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Volumn 287, Issue 16, 2012, Pages 13016-13025

Ferritin protein nanocage ion channels: Gating by N-terminal extensions

Author keywords

[No Author keywords available]

Indexed keywords

3-FOLD SYMMETRY; AMINO ACID SUBSTITUTION; BOVINE SERUM ALBUMINS; FENTON CHEMISTRY; FERRITIN PROTEIN; HELICAL HAIRPINS; HELIX BUNDLE; HIGH CONCENTRATION; HIGH RESOLUTION; HYDROPHOBIC INTERACTIONS; ION BINDING; ION CHANNEL; ION ENTRIES; MEMBRANE PROTEINS; N-TERMINAL EXTENSION; N-TERMINALS; NANOCAGES; ORDERED WATER; PROTEIN CRYSTAL; SELF-ASSEMBLED; STRUCTURAL CHANGE; STRUCTURAL DIFFERENCES; STRUCTURE CONTROL; WATER SOLUBLE PROTEIN; WILD TYPES;

EID: 84859765138     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.332734     Document Type: Article
Times cited : (62)

References (53)
  • 1
    • 79953309867 scopus 로고    scopus 로고
    • Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry
    • Theil, E. C. (2011) Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry. Curr. Opin. Chem. Biol. 15, 304-311
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 304-311
    • Theil, E.C.1
  • 3
    • 77958076541 scopus 로고    scopus 로고
    • Moving metal ions through ferritin-protein nanocages from 3-fold pores to catalytic sites
    • Tosha, T., Ng, H. L., Bhattasali, O., Alber, T., and Theil, E. C. (2010) Moving metal ions through ferritin-protein nanocages from 3-fold pores to catalytic sites. J. Am. Chem. Soc. 132, 14562-14569
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14562-14569
    • Tosha, T.1    Ng, H.L.2    Bhattasali, O.3    Alber, T.4    Theil, E.C.5
  • 4
    • 79960411403 scopus 로고    scopus 로고
    • Moving iron through ferritin protein nanocages depends on residues throughout each four α-helix bundle subunit
    • Haldar, S., Bevers, L. E., Tosha, T., and Theil, E. C. (2011) Moving iron through ferritin protein nanocages depends on residues throughout each four α-helix bundle subunit. J. Biol. Chem. 286, 25620-25627
    • (2011) J. Biol. Chem. , vol.286 , pp. 25620-25627
    • Haldar, S.1    Bevers, L.E.2    Tosha, T.3    Theil, E.C.4
  • 5
    • 76249111445 scopus 로고    scopus 로고
    • NMR reveals pathway for ferric mineral precursors to the central cavity of ferritin
    • Turano, P., Lalli, D., Felli, I. C., Theil, E. C., and Bertini, I. (2010) NMR reveals pathway for ferric mineral precursors to the central cavity of ferritin. Proc. Natl. Acad. Sci. U.S.A. 107, 545-550
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 545-550
    • Turano, P.1    Lalli, D.2    Felli, I.C.3    Theil, E.C.4    Bertini, I.5
  • 7
    • 77951995410 scopus 로고    scopus 로고
    • New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants
    • Briat, J. F., Ravet, K., Arnaud, N., Duc, C., Boucherez, J., Touraine, B., Cellier, F., and Gaymard, F. (2010) New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Ann. Bot. 105, 811-822
    • (2010) Ann. Bot. , vol.105 , pp. 811-822
    • Briat, J.F.1    Ravet, K.2    Arnaud, N.3    Duc, C.4    Boucherez, J.5    Touraine, B.6    Cellier, F.7    Gaymard, F.8
  • 8
    • 78649726635 scopus 로고    scopus 로고
    • Transcriptional regulation of ferritin and antioxidant genes by HIPK2 under genotoxic stress
    • Hailemariam, K., Iwasaki, K., Huang, B. W., Sakamoto, K., and Tsuji, Y. (2010) Transcriptional regulation of ferritin and antioxidant genes by HIPK2 under genotoxic stress. J. Cell Sci. 123, 3863-3871
    • (2010) J. Cell Sci. , vol.123 , pp. 3863-3871
    • Hailemariam, K.1    Iwasaki, K.2    Huang, B.W.3    Sakamoto, K.4    Tsuji, Y.5
  • 10
    • 77954249308 scopus 로고    scopus 로고
    • Two to tango. Regulation of Mammalian iron metabolism
