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Volumn 90, Issue 6, 2010, Pages 688-698

Aggregation of deamidated human βB2-crystallin and incomplete rescue by α-crystallin chaperone

Author keywords

crystallin chaperone; crystallins; Cataracts; Deamidation; Lens; Protein aggregation

Indexed keywords

ALPHA CRYSTALLIN; BETAB2 CRYSTALLIN; CHAPERONE; GLOBULIN; GLUTAMINE; UNCLASSIFIED DRUG; AMIDE; BETA CRYSTALLIN; BETA CRYSTALLIN B2; BETA-CRYSTALLIN B2;

EID: 77952758725     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2010.02.007     Document Type: Article
Times cited : (31)

References (34)
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 1994, D50:760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 5
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M., Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 1983, 302:415-417.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 6
    • 38949117523 scopus 로고    scopus 로고
    • Association of partially folded lens βB2-crystallins with the α-crystallin molecular chaperone
    • Evans P., Slingsby C., Wallace B.A. Association of partially folded lens βB2-crystallins with the α-crystallin molecular chaperone. Biochem. J. 2008, 409:691-699.
    • (2008) Biochem. J. , vol.409 , pp. 691-699
    • Evans, P.1    Slingsby, C.2    Wallace, B.A.3
  • 7
    • 33750078696 scopus 로고    scopus 로고
    • Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding
    • Flaugh S.L., Mills I.A., King J. Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding. J. Biol. Chem. 2006, 281:30782-30793.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30782-30793
    • Flaugh, S.L.1    Mills, I.A.2    King, J.3
  • 8
    • 0036444208 scopus 로고    scopus 로고
    • Unfolding of human lens recombinant βB2- and γC-crystallins
    • Fu L., Liang J.J. Unfolding of human lens recombinant βB2- and γC-crystallins. J. Struct. Biol. 2002, 139:191-198.
    • (2002) J. Struct. Biol. , vol.139 , pp. 191-198
    • Fu, L.1    Liang, J.J.2
  • 9
    • 35648932100 scopus 로고    scopus 로고
    • Post-translational modifications in the nuclear region of young, aged, and cataract human lenses
    • Hains P.G., Truscott R.J. Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J. Proteome Res. 2007, 10:3935-3943.
    • (2007) J. Proteome Res. , vol.10 , pp. 3935-3943
    • Hains, P.G.1    Truscott, R.J.2
  • 10
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K., Misawa K., Kuma K., Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 2002, 30:3059-3066.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 13
    • 33644858451 scopus 로고    scopus 로고
    • Deamidation in human lens βB2-crystallin destabilizes the dimer
    • Lampi K.J., Amyx K.K., Ahmann P., Steel E.A. Deamidation in human lens βB2-crystallin destabilizes the dimer. Biochemistry 2006, 45:3146-3153.
    • (2006) Biochemistry , vol.45 , pp. 3146-3153
    • Lampi, K.J.1    Amyx, K.K.2    Ahmann, P.3    Steel, E.A.4
  • 16
    • 0026354773 scopus 로고
    • High resolution structure of an oligomeric eye lens β-crystallin. Loops, arches, linkers and interfaces in βB2 dimer compared to a monomeric γ-crystallin
    • Lapatto R., Nalini V., Bax B., Driessen H., Lindley P.F., Blundell T.L., Slingsby C. High resolution structure of an oligomeric eye lens β-crystallin. Loops, arches, linkers and interfaces in βB2 dimer compared to a monomeric γ-crystallin. J. Mol. Biol. 1991, 222:1067-1083.
    • (1991) J. Mol. Biol. , vol.222 , pp. 1067-1083
    • Lapatto, R.1    Nalini, V.2    Bax, B.3    Driessen, H.4    Lindley, P.F.5    Blundell, T.L.6    Slingsby, C.7
