메뉴 건너뛰기




Volumn 1764, Issue 3, 2006, Pages 372-383

sHSPs under temperature and pressure: The opposite behaviour of lens alpha-crystallins and yeast HSP26

Author keywords

Alpha crystallin; HSP26; Small angle X ray scattering; Small heat shock protein; Temperature and pressure induced transition

Indexed keywords

ALPHA CRYSTALLIN; DIMER; HEAT SHOCK PROTEIN; RECOMBINANT HUMAN ALPHAB CRYSTALLIN; RECOMBINANT PROTEIN; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 33646007016     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.12.011     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: molecular structure and chaperone function
    • Sun Y., and Macrae T.H. Small heat shock proteins: molecular structure and chaperone function. Cell. Mol. Life Sci. 62 (2005) 2460-2476
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2460-2476
    • Sun, Y.1    Macrae, T.H.2
  • 2
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • van Montfort R., Slingsby C., and Vierling E. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv. Protein Chem. 59 (2001) 105-156
    • (2001) Adv. Protein Chem. , vol.59 , pp. 105-156
    • van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 3
    • 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
    • Basha E., Lee G.J., Breci L.A., Hausrath A.C., Buan N.R., Giese K.C., and Vierling E. 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
  • 4
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin -small heat-shock protein superfamily
    • de Jong W.W., Caspers G.J., and Leunissen J.A. 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
  • 6
    • 13144276278 scopus 로고    scopus 로고
    • Small heat shock protein of Methanococcus jannaschii, a hyperthermophile
    • Kim R., Kim K.K., Yokota H., and Kim S.H. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 9129-9133
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9129-9133
    • Kim, R.1    Kim, K.K.2    Yokota, H.3    Kim, S.H.4
  • 7
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the alpha-crystallin domain fold in a chaperone assembly
    • Stamler R., Kappe G., Boelens W., and Slingsby C. Wrapping the alpha-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353 (2005) 68-79
    • (2005) J. Mol. Biol. , vol.353 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 9
    • 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
    • Bova M.P., McHaourab H.S., Han Y., and Fung B.K. 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
  • 10
    • 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
    • Sobott F., Benesch J.L., Vierling E., and Robinson C.V. 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
  • 12
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun Y., and MacRae T.H. The small heat shock proteins and their role in human disease. FEBS J. 272 (2005) 2613-2627
    • (2005) FEBS J. , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 14
  • 15
    • 0034081704 scopus 로고    scopus 로고
    • sHsp as novel regulators of programmed cell death and tumorigenicity
    • Arrigo A.P. sHsp as novel regulators of programmed cell death and tumorigenicity. Pathol. Biol. (Paris) 48 (2000) 280-288
    • (2000) Pathol. Biol. (Paris) , vol.48 , pp. 280-288
    • Arrigo, A.P.1
  • 16
    • 0037064065 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation
    • Kamradt M.C., Chen F., Sam S., and Cryns V.L. The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J. Biol. Chem. 277 (2002) 38731-38736
    • (2002) J. Biol. Chem. , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 17
    • 0019363271 scopus 로고
    • Enzymes under extremes of physical conditions
    • Jaenicke R. Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10 (1981) 1-67
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 1-67
    • Jaenicke, R.1
  • 18
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • Heremans K. High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11 (1982) 1-21
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 19
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber G., and Drickamer H.G. The effect of high pressure upon proteins and other biomolecules. Q. Rev. Biophys. 16 (1983) 89-112
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 21
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 1595 (2002) 201-209
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 22
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter R. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Biochim. Biophys. Acta 1595 (2002) 160-184
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 160-184
    • Winter, R.1
  • 23
    • 13144290153 scopus 로고    scopus 로고
    • Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins
