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Volumn 56, Issue 2, 2007, Pages 237-246

Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system

Author keywords

Co expression; Heteropolymer; Homopolymer; In vitro protein expression; Plant ferritin subunit

Indexed keywords

BIOPOLYMER; COMPLEMENTARY DNA; FERRITIN; IRON; PROTEIN SUBUNIT; VEGETABLE PROTEIN;

EID: 35448945259     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.07.011     Document Type: Article
Times cited : (37)

References (46)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties iron storage function and cellular regulation
    • Harrison P.M., and Arosio P. The ferritins: molecular properties iron storage function and cellular regulation. Biochim. Biophys. Acta 1275 (1996) 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 2
    • 0017881105 scopus 로고
    • On ferritin heterogeneity. Further evidence for heteropolymers
    • Arosio P., Adelman T.G., and Drysdale J.W. On ferritin heterogeneity. Further evidence for heteropolymers. J. Biol. Chem. 253 (1978) 4451-4458
    • (1978) J. Biol. Chem. , vol.253 , pp. 4451-4458
    • Arosio, P.1    Adelman, T.G.2    Drysdale, J.W.3
  • 9
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron nitric oxide and oxidative stress
    • Hentze M.W., and Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. USA 93 (1996) 8175-8182
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 11
    • 0034625385 scopus 로고    scopus 로고
    • Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean)
    • Wei J.Z., and Theil E.C. Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean). J. Biol. Chem. 275 (2000) 17488-17493
    • (2000) J. Biol. Chem. , vol.275 , pp. 17488-17493
    • Wei, J.Z.1    Theil, E.C.2
  • 12
    • 0035937161 scopus 로고    scopus 로고
    • Characterization of an iron-dependent regulatory sequence involved in the transcriptional control of AtFer1 and ZmFer1 plant ferritin genes by iron
    • Petit J.M., van Wuytswinkel O., Briat J.F., and Lobreaux S. Characterization of an iron-dependent regulatory sequence involved in the transcriptional control of AtFer1 and ZmFer1 plant ferritin genes by iron. J. Biol. Chem. 276 (2001) 5584-5590
    • (2001) J. Biol. Chem. , vol.276 , pp. 5584-5590
    • Petit, J.M.1    van Wuytswinkel, O.2    Briat, J.F.3    Lobreaux, S.4
  • 13
    • 0025186372 scopus 로고
    • Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean
    • Ragland M., Briat J.F., Gagnon J., Laulhere J.P., Massenet O., and Theil E.C. Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J. Biol. Chem. 265 (1990) 18339-18344
    • (1990) J. Biol. Chem. , vol.265 , pp. 18339-18344
    • Ragland, M.1    Briat, J.F.2    Gagnon, J.3    Laulhere, J.P.4    Massenet, O.5    Theil, E.C.6
  • 14
    • 0027523668 scopus 로고
    • Iron release and uptake by plant ferritin: effects of pH reduction and chelation
    • Laulhere J.P., and Briat J.F. Iron release and uptake by plant ferritin: effects of pH reduction and chelation. Biochem. J. 290 (1993) 693-699
    • (1993) Biochem. J. , vol.290 , pp. 693-699
    • Laulhere, J.P.1    Briat, J.F.2
  • 15
    • 0028854811 scopus 로고
    • Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro
    • van Wuytswinkel O., Savino G., and Briat J.F. Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro. Biochem. J. 305 (1995) 253-261
    • (1995) Biochem. J. , vol.305 , pp. 253-261
    • van Wuytswinkel, O.1    Savino, G.2    Briat, J.F.3
  • 16
    • 0026887039 scopus 로고
    • Iron induces ferritin synthesis in maize plantlets
    • Lobreaux S., Massenet O., and Briat J.F. Iron induces ferritin synthesis in maize plantlets. Plant Mol. Biol. 19 (1992) 563-575
    • (1992) Plant Mol. Biol. , vol.19 , pp. 563-575
    • Lobreaux, S.1    Massenet, O.2    Briat, J.F.3
  • 17
    • 0035504261 scopus 로고    scopus 로고
    • Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family
    • Petit J.M., Briat J.F., and Lobréaux S. Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family. Biochem. J. 359 (2001) 575-582
