메뉴 건너뛰기




Volumn 294, Issue 2, 1999, Pages 561-577

Folding pattern of the α-crystallin domain in αA-crystallin determined by site-directed spin labeling

Author keywords

Electron paramagnetic resonance; Homology modeling; Site directed spin labeling; Small heat shock proteins; A crystallin

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; IMMUNOGLOBULIN; LENS PROTEIN; NITROXIDE; SOLVENT;

EID: 0033607618     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3242     Document Type: Article
Times cited : (107)

References (56)
  • 1
    • 0030741276 scopus 로고    scopus 로고
    • Structure and function of the conserved domain in αa-crystallin. Site-directed spin labeling identifies a β-strand located near a subunit interface
    • Berengian A. R., Bova M. P., Mchaourab H. S. Structure and function of the conserved domain in αA-crystallin. Site-directed spin labeling identifies a β-strand located near a subunit interface. Biochemistry. 36:1997;9951-9957.
    • (1997) Biochemistry , vol.36 , pp. 9951-9957
    • Berengian, A.R.1    Bova, M.P.2    Mchaourab, H.S.3
  • 2
    • 0033525723 scopus 로고    scopus 로고
    • Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins
    • Berengian A. R., Parfenova M., Mchaourab H. S. Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins. J. Biol. Chem. 274:1999;6305-6314.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6305-6314
    • Berengian, A.R.1    Parfenova, M.2    Mchaourab, H.S.3
  • 3
    • 0020482581 scopus 로고
    • A novel reversible thiol-specific spin label: Papain active site labeling and inhibition
    • Berliner L. J., Grunwald J., Hankovszky H. O., Hideg K. A novel reversible thiol-specific spin label: papain active site labeling and inhibition. Anal. Biochem. 119:1982;450-455.
    • (1982) Anal. Biochem. , vol.119 , pp. 450-455
    • Berliner, L.J.1    Grunwald, J.2    Hankovszky, H.O.3    Hideg, K.4
  • 4
    • 0028172534 scopus 로고
    • The immunoglobulin fold: Structural classification, sequence patterns and common core
    • Bork P., Holm L., Sander C. The immunoglobulin fold: structural classification, sequence patterns and common core. J. Mol. Biol. 242:1994;309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A. L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 7
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved "α-crystallin domain"
    • Caspers G., Leunissen J. A. M., de Jong W. W. The expanding small heat-shock protein family, and structure predictions of the conserved "α-crystallin domain" J. Mol. Evol. 40:1995;238-248.
    • (1995) J. Mol. Evol. , vol.40 , pp. 238-248
    • Caspers, G.1    Leunissen, J.A.M.2    De Jong, W.W.3
  • 8
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16. 3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang Z., Primm T. P., Jakana J., Lee I. H., Serysheva I., Chiu W., Gilbert H. F., Quiocho F. A. Mycobacterium tuberculosis 16-kDa antigen (Hsp16. 3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J. Biol. Chem. 271:1996;7218-7223.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7    Quiocho, F.A.8
  • 9
    • 0021118508 scopus 로고
    • Principles that determine the structure of proteins
    • Chothia C. Principles that determine the structure of proteins. Annu. Rev. Biochem. 53:1984;537-572.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 537-572
    • Chothia, C.1
  • 10
    • 0025277191 scopus 로고
    • The classification and origins of protein folding patterns
    • Chothia C., Finkelstein A. V. The classification and origins of protein folding patterns. Annu. Rev. Biochem. 59:1990;1007-1039.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 1007-1039
    • Chothia, C.1    Finkelstein, A.V.2
  • 11
    • 0000977124 scopus 로고
    • Relative orientation of close-packed β-pleated sheets in proteins
    • Chothia C., Janin J. Relative orientation of close-packed β-pleated sheets in proteins. Proc. Natl Acad. Sci. USA. 78:1981;4146-4150.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4146-4150
    • Chothia, C.1    Janin, J.2
  • 12
    • 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. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin. FEBS Letters. 369:1995;321-325.
    • (1995) FEBS Letters , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 13
    • 0027472047 scopus 로고
    • Evolution of the α-crystallin/small heat-shock protein family
    • de Jong W. W., Leunissen J. A., Voorter C. E. Evolution of the α-crystallin/small heat-shock protein family. Mol. Biol. Evol. 10:1993;103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 14
  • 15
    • 34548200331 scopus 로고    scopus 로고
    • Protein folding and misfolding inside and outside the cell
    • Dobson C. M., Ellis R. J. Protein folding and misfolding inside and outside the cell. EMBO J. 17:1998;5251-5254.
    • (1998) EMBO J. , vol.17 , pp. 5251-5254
    • Dobson, C.M.1    Ellis, R.J.2
  • 17
