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Volumn 9, Issue 11, 2014, Pages 2517-2525

Loop electrostatics modulates the intersubunit interactions in ferritin

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; FERRITIN; LYSINE; NANOCAGE;

EID: 84914175069     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500431r     Document Type: Article
Times cited : (19)

References (36)
  • 1
    • 84870394036 scopus 로고    scopus 로고
    • Ferritins for chemistry and for life
    • Theil, E. C.; Behera, R. K.; and Tosha, T. (2013) Ferritins for chemistry and for life Coord. Chem. Rev. 257, 579-586
    • (2013) Coord. Chem. Rev. , vol.257 , pp. 579-586
    • Theil, E.C.1    Behera, R.K.2    Tosha, T.3
  • 2
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms
    • Theil, E. C. (1987) Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms Annu. Rev. Biochem. 56, 289-315
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 3
    • 84888589610 scopus 로고    scopus 로고
    • Solution and solid state NMR approaches to draw iron pathways in the ferritin nanocage
    • Lalli, D. and Turano, P. (2013) Solution and solid state NMR approaches to draw iron pathways in the ferritin nanocage Acc. Chem. Res. 46, 2676-2685
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2676-2685
    • Lalli, D.1    Turano, P.2
  • 4
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: Dynamic management of biological iron and oxygen chemistry
    • Liu, X. and Theil, E. C. (2005) Ferritins: Dynamic management of biological iron and oxygen chemistry Acc. Chem. Res. 38, 167-175
    • (2005) Acc. Chem. Res. , vol.38 , pp. 167-175
    • Liu, X.1    Theil, E.C.2
  • 5
    • 77953812371 scopus 로고    scopus 로고
    • X-ray structures of ferritins and related proteins
    • Crichton, R. R. and Declercq, J. P. (2010) X-ray structures of ferritins and related proteins Biochim. Biophys. Acta 1800, 706-718
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 706-718
    • Crichton, R.R.1    Declercq, J.P.2
  • 6
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function, and cellular regulation
    • Harrison, P. M. and Arosio, P. (1996) The ferritins: Molecular properties, iron storage function, and cellular regulation Biochim. Biophys. Acta 1275, 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 7
    • 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
  • 8
    • 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
  • 9
    • 84901912875 scopus 로고    scopus 로고
    • Coordinating subdomains of ferritin protein cages with catalysis and biomineralization viewed from the C4 cage axes
    • Theil, E. C.; Turano, P.; Ghini, V.; Allegrozzi, M.; and Bernacchioni, C. (2014) Coordinating subdomains of ferritin protein cages with catalysis and biomineralization viewed from the C4 cage axes J. Biol. Inorg. Chem. 19, 615-622
    • (2014) J. Biol. Inorg. Chem. , vol.19 , pp. 615-622
    • Theil, E.C.1    Turano, P.2    Ghini, V.3    Allegrozzi, M.4    Bernacchioni, C.5
  • 10
    • 77951237506 scopus 로고    scopus 로고
    • Alanine-shaving mutagenesis to determine key interfacial residues governing the assembly of a nano-cage maxi-ferritin
    • Zhang, Y.; Raudah, S.; Teo, H.; Teo, G. W.; Fan, R.; Sun, X.; and Orner, B. P. (2010) Alanine-shaving mutagenesis to determine key interfacial residues governing the assembly of a nano-cage maxi-ferritin J. Biol. Chem. 285, 12078-12086
    • (2010) J. Biol. Chem. , vol.285 , pp. 12078-12086
    • Zhang, Y.1    Raudah, S.2    Teo, H.3    Teo, G.W.4    Fan, R.5    Sun, X.6    Orner, B.P.7
  • 11
    • 84868349861 scopus 로고    scopus 로고
    • Ferritin ion channel disorder inhibits Fe(II)/O2 reactivity at distant sites
    • Tosha, T.; Behera, R. K.; and Theil, E. C. (2012) Ferritin ion channel disorder inhibits Fe(II)/O2 reactivity at distant sites Inorg. Chem. 51, 11406-11411
    • (2012) Inorg. Chem. , vol.51 , pp. 11406-11411
    • Tosha, T.1    Behera, R.K.2    Theil, E.C.3
  • 12
    • 70449519036 scopus 로고    scopus 로고