    • (2001) Biochem. J. , vol.359 , pp. 575-582
    • Petit, J.M.1    Briat, J.F.2    Lobréaux, S.3
  • 18
    • 0027267646 scopus 로고
    • Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata
    • Wicks R.E., and Entsch B. Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata. Biochem. Biophys. Res. Commun. 192 (1993) 813-819
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 813-819
    • Wicks, R.E.1    Entsch, B.2
  • 19
    • 0033083586 scopus 로고    scopus 로고
    • Occurrence and expression of members of the ferritin gene family in cowpeas
    • Wardrop A.J., Wicks R.E., and Entsch B. Occurrence and expression of members of the ferritin gene family in cowpeas. Biochem. J. 337 (1999) 523-530
    • (1999) Biochem. J. , vol.337 , pp. 523-530
    • Wardrop, A.J.1    Wicks, R.E.2    Entsch, B.3
  • 20
    • 0038688692 scopus 로고    scopus 로고
    • Differential expression and evolutionary analysis of the three ferritin genes in the legume plant Lupinus luteus
    • Strozycki P.M., Skapska A., Szczesniak K., Sobiezcruzuk E., and Briat J.F. Differential expression and evolutionary analysis of the three ferritin genes in the legume plant Lupinus luteus. Physiol. Plant. 118 (2003) 380-389
    • (2003) Physiol. Plant. , vol.118 , pp. 380-389
    • Strozycki, P.M.1    Skapska, A.2    Szczesniak, K.3    Sobiezcruzuk, E.4    Briat, J.F.5
  • 21
    • 22744458719 scopus 로고    scopus 로고
    • Isolation and expression pattern analysis of two ferritin genes in tobacco
    • Jiang T.B. Isolation and expression pattern analysis of two ferritin genes in tobacco. J. Integr. Plant Biol. 48 (2005) 477-486
    • (2005) J. Integr. Plant Biol. , vol.48 , pp. 477-486
    • Jiang, T.B.1
  • 22
    • 0035379652 scopus 로고    scopus 로고
    • A novel plant ferritin subunit from soybean that is related to a mechanism in iron release
    • Masuda T., Goto F., and Yohsihara T. A novel plant ferritin subunit from soybean that is related to a mechanism in iron release. J. Biol. Chem. 276 (2001) 19575-19579
    • (2001) J. Biol. Chem. , vol.276 , pp. 19575-19579
    • Masuda, T.1    Goto, F.2    Yohsihara, T.3
  • 23
    • 0031900148 scopus 로고    scopus 로고
    • Iron accumulation in tobacco plants by the expression of soybean gene
    • Goto F., Yoshihara T., and Saiki H. Iron accumulation in tobacco plants by the expression of soybean gene. Transgenic Res. 7 (1998) 173-180
    • (1998) Transgenic Res. , vol.7 , pp. 173-180
    • Goto, F.1    Yoshihara, T.2    Saiki, H.3
  • 24
    • 33646841705 scopus 로고    scopus 로고
    • Morphological phylogenetic and biological characteristics of Ectropis obliqua single-nucleocapsid nucleopolyhedrovirus
    • Ma X.C., Xu H.J., Tang M.J., Xiao Q., Hong J., and Zhang C.X. Morphological phylogenetic and biological characteristics of Ectropis obliqua single-nucleocapsid nucleopolyhedrovirus. J. Microbiol. 44 (2006) 77-82
    • (2006) J. Microbiol. , vol.44 , pp. 77-82
    • Ma, X.C.1    Xu, H.J.2    Tang, M.J.3    Xiao, Q.4    Hong, J.5    Zhang, C.X.6
  • 28
    • 0018152344 scopus 로고
    • The iron content of human liver and spleen isoferritins correlates with their isoelectric point and subunit composition
    • Bomford A., Berger M., Lis Y., and Williams R. The iron content of human liver and spleen isoferritins correlates with their isoelectric point and subunit composition. Biochem. Biophys. Res. Commun. 83 (1978) 334-341
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 334-341
    • Bomford, A.1    Berger, M.2    Lis, Y.3    Williams, R.4
  • 29
    • 0032488542 scopus 로고    scopus 로고
    • Suppression of cell growth by heavy chain ferritin
    • Guo J., Juan S., and Aust S.D. Suppression of cell growth by heavy chain ferritin. Biochem. Biophys. Res. Commun. 242 (1998) 39-45
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 39-45
    • Guo, J.1    Juan, S.2    Aust, S.D.3
  • 30
    • 0030825988 scopus 로고    scopus 로고