    • Hentze, M. W., Muckenthaler, M. U., Galy, B., and Camaschella, C. (2010) Two to tango. Regulation of Mammalian iron metabolism. Cell 142, 24-38
    • (2010) Cell , vol.142 , pp. 24-38
    • Hentze, M.W.1    Muckenthaler, M.U.2    Galy, B.3    Camaschella, C.4
  • 11
    • 0032563119 scopus 로고    scopus 로고
    • Localized unfolding at the junction of three ferritin subunits: A mechanism for iron release?
    • DOI 10.1074/jbc.273.30.18685
    • Takagi, H., Shi, D., Ha, Y., Allewell, N. M., and Theil, E. C. (1998) Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J. Biol. Chem. 273, 18685-18688 (Pubitemid 28366247)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18685-18688
    • Takagi, H.1    Shi, D.2    Ha, Y.3    Allewell, N.M.4    Theil, E.C.5
  • 13
    • 77953809155 scopus 로고    scopus 로고
    • The multifaceted capacity of Dps proteins to combat bacterial stress conditions. Detoxification of iron and hydrogen peroxide and DNA binding
    • Chiancone, E., and Ceci, P. (2010) The multifaceted capacity of Dps proteins to combat bacterial stress conditions. Detoxification of iron and hydrogen peroxide and DNA binding. Biochim. Biophys. Acta 1800, 798-805
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 798-805
    • Chiancone, E.1    Ceci, P.2
  • 15
    • 84857361317 scopus 로고    scopus 로고
    • Postpartum anemia II. Prevention and treatment
    • Milman, N. (2012) Postpartum anemia II. Prevention and treatment. Ann. Hematol. 91, 143-154
    • (2012) Ann. Hematol. , vol.91 , pp. 143-154
    • Milman, N.1
  • 16
    • 0018123699 scopus 로고
    • Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues
    • Jones, T., Spencer, R., and Walsh, C. (1978) Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues. Biochemistry 17, 4011-4017 (Pubitemid 9036517)
    • (1978) Biochemistry , vol.17 , Issue.19 , pp. 4011-4017
    • Jones, T.1    Spencer, R.2    Walsh, C.3
  • 17
    • 36148954688 scopus 로고    scopus 로고
    • Peptides selected for the protein nanocage pores change the rate of iron recovery from the ferritin mineral
    • DOI 10.1074/jbc.C700153200
    • Liu, X. S., Patterson, L. D., Miller, M. J., and Theil, E. C. (2007) Peptides selected for the protein nanocage pores change the rate of iron recovery from the ferritin mineral. J. Biol. Chem. 282, 31821-31825 (Pubitemid 350106408)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 31821-31825
    • Liu, X.S.1    Patterson, L.D.2    Miller, M.J.3    Theil, E.C.4
  • 18
    • 0035954391 scopus 로고    scopus 로고
    • "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin, W., Takagi, H., Pancorbo, B., and Theil, E. C. (2001) "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites. Biochemistry 40, 7525-7532 (Pubitemid 32578017)
    • (2001) Biochemistry , vol.40 , Issue.25 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 21
    • 78751684522 scopus 로고    scopus 로고
    • Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore
    • Rosenhouse-Dantsker, A., Logothetis, D. E., and Levitan, I. (2011) Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore. Biophys. J. 100, 381-389
    • (2011) Biophys. J. , vol.100 , pp. 381-389
    • Rosenhouse-Dantsker, A.1    Logothetis, D.E.2    Levitan, I.3
  • 22
    • 78650785077 scopus 로고    scopus 로고
    • Yeast water channels. An overview of orthodox aquaporins
    • Soveral, G., Prista, C., Moura, T. F., and Loureiro-Dias, M. C. (2010) Yeast water channels. An overview of orthodox aquaporins. Biol. Cell 103, 35-54
    • (2010) Biol. Cell , vol.103 , pp. 35-54
    • Soveral, G.1    Prista, C.2    Moura, T.F.3    Loureiro-Dias, M.C.4
  • 23
    • 0027729455 scopus 로고
    • Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin
    • DOI 10.1021/bi00211a039
    • Waldo, G. S., and Theil, E. C. (1993) Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin. Biochemistry 32, 13262-13269 (Pubitemid 24005936)
