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Volumn 353, Issue 1, 2005, Pages 68-79

Wrapping the α-crystallin domain fold in a chaperone assembly

Author keywords

Echinococcus multilocularis; Molecular chaperone; Schistosoma mansoni; Small heat shock protein; crystallin

Indexed keywords

ALPHA CRYSTALLIN;

EID: 25144461582     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.025     Document Type: Article
Times cited : (146)

References (54)
  • 1
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin-small heat-shock protein superfamily
    • W.W. De Jong, G.J. Caspers, and J.A. Leunissen Genealogy of the alpha-crystallin-small heat-shock protein superfamily Int. J. Biol. Macromol. 22 1998 151 162
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • De Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 2
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • R. Van Montfort, C. Slingsby, and E. Vierling Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones Advan. Protein Chem. 59 2001 105 156
    • (2001) Advan. Protein Chem. , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 4
    • 0034737774 scopus 로고    scopus 로고
    • HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans
    • L. Ding, and E.P. Candido HSP25, a small heat shock protein associated with dense bodies and M-lines of body wall muscle in Caenorhabditis elegans J. Biol. Chem. 275 2000 9510 9517
    • (2000) J. Biol. Chem. , vol.275 , pp. 9510-9517
    • Ding, L.1    Candido, E.P.2
  • 6
    • 2342455798 scopus 로고    scopus 로고
    • Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells
    • M.D. Perng, S.F. Wen, I.P. van den, A.R. Prescott, and R.A. Quinlan Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells Mol. Biol. Cell 15 2004 2335 2346
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2335-2346
    • Perng, M.D.1    Wen, S.F.2    Van Den, I.P.3    Prescott, A.R.4    Quinlan, R.A.5
  • 7
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • N. Mounier, and A.P. Arrigo Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 7 2002 167 176
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 10
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • A.L. Hsu, C.T. Murphy, and C. Kenyon Regulation of aging and age-related disease by DAF-16 and heat-shock factor Science 300 2003 1142 1145
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 11
    • 0033853066 scopus 로고    scopus 로고
    • Small heat shock proteins, the cytoskeleton, and inclusion body formation
    • M.W. Head, and J.E. Goldman Small heat shock proteins, the cytoskeleton, and inclusion body formation Neuropathol. Appl. Neurobiol. 26 2000 304 312
    • (2000) Neuropathol. Appl. Neurobiol. , vol.26 , pp. 304-312
    • Head, M.W.1    Goldman, J.E.2
  • 13
    • 3242770627 scopus 로고    scopus 로고
    • Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: Effects on amyloid fibril formation and chaperone activity
    • A. Rekas, C.G. Adda, J.A. Aquilina, K.J. Barnham, M. Sunde, and D. Galatis Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity J. Mol. Biol. 340 2004 1167 1183
    • (2004) J. Mol. Biol. , vol.340 , pp. 1167-1183
    • Rekas, A.1    Adda, C.G.2    Aquilina, J.A.3    Barnham, K.J.4    Sunde, M.5    Galatis, D.6
  • 14
    • 1642356755 scopus 로고    scopus 로고
    • HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells
    • A. Zourlidou, M.D. Payne Smith, and D.S. Latchman HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells J. Neurochem. 88 2004 1439 1448
    • (2004) J. Neurochem. , vol.88 , pp. 1439-1448
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3
  • 15
    • 0033927557 scopus 로고    scopus 로고
    • Structure and function of small heat shock/alpha-crystallin proteins: Established concepts and emerging ideas
    • T.H. MacRae Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas Cell. Mol. Life Sci. 57 2000 899 913
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 899-913
    • MacRae, T.H.1
  • 16
    • 2542451125 scopus 로고    scopus 로고
    • Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27
    • J.R. Theriault, H. Lambert, A.T. Chavez-Zobel, G. Charest, P. Lavigne, and J. Landry Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27 J. Biol. Chem. 279 2004 23463 23471
    • (2004) J. Biol. Chem. , vol.279 , pp. 23463-23471
    • Theriault, J.R.1    Lambert, H.2    Chavez-Zobel, A.T.3    Charest, G.4    Lavigne, P.5    Landry, J.6
  • 17
    • 2142768810 scopus 로고    scopus 로고
    • Chaperone activity of cytosolic small heat shock proteins from wheat
    • E. Basha, G.J. Lee, B. Demeler, and E. Vierling Chaperone activity of cytosolic small heat shock proteins from wheat Eur. J. Biochem. 271 2004 1426 1436
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1426-1436
    • Basha, E.1    Lee, G.J.2    Demeler, B.3    Vierling, E.4
  • 18
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • G.J. Lee, A.M. Roseman, H.R. Saibil, and E. Vierling A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state EMBO J. 16 1997 659 671
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 19