    • Oxidative stress and cell death in cells expressing l -ferritin variants causing neuroferritinopathy
    • Cozzi, A.; Rovelli, E.; Frizzale, G.; Campanella, A.; Amendola, M.; Arosio, P.; and Levi, S. (2010) Oxidative stress and cell death in cells expressing l -ferritin variants causing neuroferritinopathy Neurobiol. Dis. 37, 77-85
    • (2010) Neurobiol. Dis. , vol.37 , pp. 77-85
    • Cozzi, A.1    Rovelli, E.2    Frizzale, G.3    Campanella, A.4    Amendola, M.5    Arosio, P.6    Levi, S.7
  • 13
    • 84874061841 scopus 로고    scopus 로고
    • Re-engineering protein interfaces yields copper-inducible ferritin cage assembly
    • Huard, D. J.; Kane, K. M.; and Tezcan, F. A. (2013) Re-engineering protein interfaces yields copper-inducible ferritin cage assembly Nat. Chem. Biol. 9, 169-176
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 169-176
    • Huard, D.J.1    Kane, K.M.2    Tezcan, F.A.3
  • 14
    • 84874049851 scopus 로고    scopus 로고
    • Metalloenzymes: Cage redesign explains assembly
    • Theil, E. C. and Turano, P. (2013) Metalloenzymes: Cage redesign explains assembly Nat. Chem. Biol. 9, 143-144
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 143-144
    • Theil, E.C.1    Turano, P.2
  • 16
    • 0024554254 scopus 로고
    • Recombinant H-chain ferritins: Effects of changes in the 3-fold channels
    • Treffry, A.; Harrison, P. M.; Luzzago, A.; and Cesareni, G. (1989) Recombinant H-chain ferritins: Effects of changes in the 3-fold channels FEBS Lett. 247, 268-272
    • (1989) FEBS Lett. , vol.247 , pp. 268-272
    • Treffry, A.1    Harrison, P.M.2    Luzzago, A.3    Cesareni, G.4
  • 19
    • 33751517409 scopus 로고    scopus 로고
    • High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites
    • Toussaint, L.; Bertrand, L.; Hue, L.; Crichton, R. R.; and Declercq, J. P. (2007) High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites J. Mol. Biol. 365, 440-452
    • (2007) J. Mol. Biol. , vol.365 , pp. 440-452
    • Toussaint, L.1    Bertrand, L.2    Hue, L.3    Crichton, R.R.4    Declercq, J.P.5
  • 20
    • 34748853168 scopus 로고    scopus 로고
    • 13C-13C NOESY spectra of a 480 kDa protein: Solution NMR of ferritin
    • Matzapetakis, M.; Turano, P.; Theil, E. C.; and Bertini, I. (2007) 13C-13C NOESY spectra of a 480 kDa protein: Solution NMR of ferritin J. Biomol. NMR 38, 237-242
    • (2007) J. Biomol. NMR , vol.38 , pp. 237-242
    • Matzapetakis, M.1    Turano, P.2    Theil, E.C.3    Bertini, I.4
  • 21
    • 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
  • 22
    • 3543149006 scopus 로고    scopus 로고
    • The toxicity of recombinant proteins in Escherichia coli: A comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3)
    • Dumon-Seignovert, L.; Cariot, G.; and Vuillard, L. (2004) The toxicity of recombinant proteins in Escherichia coli: A comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3) Protein Expression Purif. 37, 203-206
    • (2004) Protein Expression Purif. , vol.37 , pp. 203-206
    • Dumon-Seignovert, L.1    Cariot, G.2    Vuillard, L.3
  • 23
    • 0032793828 scopus 로고    scopus 로고
    • Crystal structure of bullfrog M ferritin at 2.8 A resolution: Analysis of subunit interactions and the binuclear metal center
    • Ha, Y.; Shi, D.; Small, G. W.; Theil, E. C.; and Allewell, N. M. (1999) Crystal structure of bullfrog M ferritin at 2.8 A resolution: Analysis of subunit interactions and the binuclear metal center J. Biol. Inorg. Chem. 4, 243-256
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 243-256
    • Ha, Y.1    Shi, D.2    Small, G.W.3    Theil, E.C.4    Allewell, N.M.5
  • 24
  • 25
    • 77958076541 scopus 로고    scopus 로고
    • Moving metal ions through ferritin-protein nanocages from three-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 three-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
  • 26
    • 0037386550 scopus 로고    scopus 로고
    • Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral
    • Liu, X.; Jin, W.; and Theil, E. C. (2003) Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral Proc. Natl. Acad. Sci. U.S.A. 100, 3653-3658