    • (1993) Biochemistry , vol.32 , Issue.48 , pp. 13262-13269
    • Waldo, G.S.1    Theil, E.C.2
  • 27
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie, A. G. (2006) The integration of macromolecular diffraction data. Acta Crystallogr. D Biol. Crystallogr. 62, 48-57
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 29
    • 0030931479 scopus 로고    scopus 로고
    • Preliminary analysis of amphibian red cell M ferritin in a novel tetragonal unit cell
    • DOI 10.1107/S0907444997003983
    • Ha, Y., Theil, E. C., and Allewell, N. M. (1997) Preliminary analysis of amphibian red cellMferritin in a novel tetragonal unit cell. Acta Crystallogr. D Biol. Crystallogr. 53, 513-523 (Pubitemid 27398690)
    • (1997) Acta Crystallographica Section D: Biological Crystallography , vol.53 , Issue.5 , pp. 513-523
    • Ha, Y.1    Theil, E.C.2    Allewell, N.M.3
  • 31
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • DOI 10.1110/ps.041185805
    • Duong-Ly, K. C., Nanda, V., Degrado, W. F., and Howard, K. P. (2005) The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci. 14, 856-861 (Pubitemid 40389355)
    • (2005) Protein Science , vol.14 , Issue.4 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    DeGrado, W.F.3    Howard, K.P.4
  • 36
    • 0037316987 scopus 로고    scopus 로고
    • Flexibility analysis of enzyme active sites by crystallographic temperature factors
    • Yuan, Z., Zhao, J., and Wang, Z. X. (2003) Flexibility analysis of enzyme active sites by crystallographic temperature factors. Protein Eng. 16, 109-114 (Pubitemid 36458649)
    • (2003) Protein Engineering , vol.16 , Issue.2 , pp. 109-114
    • Yuan, Z.1    Zhao, J.2    Wang, Z.-X.3
  • 37
    • 36549080494 scopus 로고    scopus 로고
    • Molecular Crowding Inhibits Intramolecular Breathing Motions in Proteins
    • DOI 10.1016/j.jmb.2007.07.075, PII S0022283607010534
    • Makowski, L., Rodi, D. J., Mandava, S., Minh, D. D., Gore, D. B., and Fischetti, R. F. (2008) Molecular crowding inhibits intramolecular breathing motions in proteins. J. Mol. Biol. 375, 529-546 (Pubitemid 350192471)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.2 , pp. 529-546
    • Makowski, L.1    Rodi, D.J.2    Mandava, S.3    Minh, D.D.L.4    Gore, D.B.5    Fischetti, R.F.6
  • 38
    • 63149177937 scopus 로고    scopus 로고
    • Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions
    • Li, C., and Pielak, G. J. (2009) Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions. J. Am. Chem. Soc. 131, 1368-1369
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1368-1369
    • Li, C.1    Pielak, G.J.2
  • 39
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: Dynamic management of biological iron and oxygen chemistry
    • DOI 10.1021/ar0302336
    • Liu, X., and Theil, E. C. (2005) Ferritins. Dynamic management of biological iron and oxygen chemistry. Acc. Chem. Res. 38, 167-175 (Pubitemid 40388095)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.3 , pp. 167-175
    • Liu, X.1    Theil, E.C.2
  • 40
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky, V. N. (1993) Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32, 13288-13298
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 42
    • 0032793828 scopus 로고    scopus 로고
    • Crystal structure of bullfrog M ferritin at 2.8 Å resolution: Analysis of subunit interactions and the binuclear metal center
    • DOI 10.1007/s007750050310
    • Ha, Y., Shi, D., Small, G. W., Theil, E. C., and Allewell, N. M. (1999) Crystal structure of bullfrog M ferritin at 2.8 Å resolution. Analysis of subunit interactions and the binuclear metal center. J. Biol. Inorg. Chem. 4, 243-256 (Pubitemid 29331013)
    • (1999) Journal of Biological Inorganic Chemistry , vol.4 , Issue.3 , pp. 243-256