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • J. Horwitz Alpha-crystallin can function as a molecular chaperone Proc. Natl Acad. Sci. USA 89 1992 10449 10453
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 20
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • M. Ehrnsperger, S. Graber, M. Gaestel, and J. Buchner Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation EMBO J. 16 1997 221 229
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 21
    • 0034711315 scopus 로고    scopus 로고
    • Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins
    • S. Studer, and F. Narberhaus Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins J. Biol. Chem. 275 2000 37212 37218
    • (2000) J. Biol. Chem. , vol.275 , pp. 37212-37218
    • Studer, S.1    Narberhaus, F.2
  • 22
    • 0038109739 scopus 로고    scopus 로고
    • On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii
    • R. Kim, L. Lai, H.H. Lee, G.W. Cheong, K.K. Kim, and Z. Wu On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii Proc. Natl Acad. Sci. USA 100 2003 8151 8155
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 8151-8155
    • Kim, R.1    Lai, L.2    Lee, H.H.3    Cheong, G.W.4    Kim, K.K.5    Wu, Z.6
  • 24
    • 1542320089 scopus 로고    scopus 로고
    • The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
    • E. Basha, G.J. Lee, L.A. Breci, A.C. Hausrath, N.R. Buan, K.C. Giese, and E. Vierling The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions J. Biol. Chem. 279 2004 7566 7575
    • (2004) J. Biol. Chem. , vol.279 , pp. 7566-7575
    • Basha, E.1    Lee, G.J.2    Breci, L.A.3    Hausrath, A.C.4    Buan, N.R.5    Giese, K.C.6    Vierling, E.7
  • 25
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • A. Mogk, C. Schlieker, K.L. Friedrich, H.J. Schonfeld, E. Vierling, and B. Bukau Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK J. Biol. Chem. 278 2003 31033 31042
    • (2003) J. Biol. Chem. , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schonfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 26
    • 21244497886 scopus 로고    scopus 로고
    • Disassembling protein aggregates in the yeast cytosol: The cooperation of Hsp26 with Ssa1 and Hsp104
    • M. Haslbeck, A. Miess, T. Stromer, S. Walter, and J. Buchner Disassembling protein aggregates in the yeast cytosol: the cooperation of Hsp26 with Ssa1 and Hsp104 J. Biol. Chem. 280 2005 23861 23868
    • (2005) J. Biol. Chem. , vol.280 , pp. 23861-23868
    • Haslbeck, M.1    Miess, A.2    Stromer, T.3    Walter, S.4    Buchner, J.5
  • 27
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation: Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • A.G. Cashikar, M. Duennwald, and S. Lindquist A chaperone pathway in protein disaggregation: Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104 J. Biol. Chem. 280 2005 23869 23875
    • (2005) J. Biol. Chem. , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.3
  • 28
    • 3543039976 scopus 로고    scopus 로고
    • Mutants in a small heat shock protein that affect the oligomeric state - Analysis and allele-specific suppression
    • K.C. Giese, and E.J. Vierling Mutants in a small heat shock protein that affect the oligomeric state - analysis and allele-specific suppression J. Biol. Chem. 279 2004 32674 32683
    • (2004) J. Biol. Chem. , vol.279 , pp. 32674-32683
    • Giese, K.C.1    Vierling, E.J.2
  • 29
    • 14844292563 scopus 로고    scopus 로고
    • A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins
    • X. Fu, H. Zhang, X. Zhang, Y. Cao, W. Jiao, and C. Liu A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins J. Biol. Chem. 280 2005 6337 6348
    • (2005) J. Biol. Chem. , vol.280 , pp. 6337-6348
    • Fu, X.1    Zhang, H.2    Zhang, X.3    Cao, Y.4    Jiao, W.5    Liu, C.6
  • 30
    • 0034067386 scopus 로고    scopus 로고
    • Mouse Hsp25, a small shock protein. the role of its C-terminal extension in oligomerization and chaperone action
    • R.A. Lindner, J.A. Carver, M. Ehrnsperger, J. Buchner, G. Esposito, and J. Behlke Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action Eur. J. Biochem. 267 2000 1923 1932
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1923-1932
    • Lindner, R.A.1    Carver, J.A.2    Ehrnsperger, M.3    Buchner, J.4    Esposito, G.5    Behlke, J.6
  • 31
    • 1642524277 scopus 로고    scopus 로고
    • Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins
    • T. Stromer, E. Fischer, K. Richter, M. Haslbeck, and J. Buchner Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domain is important for oligomer assembly and the binding of unfolding proteins J. Biol. Chem. 279 2004 11222 11228
    • (2004) J. Biol. Chem. , vol.279 , pp. 11222-11228
    • Stromer, T.1    Fischer, E.2    Richter, K.3    Haslbeck, M.4    Buchner, J.5
  • 32
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
    • M.P. Bova, H.S. McHaourab, Y. Han, and B.K. Fung Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations J. Biol. Chem. 275 2000 1035 1042
    • (2000) J. Biol. Chem. , vol.275 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 33
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • K.K. Kim, R. Kim, and S.H. Kim Crystal structure of a small heat-shock protein Nature 394 1998 595 599