  • 17
    • 33646377432 scopus 로고    scopus 로고
    • Domain interaction sites of human lens βB2-crystallin
    • Liu B.F., Liang J.J. Domain interaction sites of human lens βB2-crystallin. J. Biol. Chem. 2006, 281:2624-2630.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2624-2630
    • Liu, B.F.1    Liang, J.J.2
  • 18
    • 17744391285 scopus 로고    scopus 로고
    • Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in βB2-crystallin by simulation and experiment
    • MacDonald J.T., Purkiss A.G., Smith M.A., Evans P., Goodfellow J.M., Slingsby C. Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in βB2-crystallin by simulation and experiment. Protein Sci. 2005, 14:1282-1292.
    • (2005) Protein Sci. , vol.14 , pp. 1282-1292
    • MacDonald, J.T.1    Purkiss, A.G.2    Smith, M.A.3    Evans, P.4    Goodfellow, J.M.5    Slingsby, C.6
  • 19
    • 34247580177 scopus 로고    scopus 로고
    • Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin
    • McHaourab H.S., Kumar M.S., Koteiche H.A. Specificity of αA-crystallin binding to destabilized mutants of βB1-crystallin. FEBS Lett. 2007, 581:1939-1943.
    • (2007) FEBS Lett. , vol.581 , pp. 1939-1943
    • McHaourab, H.S.1    Kumar, M.S.2    Koteiche, H.A.3
  • 20
    • 35648997078 scopus 로고    scopus 로고
    • Folding and stability of the isolated Greek key domains of the long-lived human lens proteins γD-crystallin and γS-crystallin
    • Mills I.A., Flaugh S.L., Kosinski-Collins M.S., King J.A. Folding and stability of the isolated Greek key domains of the long-lived human lens proteins γD-crystallin and γS-crystallin. Protein Sci. 2007, 16:2427-2444.
    • (2007) Protein Sci. , vol.16 , pp. 2427-2444
    • Mills, I.A.1    Flaugh, S.L.2    Kosinski-Collins, M.S.3    King, J.A.4
  • 21
    • 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., Tardieu A. Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins. J. Biol. Chem. 2003, 278:13747-13756.
    • (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
  • 22
    • 34347205682 scopus 로고    scopus 로고
    • X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the α-crystallin shell
    • Regini J.W., Grossmann J.G., Timmins P., Harding J.J., Quantock A.J., Hodson S.A., Elliott G.F. X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the α-crystallin shell. Invest. Ophthalmol. Vis. Sci. 2007, 48:2695-2700.
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 2695-2700
    • Regini, J.W.1    Grossmann, J.G.2    Timmins, P.3    Harding, J.J.4    Quantock, A.J.5    Hodson, S.A.6    Elliott, G.F.7
  • 23
    • 2542576224 scopus 로고    scopus 로고
    • Prediction of primary structure deamidation rates of asparaginyl and glutaminyl peptides through steric and catalytic effects
    • Robinson N.E., Robinson A.B. Prediction of primary structure deamidation rates of asparaginyl and glutaminyl peptides through steric and catalytic effects. J. Pept. Res. 2004, 63:437-448.
    • (2004) J. Pept. Res. , vol.63 , pp. 437-448
    • Robinson, N.E.1    Robinson, A.B.2
  • 24
    • 1942437441 scopus 로고    scopus 로고
    • Binding of destabilized βB2-crystallin mutants to α-crystallin: the role of a folding intermediate
    • Sathish H.A., Koteiche H.A., McHaourab H.S. Binding of destabilized βB2-crystallin mutants to α-crystallin: the role of a folding intermediate. J. Biol. Chem. 2004, 279:16425-16432.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16425-16432
    • Sathish, H.A.1    Koteiche, H.A.2    McHaourab, H.S.3
  • 25
  • 26
    • 33646007016 scopus 로고    scopus 로고