    • (discussion 562-3)
    • Winter R., and Dzwolak W. Exploring the temperature-pressure configurational landscape of biomolecules: from lipid membranes to proteins. Philos. Trans, A Math. Phys. Eng. Sci. 363 (2005) 537-562 (discussion 562-3)
    • (2005) Philos. Trans, A Math. Phys. Eng. Sci. , vol.363 , pp. 537-562
    • Winter, R.1    Dzwolak, W.2
  • 24
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., and Royer C.A. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem. Sci. 26 (2001) 612-618
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 25
    • 0027405350 scopus 로고
    • Molten-globule conformation of arc repressor monomers determined by high-pressure 1H NMR spectroscopy
    • Peng X., Jonas J., and Silva J. Molten-globule conformation of arc repressor monomers determined by high-pressure 1H NMR spectroscopy. Proc. Natl. Acad. Sci. 90 (1993) 1776-1780
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 1776-1780
    • Peng, X.1    Jonas, J.2    Silva, J.3
  • 26
    • 0034612254 scopus 로고    scopus 로고
    • The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state
    • Ferrao-Gonzales A.D., Souto S.O., Silva J.L., and Foguel D. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc. Natl. Acad. Sci. 97 (2000) 6445-6450
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 6445-6450
    • Ferrao-Gonzales, A.D.1    Souto, S.O.2    Silva, J.L.3    Foguel, D.4
  • 27
    • 0033580633 scopus 로고    scopus 로고
    • Structural characterization of lactate dehydrogenase dissociation under high pressure studied by synchrotron high-pressure small-angle X-ray scattering
    • Fujisawa T., Kato M., and Inoko Y. Structural characterization of lactate dehydrogenase dissociation under high pressure studied by synchrotron high-pressure small-angle X-ray scattering. Biochemistry 38 (1999) 6411-6418
    • (1999) Biochemistry , vol.38 , pp. 6411-6418
    • Fujisawa, T.1    Kato, M.2    Inoko, Y.3
  • 28
    • 0346527362 scopus 로고    scopus 로고
    • Heat-induced quaternary transitions in hetero- and homo-polymers of alpha-crystallin
    • Burgio M.R., Bennett P.M., and Koretz J.F. Heat-induced quaternary transitions in hetero- and homo-polymers of alpha-crystallin. Mol. Vis. 7 (2001) 228-233
    • (2001) Mol. Vis. , vol.7 , pp. 228-233
    • Burgio, M.R.1    Bennett, P.M.2    Koretz, J.F.3
  • 29
    • 0038529737 scopus 로고    scopus 로고
    • Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins
    • Putilina T., Skouri-Panet F., Prat K., Lubsen N.H., and Tardieu A. Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins. J. Biol. Chem. 278 (2003) 13747-13756
    • (2003) J. Biol. Chem. , vol.278 , pp. 13747-13756
    • Putilina, T.1    Skouri-Panet, F.2    Prat, K.3    Lubsen, N.H.4    Tardieu, A.5
  • 30
    • 1242339668 scopus 로고    scopus 로고
    • Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction
    • Regini J.W., Grossmann J.G., Burgio M.R., Malik N.S., Koretz J.F., Hodson S.A., and Elliott G.F. Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction. J. Mol. Biol. 336 (2004) 1185-1194
    • (2004) J. Mol. Biol. , vol.336 , pp. 1185-1194
    • Regini, J.W.1    Grossmann, J.G.2    Burgio, M.R.3    Malik, N.S.4    Koretz, J.F.5    Hodson, S.A.6    Elliott, G.F.7
  • 32
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M., and Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302 (1983) 415-417
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 34
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 10449-10453
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 35
    • 0033984092 scopus 로고    scopus 로고
    • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
    • Sugiyama Y., Suzuki A., Kishigawa M., Akutsu R., Hirose T., Waye M.M., Tsui S.K., Yoshida S., and Ohno S. Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. J. Biol. Chem. 275 (2000) 1095-1104
    • (2000) J. Biol. Chem. , vol.275 , pp. 1095-1104
    • Sugiyama, Y.1    Suzuki, A.2    Kishigawa, M.3    Akutsu, R.4    Hirose, T.5    Waye, M.M.6    Tsui, S.K.7    Yoshida, S.8    Ohno, S.9
  • 36
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz J. Alpha-crystallin. Exp. Eye Res. 76 (2003) 145-153
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 37
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin
    • Aquilina J.A., Benesch J.L., Bateman O.A., Slingsby C., and Robinson C.V. Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10611-10616
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 38
    • 21744436278 scopus 로고    scopus 로고
    • The activation mechanism of Hsp26 does not require dissociation of the oligomer
    • Franzmann T.M., Wuhr M., Richter K., Walter S., and Buchner J. The activation mechanism of Hsp26 does not require dissociation of the oligomer. J. Mol. Biol. 350 (2005) 1083-1093