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 35
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
    • F. Sobott, J.L. Benesch, E. Vierling, and C.V. Robinson Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry J. Biol. Chem. 277 2002 38921 38929
    • (2002) J. Biol. Chem. , vol.277 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.2    Vierling, E.3    Robinson, C.V.4
  • 36
    • 4444370076 scopus 로고    scopus 로고
    • Tsp36, a tapeworm small heat-shock protein with a duplicated alpha-crystallin domain, forms dimers and tetramers with good chaperone-like activity
    • G. Kappe, J.A. Aquilina, L. Wunderink, B. Kamps, C.V. Robinson, and T. Garate Tsp36, a tapeworm small heat-shock protein with a duplicated alpha-crystallin domain, forms dimers and tetramers with good chaperone-like activity Proteins: Struct. Funct. Genet. 57 2004 109 117
    • (2004) Proteins: Struct. Funct. Genet. , vol.57 , pp. 109-117
    • Kappe, G.1    Aquilina, J.A.2    Wunderink, L.3    Kamps, B.4    Robinson, C.V.5    Garate, T.6
  • 37
    • 0031954978 scopus 로고    scopus 로고
    • Sequence and preliminary characterisation of a Taenia saginata oncosphere gene homologue of the small heat-shock protein family
    • L. Benitez, L.J. Harrison, R.M. Parkhouse, and T. Garate Sequence and preliminary characterisation of a Taenia saginata oncosphere gene homologue of the small heat-shock protein family Parasitol. Res. 84 1998 423 425
    • (1998) Parasitol. Res. , vol.84 , pp. 423-425
    • Benitez, L.1    Harrison, L.J.2    Parkhouse, R.M.3    Garate, T.4
  • 38
    • 0022526802 scopus 로고
    • Sequence and expression of a major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alpha-crystallins
    • V. Nene, D.W. Dunne, K.S. Johnson, D.W. Taylor, and J.S. Cordingley Sequence and expression of a major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alpha-crystallins Mol. Biochem. Parasitol. 21 1986 179 188
    • (1986) Mol. Biochem. Parasitol. , vol.21 , pp. 179-188
    • Nene, V.1    Dunne, D.W.2    Johnson, K.S.3    Taylor, D.W.4    Cordingley, J.S.5
  • 39
    • 0042833263 scopus 로고    scopus 로고
    • Analysis of cDNAs coding for immunologically dominant antigens from an oncosphere-specific cDNA library of Echinococcus multilocularis
    • A. Merckelbach, M. Wager, and R. Lucius Analysis of cDNAs coding for immunologically dominant antigens from an oncosphere-specific cDNA library of Echinococcus multilocularis Parasitol. Res. 90 2003 493 501
    • (2003) Parasitol. Res. , vol.90 , pp. 493-501
    • Merckelbach, A.1    Wager, M.2    Lucius, R.3
  • 40
    • 0032103941 scopus 로고    scopus 로고
    • Identification of the immunodominant T cell epitope of p38, a major egg antigen, and characterization of the epitope-specific Th responsiveness during murine Schistosomiasis mansoni
    • Y. Chen, and D.L. Boros Identification of the immunodominant T cell epitope of p38, a major egg antigen, and characterization of the epitope-specific Th responsiveness during murine Schistosomiasis mansoni J. Immunol. 160 1998 5420 5427
    • (1998) J. Immunol. , vol.160 , pp. 5420-5427
    • Chen, Y.1    Boros, D.L.2
  • 41
    • 0034333196 scopus 로고    scopus 로고
    • Rapid automatic detection and alignment of repeats in protein sequences
    • A. Heger, and L. Holm Rapid automatic detection and alignment of repeats in protein sequences Proteins: Struct. Funct. Genet. 41 2000 224 237
    • (2000) Proteins: Struct. Funct. Genet. , vol.41 , pp. 224-237
    • Heger, A.1    Holm, L.2
  • 42
    • 85047698890 scopus 로고    scopus 로고
    • Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallin
    • M.M. Valdez, J.I. Clark, G.J. Wu, and P.J. Muchowski Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallin Eur. J. Biochem. 269 2002 1806 1813
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1806-1813
    • Valdez, M.M.1    Clark, J.I.2    Wu, G.J.3    Muchowski, P.J.4
  • 44
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • S. Doublié Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 47
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • G.S. French, and K.S. Wilson On the treatment of negative intensity observations Acta Crystallog. sect. A 34 1978 517 525
    • (1978) Acta Crystallog. Sect. a , vol.34 , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 49
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. De La Fortelle, and G. Bricogne Maximum-likelihood heavy atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 50
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 52
  • 53
    • 0032945191 scopus 로고    scopus 로고
    • CORA - Topological fingerprints for protein structural families
    • C.A. Orengo CORA - topological fingerprints for protein structural families Protein Sci. 8 1999 699 715
    • (1999) Protein Sci. , vol.8 , pp. 699-715
    • Orengo, C.A.1
  • 54
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • S.R. Eddy Profile hidden Markov models Bioinformatics 14 1998 755 763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1


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