    • 0000098859 scopus 로고
    • Resolved electron-electron spin-spin splittings in EPR spectra
    • L. J. Berliner, & J. Reuben. New York: Plenum Press
    • Eaton G. R., Eaton S. S. Resolved electron-electron spin-spin splittings in EPR spectra. Berliner L. J., Reuben J. Biological Magnetic Resonance. 1989;340-397 Plenum Press, New York.
    • (1989) Biological Magnetic Resonance , pp. 340-397
    • Eaton, G.R.1    Eaton, S.S.2
  • 18
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M., Graber S., Gaestel M., Buchner J. 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
  • 19
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis R. J., Hartl F. U. Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 9:1999;102-110.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 20
    • 0027016905 scopus 로고
    • Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin
    • Farahbakhsh Z. T., Altenbach C., Hubbell W. L. Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin. Photochem. Photobiol. 56:1992;1019-1033.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1019-1033
    • Farahbakhsh, Z.T.1    Altenbach, C.2    Hubbell, W.L.3
  • 22
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, αb-crystallin, has a variable quaternary structure
    • Haley D. A., Horwitz J., Stewart P. L. The small heat-shock protein, αB-crystallin, has a variable quaternary structure. J. Mol. Biol. 277:1998;27-35.
    • (1998) J. Mol. Biol. , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 23
    • 0030066039 scopus 로고    scopus 로고
    • Distinguishing helix conformations in alanine-rich peptides using unnatural amino acid TOAC and electron spin resonance
    • Hanson P., Martinez G., Millhauser G., Formaggio F., Crisma M., Toniolo C., Vita C. Distinguishing helix conformations in alanine-rich peptides using unnatural amino acid TOAC and electron spin resonance. J. Am. Chem. Soc. 118:1996a;271-272.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 271-272
    • Hanson, P.1    Martinez, G.2    Millhauser, G.3    Formaggio, F.4    Crisma, M.5    Toniolo, C.6    Vita, C.7
  • 24
    • 0029758045 scopus 로고    scopus 로고
    • ESR characterization of hexameric, helical peptides using double TOAC spin labeling
    • Hanson P., Millhauser G., Formaggio F., Crisma M., Toniolo C. ESR characterization of hexameric, helical peptides using double TOAC spin labeling. J. Am. Chem. Soc. 118:1996b;7618-7625.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7618-7625
    • Hanson, P.1    Millhauser, G.2    Formaggio, F.3    Crisma, M.4    Toniolo, C.5
  • 25
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz J. α-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
  • 27
    • 2142750383 scopus 로고
    • Continuous and stopped flow EPR spectrometer based on a loop gap resonator
    • Hubbell W. L., Froncisz W., Hyde J. S. Continuous and stopped flow EPR spectrometer based on a loop gap resonator. Rev. Sci. Instrum. 58:1987;1879-1886.
    • (1987) Rev. Sci. Instrum. , vol.58 , pp. 1879-1886
    • Hubbell, W.L.1    Froncisz, W.2    Hyde, J.S.3
  • 29
    • 0030950516 scopus 로고    scopus 로고
    • Molecular distances from dipolar coupled spin-labels: The global analysis of multifrequency continuous wave electron paramagnetic resonance data
    • Hustedt E. J., Smirnov A. I., Laub C. F., Cobb C. E., Beth A. H. Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data. Biophys. J. 72:1997;1861-1877.
    • (1997) Biophys. J. , vol.72 , pp. 1861-1877
    • Hustedt, E.J.1    Smirnov, A.I.2    Laub, C.F.3    Cobb, C.E.4    Beth, A.H.5
  • 30
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim K. K., Kim R., Kim S.-H. 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
  • 31
    • 0032555364 scopus 로고    scopus 로고
    • Caenorhabditis elegans small heat-shock proteins Hsp12. 2 and Hsp12. 3 form tetramers and no chaperone-like activity
    • Kokke B. P. A., Leroux M. R., Candido E. P. M., Boelens W. C., de Jong W. W. Caenorhabditis elegans small heat-shock proteins Hsp12. 2 and Hsp12. 3 form tetramers and no chaperone-like activity. FEBS Letters. 433:1998;228-232.
    • (1998) FEBS Letters , vol.433 , pp. 228-232
    • Kokke, B.P.A.1    Leroux, M.R.2    Candido, E.P.M.3    Boelens, W.C.4    De Jong, W.W.5
  • 32
    • 0032530971 scopus 로고    scopus 로고
    • Identification of protein folding patterns using site-directed spin labeling. Structural characterization of a β-sheet and putative substrate binding regions in the conserved domain of αa-crystallin
    • Koteiche H. A., Berengian A. R., Mchaourab H. S. Identification of protein folding patterns using site-directed spin labeling. Structural characterization of a β-sheet and putative substrate binding regions in the conserved domain of αA-crystallin. Biochemistry. 37:1998;12681-12688.
    • (1998) Biochemistry , vol.37 , pp. 12681-12688
    • Koteiche, H.A.1    Berengian, A.R.2    Mchaourab, H.S.3