    • Recombinant ferritin: modulation of subunit stoichiometry in bacterial expression systems
    • Rucker P., Torti F.M., and Torti S.V. Recombinant ferritin: modulation of subunit stoichiometry in bacterial expression systems. Protein Eng. 10 (1997) 967-973
    • (1997) Protein Eng. , vol.10 , pp. 967-973
    • Rucker, P.1    Torti, F.M.2    Torti, S.V.3
  • 33
    • 0035289758 scopus 로고    scopus 로고
    • Enhanced iron uptake of Saccharomyces cerevisiae by heterologous expression of a tadpole ferritin gene
    • Shin Y.M., Kwon T.H., Kim K.S., Kim D.H., Kim J.H., and Yang M.S. Enhanced iron uptake of Saccharomyces cerevisiae by heterologous expression of a tadpole ferritin gene. Appl. Environ. Microbiol. 67 (2001) 1280-1283
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1280-1283
    • Shin, Y.M.1    Kwon, T.H.2    Kim, K.S.3    Kim, D.H.4    Kim, J.H.5    Yang, M.S.6
  • 34
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • Santambrogio P., Levi S., Cozzi A., Rovida E., Albertini A., and Arosio P. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J. Biol. Chem. 268 (1993) 12744-12748
    • (1993) J. Biol. Chem. , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, P.6
  • 36
    • 0027056014 scopus 로고
    • Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin
    • Lobreaux S., Yewdall S.J., Briat J.F., and Harrison P.M. Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin. Biochem. J. 288 (1992) 931-939
    • (1992) Biochem. J. , vol.288 , pp. 931-939
    • Lobreaux, S.1    Yewdall, S.J.2    Briat, J.F.3    Harrison, P.M.4
  • 37
    • 0029040871 scopus 로고
    • High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and solvation in function
    • Trikha J., Theil E.C., and Allewell N.M. High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and solvation in function. J. Mol. Biol. 248 (1995) 949-967
    • (1995) J. Mol. Biol. , vol.248 , pp. 949-967
    • Trikha, J.1    Theil, E.C.2    Allewell, N.M.3
  • 38
    • 0037474247 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of plant ferritin from Glycine max
    • Masuda T., Mikami B., Goto F., Yoshihara T., and Utsumi S. Crystallization and preliminary X-ray crystallographic analysis of plant ferritin from Glycine max. Biochim. Biophys. Acta 1645 (2003) 113-115
    • (2003) Biochim. Biophys. Acta , vol.1645 , pp. 113-115
    • Masuda, T.1    Mikami, B.2    Goto, F.3    Yoshihara, T.4    Utsumi, S.5
  • 39
    • 0025970277 scopus 로고
    • Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development
    • Lobreaux S., and Briat J.F. Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development. Biochem. J. 274 (1991) 601-606
    • (1991) Biochem. J. , vol.274 , pp. 601-606
    • Lobreaux, S.1    Briat, J.F.2
  • 40
    • 0024297030 scopus 로고
    • Purification and characterization of ferritins from maize pea and soya bean seeds. Distribution in various pea organs
    • Laulhere J.P., Lescure A.M., and Briat J.F. Purification and characterization of ferritins from maize pea and soya bean seeds. Distribution in various pea organs. J. Biol. Chem. 263 (1988) 10289-10294
    • (1988) J. Biol. Chem. , vol.263 , pp. 10289-10294
    • Laulhere, J.P.1    Lescure, A.M.2    Briat, J.F.3
  • 45
    • 0023645647 scopus 로고
    • Isolation and characterization of ferritin from soyabeans (Glycine max)
    • Sczekan S.R., and Joshi J.G. Isolation and characterization of ferritin from soyabeans (Glycine max). J. Biol. Chem. 262 (1987) 13780-13788
    • (1987) J. Biol. Chem. , vol.262 , pp. 13780-13788
    • Sczekan, S.R.1    Joshi, J.G.2
  • 46
    • 0024977973 scopus 로고
    • Mechanism of the transition from plant ferritin to phytosiderin
    • Laulhere J.P., Laboure A.M., and Briat J.F. Mechanism of the transition from plant ferritin to phytosiderin. J. Biol. Chem. 264 (1989) 3629-3635
    • (1989) J. Biol. Chem. , vol.264 , pp. 3629-3635
    • Laulhere, J.P.1    Laboure, A.M.2    Briat, J.F.3


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