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3653-3658
    • Liu, X.1    Jin, W.2    Theil, E.C.3
  • 27
    • 0030574045 scopus 로고    scopus 로고
    • Loop mutations affect ferritin solubility causing non-native aggregation of subunits or precipitation of fully assembled polymers
    • Jappelli, R. and Cesareni, G. (1996) Loop mutations affect ferritin solubility causing non-native aggregation of subunits or precipitation of fully assembled polymers FEBS Lett. 394, 311-315
    • (1996) FEBS Lett. , vol.394 , pp. 311-315
    • Jappelli, R.1    Cesareni, G.2
  • 28
    • 0023462561 scopus 로고
    • Mechanism of the self-assembly of apoferritin from horse spleen-Cross-linking and spectroscopic analysis
    • Gerl, M. and Jaenick, R. (1987) Mechanism of the self-assembly of apoferritin from horse spleen-Cross-linking and spectroscopic analysis Eur. Biophys J. 15, 103-109
    • (1987) Eur. Biophys J. , vol.15 , pp. 103-109
    • Gerl, M.1    Jaenick, R.2
  • 29
    • 0023952111 scopus 로고
    • Self-assembly of apoferritin from horse spleen after reversible chemical modification with 2,3-dimethylmaleic anhydride
    • Gerl, M.; Jaenick, R.; Smith, J. M. A.; and Harrison, P. M. (1987) Self-assembly of apoferritin from horse spleen after reversible chemical modification with 2,3-dimethylmaleic anhydride Biochemistry 27, 4089-4096
    • (1987) Biochemistry , vol.27 , pp. 4089-4096
    • Gerl, M.1    Jaenick, R.2    Smith, J.M.A.3    Harrison, P.M.4
  • 30
    • 0023227851 scopus 로고
    • On the mechanism of horse spleen apoferritin assembly: A sedimentation velocity and circular dichroism study
    • Stefanini, S.; Vecchini, P.; and Chiancone, E. (1987) On the mechanism of horse spleen apoferritin assembly: A sedimentation velocity and circular dichroism study Biochemistry 26, 1831-1837
    • (1987) Biochemistry , vol.26 , pp. 1831-1837
    • Stefanini, S.1    Vecchini, P.2    Chiancone, E.3
  • 31
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • Schreiber, G.; Haran, G.; and Zhou, H. X. (2009) Fundamental aspects of protein-protein association kinetics Chem. Rev. 109, 839-860
    • (2009) Chem. Rev. , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 32
    • 0030931479 scopus 로고    scopus 로고
    • Preliminary analysis of amphibian red cell M ferritin in a novel tetragonal unit cell
    • Ha, Y.; Theil, E. C.; and Allewell, N. M. (1997) Preliminary analysis of amphibian red cell M ferritin in a novel tetragonal unit cell Acta Crystallogr. D Biol. Crystallogr. 53, 513-523
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 513-523
    • Ha, Y.1    Theil, E.C.2    Allewell, N.M.3
  • 33
    • 0035024436 scopus 로고    scopus 로고
    • Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI
    • Longenecker, K. L.; Garrard, S. M.; Sheffield, P. J.; and Derewenda, Z. S. (2001) Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI Acta Crystallogr. D Biol. Crystallogr. 57, 679-688
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 679-688
    • Longenecker, K.L.1    Garrard, S.M.2    Sheffield, P.J.3    Derewenda, Z.S.4
  • 34
    • 27744607600 scopus 로고    scopus 로고
    • Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution
    • Banci, L.; Bertini, I.; Damelio, N.; Gaggelli, E.; Libralesso, E.; Matecko, I.; Turano, P.; and Valentine, J. S. (2005) Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution J. Biol. Chem. 280, 35815-35821
    • (2005) J. Biol. Chem. , vol.280 , pp. 35815-35821
    • Banci, L.1    Bertini, I.2    Damelio, N.3    Gaggelli, E.4    Libralesso, E.5    Matecko, I.6    Turano, P.7    Valentine, J.S.8
  • 36
    • 34548558727 scopus 로고    scopus 로고
    • Crystallization of soluble proteins in vapor diffusion for X-ray crystallography
    • Benvenuti, M. and Mangani, S. (2007) Crystallization of soluble proteins in vapor diffusion for X-ray crystallography Nat. Protoc. 2, 1633-1651
    • (2007) Nat. Protoc. , vol.2 , pp. 1633-1651
    • Benvenuti, M.1    Mangani, S.2


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