메뉴 건너뛰기




Volumn 258, Issue 1, 1998, Pages 170-183

Structural alterations of α-crystallin during its chaperone action

Author keywords

crystallin; Fluorescence spectroscopy; Molecular chaperone; NMR spectroscopy; Small heatshock protein

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; GLOBULAR PROTEIN; HEAT SHOCK PROTEIN; OVOTRANSFERRIN;

EID: 0032533361     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580170.x     Document Type: Article
Times cited : (96)

References (56)
  • 1
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Büchner, J. (1996) Supervising the fold: functional principles of molecular chaperones, FASEB J. 10, 10-19.
    • (1996) FASEB J. , vol.10 , pp. 10-19
    • Büchner, J.1
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996) Molecular chaperones in cellular protein folding, Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 3
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperone α-crystallin. from lens transparency to molecular pathology
    • Groenen, P. J. T. A., Merck, K. B., de Jong, W. W. & Bloemendal, H. (1994) Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology, Eur. J. Biochem. 225, 1-19.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1-19
    • Groenen, P.J.T.A.1    Merck, K.B.2    De Jong, W.W.3    Bloemendal, H.4
  • 4
    • 0343742639 scopus 로고    scopus 로고
    • Binding of nonnative protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger, M., Gräber, S., Gaestel, M. & Buchner, J. (1997) Binding of nonnative protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation, EMBO J. 16, 221-229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 5
    • 0027673091 scopus 로고
    • Comparison of the homologous carboxyl-terminal domain and tail of α-crystallin and small-heat shock protein
    • Merck. K. B., Horwitz, J., Kersten, M., Overkamp, P., Gaestel, M., Bloemendal, H. & de Jong, W. W. (1993) Comparison of the homologous carboxyl-terminal domain and tail of α-crystallin and small-heat shock protein, Mol. Biol. Rep. 18, 209-215.
    • (1993) Mol. Biol. Rep. , vol.18 , pp. 209-215
    • Merck, K.B.1    Horwitz, J.2    Kersten, M.3    Overkamp, P.4    Gaestel, M.5    Bloemendal, H.6    De Jong, W.W.7
  • 6
    • 0030826325 scopus 로고    scopus 로고
    • Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
    • Leroux, M. R., Melki, R., Gordon, B., Batelier, G. & Candido, E. P. M. (1997) Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides, J. Biol. Chem. 272, 24646-24656.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24646-24656
    • Leroux, M.R.1    Melki, R.2    Gordon, B.3    Batelier, G.4    Candido, E.P.M.5
  • 8
    • 0028984175 scopus 로고
    • 1H-NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids
    • 1H-NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids, FEBS Lett. 369, 305-310.
    • (1995) FEBS Lett. , vol.369 , pp. 305-310
    • Carver, J.A.1    Esposito, G.2    Schwedersky, G.3    Gaestel, M.4
  • 10
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, αB-crystallin, has a variable quarternary structure
    • Haley, D. A., Horwitz, J. & Stewart, P. L. (1998) The small heat-shock protein, αB-crystallin, has a variable quarternary structure, J. Mol. Biol. 277, 27-35.
    • (1998) J. Mol. Biol. , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 11
    • 0027933712 scopus 로고
    • A possible chaperone-like quaternary structure for α-crystallin
    • Carver, J. A., Aquilina, J. A. & Truscott, R. J. W. (1994) A possible chaperone-like quaternary structure for α-crystallin, Exp. Eye Res. 59, 231-234.
    • (1994) Exp. Eye Res. , vol.59 , pp. 231-234
    • Carver, J.A.1    Aquilina, J.A.2    Truscott, R.J.W.3
  • 13
    • 0030783517 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone, α-crystallin, with molten globule states of bovine α-lactalbumin
    • Lindner, R. A., Kapur. A. & Carver, J. A. (1997) The interaction of the molecular chaperone, α-crystallin, with molten globule states of bovine α-lactalbumin, J. Biol. Chem. 272, 27 722-27 729.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27722-27729
    • Lindner, R.A.1    Kapur, A.2    Carver, J.A.3
  • 14
    • 0025325591 scopus 로고
    • Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4
    • Slingsby, C. & Bateman, O. A. (1990) Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4, Exp. Eye Res. 51, 21-26.
    • (1990) Exp. Eye Res. , vol.51 , pp. 21-26
    • Slingsby, C.1    Bateman, O.A.2
  • 15
    • 0023178690 scopus 로고
    • Isolation of α-crystallin subunits by gel filtration
    • Stevens, A. & Augusteyn, R. C. (1987) Isolation of α-crystallin subunits by gel filtration, Curr. Eye Res. 6, 739-740.
    • (1987) Curr. Eye Res. , vol.6 , pp. 739-740
    • Stevens, A.1    Augusteyn, R.C.2
  • 18
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D. J., Haberkorn, R. A. & Ruben, D. J. (1982) A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants, J. Magn. Reson. 48. 286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 20
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 21