    • (2005) J. Mol. Biol. , vol.350 , pp. 1083-1093
    • Franzmann, T.M.1    Wuhr, M.2    Richter, K.3    Walter, S.4    Buchner, J.5
  • 39
    • 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
    • Stromer T., Fischer E., Richter K., Haslbeck M., and Buchner J. 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
  • 40
    • 0022887592 scopus 로고
    • Calf lens alpha-crystallin quaternary structure, a three-layer tetrahedral model
    • Tardieu A., Laporte D., Licinio P., Krop B., and Delaye M. Calf lens alpha-crystallin quaternary structure, a three-layer tetrahedral model. J. Mol. Biol. 192 (1986) 711-724
    • (1986) J. Mol. Biol. , vol.192 , pp. 711-724
    • Tardieu, A.1    Laporte, D.2    Licinio, P.3    Krop, B.4    Delaye, M.5
  • 41
    • 0024602852 scopus 로고
    • Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of alpha-crystallin solutions
    • Veretout F., Delaye M., and Tardieu A. Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of alpha-crystallin solutions. J. Mol. Biol. 205 (1989) 713-728
    • (1989) J. Mol. Biol. , vol.205 , pp. 713-728
    • Veretout, F.1    Delaye, M.2    Tardieu, A.3
  • 42
    • 0033920831 scopus 로고    scopus 로고
    • A small-angle X-ray solution scattering study of bovine alpha-crystallin
    • Vanhoudt J., Abgar S., Aerts T., and Clauwaert J. A small-angle X-ray solution scattering study of bovine alpha-crystallin. Eur. J. Biochem. 267 (2000) 3848-3858
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3848-3858
    • Vanhoudt, J.1    Abgar, S.2    Aerts, T.3    Clauwaert, J.4
  • 46
    • 84944815124 scopus 로고
    • Small-angle-scattering-data treatment by the regularization method
    • Svergun D.I., Semenyuk A.V., and Feigin L.A. Small-angle-scattering-data treatment by the regularization method. Acta Crystallogr. A44 (1988) 244-251
    • (1988) Acta Crystallogr. , vol.A44 , pp. 244-251
    • Svergun, D.I.1    Semenyuk, A.V.2    Feigin, L.A.3
  • 47
    • 33646005395 scopus 로고
    • Glatter O., and Kratky O. (Eds), Academic Press, London Vol. Chapt. 2
    • Porod G. Small Angle X-ray Scattering. In: Glatter O., and Kratky O. (Eds) (1982), Academic Press, London Vol. Chapt. 2
    • (1982) Small Angle X-ray Scattering
    • Porod, G.1
  • 48
    • 0742272143 scopus 로고    scopus 로고
    • Recognition and separation of single particles with size variation by statistical analysis of their images
    • White H.E., Saibil H.R., Ignatiou A., and Orlova E.V. Recognition and separation of single particles with size variation by statistical analysis of their images. J. Mol. Biol. 336 (2004) 453-460
    • (2004) J. Mol. Biol. , vol.336 , pp. 453-460
    • White, H.E.1    Saibil, H.R.2    Ignatiou, A.3    Orlova, E.V.4
  • 49
    • 0033580649 scopus 로고    scopus 로고
    • Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering
    • Panick G., Malessa R., and Winter R. Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry 38 (1999) 6512-6519
    • (1999) Biochemistry , vol.38 , pp. 6512-6519
    • Panick, G.1    Malessa, R.2    Winter, R.3
  • 50
    • 0032078724 scopus 로고    scopus 로고
    • alpha-crystallin quaternary structure and interactive properties control eye lens transparency
    • Tardieu A. alpha-crystallin quaternary structure and interactive properties control eye lens transparency. Int. J. Biol. Macromol. 22 (1998) 211-217
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 211-217
    • Tardieu, A.1
  • 51
    • 0037437224 scopus 로고    scopus 로고
    • On the temperature-pressure free-energy landscape of proteins
    • Ravindra R., and Winter R. On the temperature-pressure free-energy landscape of proteins. ChemPhysChem 4 (2003) 359-365
    • (2003) ChemPhysChem , vol.4 , pp. 359-365
    • Ravindra, R.1    Winter, R.2
  • 52
    • 0035815110 scopus 로고    scopus 로고
    • Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of Staphylococcal nuclease
    • Seemann H., Winter R., and Royer C.A. Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of Staphylococcal nuclease. J. Mol. Biol. 307 (2001) 1091-1102
    • (2001) J. Mol. Biol. , vol.307 , pp. 1091-1102
    • Seemann, H.1    Winter, R.2    Royer, C.A.3
  • 53
    • 0037444760 scopus 로고    scopus 로고
    • Chaperone-like activity of alpha-crystallin is enhanced by high-pressure treatment
    • Bode C., Tolgyesi F.G., Smeller L., Heremans K., Avilov S.V., and Fidy J. Chaperone-like activity of alpha-crystallin is enhanced by high-pressure treatment. Biochem. J. 370 (2003) 859-866
    • (2003) Biochem. J. , vol.370 , pp. 859-866
    • Bode, C.1    Tolgyesi, F.G.2    Smeller, L.3    Heremans, K.4    Avilov, S.V.5    Fidy, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.