    • SHSPs under temperature and pressure: the opposite behaviour of lens alpha-crystallins and yeast HSP26
    • Skouri-Panet F., Quevillon-Cheruel S., Michiel M., Tardieu A., Finet S. sHSPs under temperature and pressure: the opposite behaviour of lens alpha-crystallins and yeast HSP26. Biochim. Biophys. Acta 2006, 1764:372-383.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 372-383
    • Skouri-Panet, F.1    Quevillon-Cheruel, S.2    Michiel, M.3    Tardieu, A.4    Finet, S.5
  • 27
    • 0025371285 scopus 로고
    • Quaternary interactions in eye lens β-crystallins: basic and acidic subunits of β-crystallins favor heterologous association
    • Slingsby C., Bateman O.A. Quaternary interactions in eye lens β-crystallins: basic and acidic subunits of β-crystallins favor heterologous association. Biochemistry 1990, 29:6592-6599.
    • (1990) Biochemistry , vol.29 , pp. 6592-6599
    • Slingsby, C.1    Bateman, O.A.2
  • 28
    • 33947723561 scopus 로고    scopus 로고
    • Mutation of interfaces in domain-swapped human βB2-crystallin
    • Smith M.A., Bateman O.A., Jaenicke R., Slingsby C. Mutation of interfaces in domain-swapped human βB2-crystallin. Protein Sci. 2007, 16:615-625.
    • (2007) Protein Sci. , vol.16 , pp. 615-625
    • Smith, M.A.1    Bateman, O.A.2    Jaenicke, R.3    Slingsby, C.4
  • 29
    • 34547631078 scopus 로고    scopus 로고
    • Deamidation alters the structure and decreases the stability of human lens βA3-crystallin
    • Takata T., Oxford J.T., Brandon T.R., Lampi K.J. Deamidation alters the structure and decreases the stability of human lens βA3-crystallin. Biochemistry 2007, 46:8861-8871.
    • (2007) Biochemistry , vol.46 , pp. 8861-8871
    • Takata, T.1    Oxford, J.T.2    Brandon, T.R.3    Lampi, K.J.4
  • 30
    • 50049119429 scopus 로고    scopus 로고
    • Deamidation destabilizes and triggers aggregation of a lens protein, βA3-crystallin
    • Takata T., Oxford J.T., Demeler B., Lampi K.J. Deamidation destabilizes and triggers aggregation of a lens protein, βA3-crystallin. Protein Sci. 2008, 17:1565-1575.
    • (2008) Protein Sci. , vol.17 , pp. 1565-1575
    • Takata, T.1    Oxford, J.T.2    Demeler, B.3    Lampi, K.J.4
  • 31
    • 28644447919 scopus 로고    scopus 로고
    • Identification of posttranslational modifications by blind search of mass spectra
    • Tsur D., Tanner S., Zandi E., Bafna V., Pevzner P.A. Identification of posttranslational modifications by blind search of mass spectra. Nat. Biotechnol. 2005, 23:1562-1567.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1562-1567
    • Tsur, D.1    Tanner, S.2    Zandi, E.3    Bafna, V.4    Pevzner, P.A.5
  • 33
    • 0033525632 scopus 로고    scopus 로고
    • Folding and self-assembly of the domains of βB2-crystallin from rat eye lens
    • Wieligmann K., Mayr E.M., Jaenicke R. Folding and self-assembly of the domains of βB2-crystallin from rat eye lens. J. Mol. Biol. 1999, 286:989-994.
    • (1999) J. Mol. Biol. , vol.286 , pp. 989-994
    • Wieligmann, K.1    Mayr, E.M.2    Jaenicke, R.3
  • 34
    • 33750142707 scopus 로고    scopus 로고
    • Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?
    • Wilmarth P.A., Tanner S., Dasari S., Nagalla S.R., Riviere M.A., Bafna V., Pevzner P.A., David L.L. Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?. J. Proteome Res. 2006, 10:2554-2566.
    • (2006) J. Proteome Res. , vol.10 , pp. 2554-2566
    • Wilmarth, P.A.1    Tanner, S.2    Dasari, S.3    Nagalla, S.R.4    Riviere, M.A.5    Bafna, V.6    Pevzner, P.A.7    David, L.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.