1087.
    • (2011) Mol Microbiol , vol.80 , pp. 1075-1087
    • Komeili, A.1    Quinlan, A.2    Murat, D.3    Vali, H.4
  • 11
    • 34648833810 scopus 로고    scopus 로고
    • Structure of the zinc transporter YiiP
    • Lu, M., and Fu, D. (2007) Structure of the zinc transporter YiiP. Science 317: 1746-1748.
    • (2007) Science , vol.317 , pp. 1746-1748
    • Lu, M.1    Fu, D.2
  • 12
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • Lu, M., Chai, J., and Fu, D. (2009) Structural basis for autoregulation of the zinc transporter YiiP. Nat Struct Mol Biol 16: 1063-1068.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1063-1068
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 13
    • 34248649906 scopus 로고    scopus 로고
    • Phylogenetic and functional analysis of the Cation Diffusion Facilitator (CDF) family: improved signature and prediction of substrate specificity
    • Montanini, B., Blaudez, D., Jeandroz, S., Sanders, D., and Chalot, M. (2007) Phylogenetic and functional analysis of the Cation Diffusion Facilitator (CDF) family: improved signature and prediction of substrate specificity. BMC Genomics 8: 107.
    • (2007) BMC Genomics , vol.8 , pp. 107
    • Montanini, B.1    Blaudez, D.2    Jeandroz, S.3    Sanders, D.4    Chalot, M.5
  • 14
    • 77950442198 scopus 로고    scopus 로고
    • Comprehensive genetic dissection of the magnetosome gene island reveals the step-wise assembly of a prokaryotic organelle
    • Murat, D., Quinlan, A., Vali, H., and Komeili, A. (2010) Comprehensive genetic dissection of the magnetosome gene island reveals the step-wise assembly of a prokaryotic organelle. Proc Natl Acad Sci USA 107: 5593-5598.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5593-5598
    • Murat, D.1    Quinlan, A.2    Vali, H.3    Komeili, A.4
  • 15
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies, D.H. (2003) Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol Rev 27: 313-339.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 16
    • 34648819082 scopus 로고    scopus 로고
    • How cells control zinc homeostasis
    • Nies, D.H. (2007) How cells control zinc homeostasis. Science 317: 1695-1696.
    • (2007) Science , vol.317 , pp. 1695-1696
    • Nies, D.H.1
  • 17
    • 0024746282 scopus 로고
    • Expression and nucleotide sequence of a plasmid-determined divalent cation efflux system from Alcaligenes eutrophus
    • Nies, D.H., Nies, A., Chu, L., and Silver, S. (1989) Expression and nucleotide sequence of a plasmid-determined divalent cation efflux system from Alcaligenes eutrophus. Proc Natl Acad Sci USA 86: 7351-7355.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7351-7355
    • Nies, D.H.1    Nies, A.2    Chu, L.3    Silver, S.4
  • 18
    • 0030953624 scopus 로고    scopus 로고
    • A novel family of ubiquitous heavy metal ion transport proteins
    • Paulsen, I.T., and Saier, M.H., Jr (1997) A novel family of ubiquitous heavy metal ion transport proteins. J Membr Biol 156: 99-103.
    • (1997) J Membr Biol , vol.156 , pp. 99-103
    • Paulsen, I.T.1    Saier Jr, M.H.2
  • 19
    • 33644873454 scopus 로고    scopus 로고
    • TCDB: the Transporter Classification Database for membrane transport protein analyses and information
    • Saier, M.H.J., Tran, C.V., and Barabote, R.D. (2006) TCDB: the Transporter Classification Database for membrane transport protein analyses and information. Nucleic Acids Res 34: D181-D186.
    • (2006) Nucleic Acids Res , vol.34
    • Saier, M.H.J.1    Tran, C.V.2    Barabote, R.D.3
  • 20
    • 33644763960 scopus 로고    scopus 로고
    • An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria
    • Scheffel, A., Gruska, M., Faivre, D., Linaroudis, A., Plitzko, J.M., and Schüler, D. (2006) An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria. Nature 440: 110-114.
    • (2006) Nature , vol.440 , pp. 110-114
    • Scheffel, A.1    Gruska, M.2    Faivre, D.3    Linaroudis, A.4    Plitzko, J.M.5    Schüler, D.6
  • 21
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi, H., Bencze, K.Z., Stemmler, T.L., and Philpott, C.C. (2008) A cytosolic iron chaperone that delivers iron to ferritin. Science 320: 1207-1210.
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 22
    • 0022927168 scopus 로고
    • Magnetotactic bacteria and single-domain magnetite in hemipelagic sediments
    • Stolz, J.F., Chang, S.-B.R., and Kirschvink, J.L. (1986) Magnetotactic bacteria and single-domain magnetite in hemipelagic sediments. Nature 321: 849-851.
    • (1986) Nature , vol.321 , pp. 849-851
    • Stolz, J.F.1    Chang, S.-B.2    Kirschvink, J.L.3
  • 23
    • 80855144209 scopus 로고    scopus 로고
    • The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly
    • Uebe, R., Junge, K., Henn, V., Poxleitner, G., Katzmann, E., Plitzko, J.M., etal. (2011) The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly. Mol Microbiol 82: 818-835).
    • (2011) Mol Microbiol , vol.82 , pp. 818-835
    • Uebe, R.1    Junge, K.2    Henn, V.3    Poxleitner, G.4    Katzmann, E.5    Plitzko, J.M.6
  • 24
    • 26644450950 scopus 로고    scopus 로고
    • Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF)
    • Wei, Y.N., and Fu, D. (2005) Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF). J Biol Chem 280: 33716-33724.
    • (2005) J Biol Chem , vol.280 , pp. 33716-33724
    • Wei, Y.N.1    Fu, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.