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz, J. (1992) α-Crystallin can function as a molecular chaperone, Proc. Natl Acad. Sci. USA 89, 10449-10453.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 22
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob, U., Gaestel, M., Engel, K. & Buchner, J. (1993) Small heat shock proteins are molecular chaperones, J. Biol. Chem. 268, 1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 23
    • 0028984242 scopus 로고
    • On the thermal stability of α-crystallin: A new insight from infrared spectroscopy
    • Surewicz, W. K. & Olesen, P. R. (1995) On the thermal stability of α-crystallin: a new insight from infrared spectroscopy. Biochemistry 34, 9655-9660.
    • (1995) Biochemistry , vol.34 , pp. 9655-9660
    • Surewicz, W.K.1    Olesen, P.R.2
  • 24
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Raman, B., Ramakrishna, T. & Rao, Ch. M. (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 365, 133-136.
    • (1995) FEBS Lett. , vol.365 , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Rao, Ch.M.3
  • 25
    • 0029124685 scopus 로고
    • Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin
    • Das, K. P. & Surewicz, W. K. (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin, FEBS Lett. 369. 321-325.
    • (1995) FEBS Lett. , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 27
    • 0023888625 scopus 로고
    • Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin
    • Chiesa, R., Gawinowicz-Kolks, M. A., Kleiman, N. J. & Spector, A. (1988) Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin, Exp. Eye Res. 46, 199-208.
    • (1988) Exp. Eye Res. , vol.46 , pp. 199-208
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Kleiman, N.J.3    Spector, A.4
  • 29
    • 0030452980 scopus 로고    scopus 로고
    • Age-related changes in bovine α-crystallin and highmolecular-weight mass protein
    • Carver, J. A., Nicholls, K. A., Aquilina, J. A. & Truscott, R. J. W. (1996) Age-related changes in bovine α-crystallin and highmolecular-weight mass protein, Exp. Eye Res. 63, 639-647.
    • (1996) Exp. Eye Res. , vol.63 , pp. 639-647
    • Carver, J.A.1    Nicholls, K.A.2    Aquilina, J.A.3    Truscott, R.J.W.4
  • 30
    • 0027193482 scopus 로고
    • An investigation into the stability of α-crystallin by NMR spectroscopy; evidence for a two-domain structure
    • Carver, J. A., Aquilina, J. A. & Truscott, R. J. W. (1993) An investigation into the stability of α-crystallin by NMR spectroscopy; evidence for a two-domain structure, Biochim. Biophys. Acta 1164, 22-28.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 22-28
    • Carver, J.A.1    Aquilina, J.A.2    Truscott, R.J.W.3
  • 31
    • 0025832120 scopus 로고
    • Interaction and aggregation of lens crystallins
    • Liang, J. N. & Li, X.-Y. (1991) Interaction and aggregation of lens crystallins, Exp. Eye Res. 53, 61-66.
    • (1991) Exp. Eye Res. , vol.53 , pp. 61-66
    • Liang, J.N.1    Li, X.-Y.2
  • 33
    • 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
    • Lee, G. J., Roseman, A. M., Saibil, H. R. & Vierling, E. (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state, EMBO J. 16, 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
  • 34
    • 85007751156 scopus 로고
    • Thiol-dependent gelation of the domain I-truncated fragment of bovine serum albumin
    • Shin, W.-S. & Hirose, M. (1995) Thiol-dependent gelation of the domain I-truncated fragment of bovine serum albumin, Biosci. Biotechnol. Biochem. 59, 817-821.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 817-821
    • Shin, W.-S.1    Hirose, M.2
  • 35
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate
    • Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L. & Hartl, F. U. (1991) Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule'-like intermediate, Nature 352, 36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 36
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K. & Hartl, F. U. (1992) Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding, Nature 356, 683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 37
    • 0026755898 scopus 로고
    • Peptide binding by chaperone SecB: Implications for recognition of nonnative structure
    • Randall, L. L. (1992) Peptide binding by chaperone SecB: implications for recognition of nonnative structure, Science 257, 241-245.
    • (1992) Science , vol.257 , pp. 241-245
    • Randall, L.L.1
  • 39
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study
    • Alexandrescu, A. T., Evans, P. A., Pitkeathly, M., Baum, J. & Dobson, C. M. (1993) Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: a two-dimensional NMR study, Biochemistry 32, 1707-1718.
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, P.A.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 40
    • 0024438885 scopus 로고
    • Renaturation of ovotransferrin under two-step conditions allowing primary folding of the fully reduced form and the subsequent regeneration of the intramolecular disulfides
    • Hirose, M., Akuta, T. & Takahashi, N. (1989) Renaturation of ovotransferrin under two-step conditions allowing primary folding of the fully reduced form and the subsequent regeneration of the intramolecular disulfides, J. Biol. Chem. 264, 16867-16872.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16867-16872