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee G. J., Pokala N., Vierling E. Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J. Biol. Chem. 270:1995;10432-10438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 35
    • 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. 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
  • 36
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • Matthews B. W. Studies on protein stability with T4 lysozyme. Advan. Protein Chem. 46:1995;249-278.
    • (1995) Advan. Protein Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 37
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side-chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab H. S., Lietzow M. A., Hideg K., Hubbell W. L. Motion of spin-labeled side-chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry. 35:1996;7692-7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 38
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • Mchaourab H. S., Oh K. J., Fang C. J., Hubbell W. L. Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry. 36:1997a;307-316.
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • Mchaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 39
    • 0030732692 scopus 로고    scopus 로고
    • Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the α-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface
    • Mchaourab H. S., Berengian A. R., Koteiche H. A. Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the α-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface. Biochemistry. 36:1997b;14627-14634.
    • (1997) Biochemistry , vol.36 , pp. 14627-14634
    • Mchaourab, H.S.1    Berengian, A.R.2    Koteiche, H.A.3
  • 40
    • 0026783919 scopus 로고
    • Short alanine-based peptides may form 3(10)-helices and not α-helices in aqueous solution
    • Miick S. M., Martinez G. V., Fiori W. R., Todd A. P., Millhauser G. L. Short alanine-based peptides may form 3(10)-helices and not α-helices in aqueous solution. Nature. 359:1992;653-655.
    • (1992) Nature , vol.359 , pp. 653-655
    • Miick, S.M.1    Martinez, G.V.2    Fiori, W.R.3    Todd, A.P.4    Millhauser, G.L.5
  • 43
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell D. A., Lindquist S. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27:1993;437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 44
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell D. A., Kowal A. S., Singer M. A., Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 372:1994;475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 47
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein M. D., Shin Y. K. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl Acad. Sci. USA. 92:1995;8239-8243.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 48
    • 0031740095 scopus 로고    scopus 로고
    • Molecular studies of prion diseases
    • Safar J., Prusiner S. B. Molecular studies of prion diseases. Prog. Brain Res. 117:1998;421-434.
    • (1998) Prog. Brain Res. , vol.117 , pp. 421-434
    • Safar, J.1    Prusiner, S.B.2
  • 49
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., Blundell T. L. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 50
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone α-crystallin: Identification of binding sites in αb-crystallin
    • Sharma K. K., Kaur H., Kester K. Functional elements in molecular chaperone α-crystallin: identification of binding sites in αB-crystallin. Biochem. Biophys. Res. Commun. 239:1997;217-222.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 217-222
    • Sharma, K.K.1    Kaur, H.2    Kester, K.3
  • 52
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative diseases
    • Stott K., Blackburn J. M., Butler P. J. G., Perutz M. Incorporation of glutamine repeats makes protein oligomerize: Implications for neurodegenerative diseases. Proc. Natl Acad. Sci. USA. 92:1995;6509-6513.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.G.3    Perutz, M.4
  • 53
    • 0031962334 scopus 로고    scopus 로고
    • Intermolecular exchange and stabilization of recombinant human αa- And αb-crystallin
    • Sun T. X., Liang J. J. N. Intermolecular exchange and stabilization of recombinant human αA- and αB-crystallin. J. Biol. Chem. 273:1998;286-290.
    • (1998) J. Biol. Chem. , vol.273 , pp. 286-290
    • Sun, T.X.1    Liang, J.J.N.2
  • 54
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. 4 Å resolution
    • Sutton R. B., Fasshauer D., Jahn R., Brunger A. T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2. 4 Å resolution. Nature. 395:1998;347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 55
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski J. Q., Goedert M., Iwatsubo T., Lee V. M. Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ. 5:1998;832-837.
    • (1998) Cell Death Differ. , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.