    • Ha, Y.1    Shi, D.2    Small, G.W.3    Theil, E.C.4    Allewell, N.M.5
  • 43
    • 0037380857 scopus 로고    scopus 로고
    • Functional properties of threefold and fourfold channels in ferritin deduced from electrostatic calculations
    • Takahashi, T., and Kuyucak, S. (2003) Functional properties of 3-fold and 4-fold channels in ferritin deduced from electrostatic calculations. Biophys. J. 84, 2256-2263 (Pubitemid 36373548)
    • (2003) Biophysical Journal , vol.84 , Issue.4 , pp. 2256-2263
    • Takahashi, T.1    Kuyucak, S.2
  • 44
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D., and Simons, K. (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 45
    • 77950596053 scopus 로고    scopus 로고
    • Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis
    • Lundmark, R., and Carlsson, S. R. (2010) Driving membrane curvature in clathrin-dependent and clathrin-independent endocytosis. Semin. Cell Dev. Biol. 21, 363-370
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 363-370
    • Lundmark, R.1    Carlsson, S.R.2
  • 48
    • 77950463631 scopus 로고    scopus 로고
    • Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin
    • Masuda, T., Goto, F., Yoshihara, T., and Mikami, B. (2010) Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin. J. Biol. Chem. 285, 4049-4059
    • (2010) J. Biol. Chem. , vol.285 , pp. 4049-4059
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3    Mikami, B.4
  • 49
    • 0017803865 scopus 로고
    • Electron density map of apoferritin at 2.8-Å resolution
    • Banyard, S. H., Stammers, D. K., and Harrison, P. M. (1978) Electron density map of apoferritin at 2.8 Å resolution. Nature 271, 282-284 (Pubitemid 8256562)
    • (1978) Nature , vol.271 , Issue.5642 , pp. 282-284
    • Banyard, S.H.1    Stammers, D.K.2    Harrison, P.M.3
  • 50
    • 79959209134 scopus 로고    scopus 로고
    • Iron homeostasis and management of oxidative stress response in bacteria
    • Cornelis, P., Wei, Q., Andrews, S. C., and Vinckx, T. (2011) Iron homeostasis and management of oxidative stress response in bacteria. Metallomics 3, 540-549
    • (2011) Metallomics , vol.3 , pp. 540-549
    • Cornelis, P.1    Wei, Q.2    Andrews, S.C.3    Vinckx, T.4
  • 51
    • 70350634117 scopus 로고    scopus 로고
    • Living with iron (and oxygen). Questions and answers about iron homeostasis
    • Theil, E. C., and Goss, D. J. (2009) Living with iron (and oxygen). Questions and answers about iron homeostasis. Chem. Rev. 109, 4568-4579
    • (2009) Chem. Rev. , vol.109 , pp. 4568-4579
    • Theil, E.C.1    Goss, D.J.2
  • 52
    • 0027748181 scopus 로고
    • Iron (II) oxidation and early intermediates of iron-core formation in recombinant human H-chain ferritin
    • Bauminger, E. R., Harrison, P. M., Hechel, D., Hodson, N. W., Nowik, I., Treffry, A., and Yewdall, S. J. (1993) Iron(II) oxidation and early intermediates of iron core formation in recombinant human H-chain ferritin. Biochem. J. 296, 709-719 (Pubitemid 24008188)
    • (1993) Biochemical Journal , vol.296 , Issue.3 , pp. 709-719
    • Bauminger, E.R.1    Harrison, P.M.2    Hechel, D.3    Hodson, N.W.4    Nowik, I.5    Treffry, A.6    Yewdall, S.J.7
  • 53
    • 0030035534 scopus 로고    scopus 로고
    • Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation
    • Levi, S., Santambrogio, P., Corsi, B., Cozzi, A., and Arosio, P. (1996) Evidence that residues exposed on the 3-fold channels have active roles in the mechanism of ferritin iron incorporation. Biochem. J. 317, 467-473 (Pubitemid 26253983)
    • (1996) Biochemical Journal , vol.317 , Issue.2 , pp. 467-473
    • Levi, S.1    Santambrogio, P.2    Corsi, B.3    Cozzi, A.4    Arosio, P.5


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