    • Hirose, M.1    Akuta, T.2    Takahashi, N.3
  • 41
    • 0026086820 scopus 로고
    • Partially folded state of the disulfide-reduced N-terminal half-molecule of ovotransferrin as a renaturant intermediate
    • Hirose, M. & Yamashita, H. (1991) Partially folded state of the disulfide-reduced N-terminal half-molecule of ovotransferrin as a renaturant intermediate, J. Biol. Chem. 266, 1463-1468.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1463-1468
    • Hirose, M.1    Yamashita, H.2
  • 42
    • 0030891712 scopus 로고    scopus 로고
    • Heat-induced conformational change and increased chaperone activity of lens α-crystallin
    • Das, B. K., Liang, J. J.-N. & Chakrabarti, B. (1997) Heat-induced conformational change and increased chaperone activity of lens α-crystallin, Curr. Eye Res. 16, 303-309.
    • (1997) Curr. Eye Res. , vol.16 , pp. 303-309
    • Das, B.K.1    Liang, J.J.-N.2    Chakrabarti, B.3
  • 43
    • 0030798628 scopus 로고    scopus 로고
    • Chaperone-like activity and temperature-induced structural changes of α-crystallin
    • Raman, B. & Rao, Ch. M. (1997) Chaperone-like activity and temperature-induced structural changes of α-crystallin, J. Biol. Chem. 272, 23559-23564.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23559-23564
    • Raman, B.1    Rao, Ch.M.2
  • 44
    • 0023777949 scopus 로고
    • Heat-induced changes in the conformation of α- And β-crystallins: Unique thermal stability of α-crystallin
    • Maiti, M., Kono, M. & Chakrabarti, B. (1988) Heat-induced changes in the conformation of α- and β-crystallins: unique thermal stability of α-crystallin, FEBS Lett. 236, 109-114.
    • (1988) FEBS Lett. , vol.236 , pp. 109-114
    • Maiti, M.1    Kono, M.2    Chakrabarti, B.3
  • 46
    • 0023810710 scopus 로고
    • High-molecular-weight protein aggregates of calf and cow lens: Spectroscopic evaluation
    • Messmer, M. & Chakrabarti, B. (1988) High-molecular-weight protein aggregates of calf and cow lens: spectroscopic evaluation, Exp. Eye Res. 47, 173-183.
    • (1988) Exp. Eye Res. , vol.47 , pp. 173-183
    • Messmer, M.1    Chakrabarti, B.2
  • 47
    • 0030995724 scopus 로고    scopus 로고
    • The Hydrophobic probe 4,4′-bis-(1-anilino-8-naphthalene sulfonic acid) is specifically photoincorporated into the N-terminal domain of αB-crystallin
    • Smulders, R. H. P. H. & de Jong, W. W. (1997) The Hydrophobic probe 4,4′-bis-(1-anilino-8-naphthalene sulfonic acid) is specifically photoincorporated into the N-terminal domain of αB-crystallin, FEBS Lett. 409, 101-104.
    • (1997) FEBS Lett. , vol.409 , pp. 101-104
    • Smulders, R.H.P.H.1    De Jong, W.W.2
  • 48
    • 0030933472 scopus 로고    scopus 로고
    • Conformational and functional differences between recombinant human lens αA and αB-crystallin
    • Sun, T.-X., Das, B. K. & Liang, J. J.-N. (1997) Conformational and functional differences between recombinant human lens αA and αB-crystallin, J. Biol, Chem. 272, 6220-6225.
    • (1997) J. Biol, Chem. , vol.272 , pp. 6220-6225
    • Sun, T.-X.1    Das, B.K.2    Liang, J.J.-N.3
  • 49
    • 0032078745 scopus 로고    scopus 로고
    • NMR spectroscopy of α-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins
    • Carver, J. A. & Lindner, R. A. (1998) NMR spectroscopy of α-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins, Int. J. Biol. Macromol. 22, 197-209.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 50
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-crystallin
    • Hayer-Hartl, M. K., Ewbank, J. J., Creighton, T. E. & Hartl, F. U. (1994) Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-crystallin, EMBO J. 13, 3192-3202.
    • (1994) EMBO J. , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Hartl, F.U.4
  • 51
    • 0028466392 scopus 로고
    • The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
    • Okazaki, A., Ikura, T, Nikaido, K. & Kuwajima, K. (1994) The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state, Nat. Struct. Biol. 1, 439-446.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 439-446
    • Okazaki, A.1    Ikura, T.2    Nikaido, K.3    Kuwajima, K.4
  • 54
    • 0028178722 scopus 로고
    • αA- and αB-crystallin in the retina. Association with the post-Golgi compartment of frog retinal photoreceptors
    • Deretic, D., Aebersold, R. H., Morrison, H. D. & Papermaster, D. S. (1994) αA- and αB-crystallin in the retina. Association with the post-Golgi compartment of frog retinal photoreceptors. J. Biol. Chem. 269, 16853-16861.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16853-16861
    • Deretic, D.1    Aebersold, R.H.2    Morrison, H.D.3    Papermaster, D.S.4
  • 55
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein Hsp25 abolish its actin polymerisation-inhibiting activity
    • Benndorf, R., Hayess, K., Ryazantsev, S., Wieske, M., Behlke, J. & Lutsch, G. (1994) Phosphorylation and supramolecular organization of murine small heat shock protein Hsp25 abolish its actin polymerisation-inhibiting activity, J. Biol. Chem. 269, 20780-20784.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.