메뉴 건너뛰기




Volumn 12, Issue , 2006, Pages 1372-1379

The cataract-causing mutation G98R in human αA-crystallin leads to folding defects and loss of chaperone activity

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; ARGININE; CHAPERONE; GLYCINE; INSULIN; UREA;

EID: 33751518175     PISSN: 10900535     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (36)

References (47)
  • 1
    • 0010503986 scopus 로고
    • Complete structure of the alpha B-crystallin gene: Conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes
    • Quax-Jeuken Y, Quax W, van Rens G, Khan PM, Bloemendal H. Complete structure of the alpha B-crystallin gene: conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes. Proc Natl Acad Sci U S A 1985; 82:5819-23.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 5819-5823
    • Quax-Jeuken, Y.1    Quax, W.2    van Rens, G.3    Khan, P.M.4    Bloemendal, H.5
  • 2
    • 0028254544 scopus 로고
    • Expression of the alpha-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues
    • Sax CM, Piatigorsky J. Expression of the alpha-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues. Adv Enzymol Relat Areas Mol Biol 1994; 69:155-201.
    • (1994) Adv Enzymol Relat Areas Mol Biol , vol.69 , pp. 155-201
    • Sax, C.M.1    Piatigorsky, J.2
  • 3
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci U S A 1982; 79:2360-4.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 4
    • 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 1992; 89:10449-53.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 5
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystallin
    • Raman B, Rao CM. Chaperone-like activity and quaternary structure of alpha-crystallin. J Biol Chem 1994; 269:27264-8.
    • (1994) J Biol Chem , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.M.2
  • 6
    • 0030933472 scopus 로고    scopus 로고
    • Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin
    • Sun TX, Das BK, Liang JJ. Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin. J Biol Chem 1997; 272:6220-5.
    • (1997) J Biol Chem , vol.272 , pp. 6220-6225
    • Sun, T.X.1    Das, B.K.2    Liang, J.J.3
  • 7
    • 0033588379 scopus 로고    scopus 로고
    • Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins
    • Kumar LV, Ramakrishna T, Rao CM. Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins. J Biol Chem 1999; 274:24137-41.
    • (1999) J Biol Chem , vol.274 , pp. 24137-24141
    • Kumar, L.V.1    Ramakrishna, T.2    Rao, C.M.3
  • 8
    • 0033521012 scopus 로고    scopus 로고
    • Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates
    • Datta SA, Rao CM. Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates. J Biol Chem 1999; 274:34773-8.
    • (1999) J Biol Chem , vol.274 , pp. 34773-34778
    • Datta, S.A.1    Rao, C.M.2
  • 9
    • 0035947181 scopus 로고    scopus 로고
    • Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation
    • Rajaraman K, Raman B, Ramakrishna T, Rao CM. Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation. FEBS Lett 2001; 497:118-23.
    • (2001) FEBS Lett , vol.497 , pp. 118-123
    • Rajaraman, K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 10
    • 0030758693 scopus 로고    scopus 로고
    • Molecular chaperones protect catalase against thermal stress
    • Hook DW, Harding JJ. Molecular chaperones protect catalase against thermal stress. Eur J Biochem 1997; 247:380-5.
    • (1997) Eur J Biochem , vol.247 , pp. 380-385
    • Hook, D.W.1    Harding, J.J.2
  • 11
    • 0034693132 scopus 로고    scopus 로고
    • Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress
    • Marini I, Moschini R, Del Corso A, Mura U. Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress. J Biol Chem 2000; 275:32559-65.
    • (2000) J Biol Chem , vol.275 , pp. 32559-32565
    • Marini, I.1    Moschini, R.2    Del Corso, A.3    Mura, U.4
  • 12
    • 18844471719 scopus 로고    scopus 로고
    • Protection of a restriction enzyme from heat inactivation by [alpha]-crystallin
    • Hess JF, FitzGerald PG. Protection of a restriction enzyme from heat inactivation by [alpha]-crystallin. Mol Vis 1998; 4:29.
    • (1998) Mol Vis , vol.4 , pp. 29
    • Hess, J.F.1    FitzGerald, P.G.2
  • 13
    • 0035504258 scopus 로고    scopus 로고
    • Unfolding and refolding of a quinone oxidoreductase: Alpha-crystallin, a molecular chaperone, assists its reactivation
    • Goenka S, Raman B, Ramakrishna T, Rao CM. Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation. Biochem J 2001; 359:547-56.
    • (2001) Biochem J , vol.359 , pp. 547-556
    • Goenka, S.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 14
    • 0032540350 scopus 로고    scopus 로고
    • Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme
    • Rawat U, Rao M. Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme. J Biol Chem 1998; 273:9415-23.
    • (1998) J Biol Chem , vol.273 , pp. 9415-9423
    • Rawat, U.1    Rao, M.2
  • 15
    • 0036838853 scopus 로고    scopus 로고
    • Alpha-crystallin and ATP facilitate the in vitro renaturation of xylanase: Enhancement of refolding by metal ions
    • Nath D, Rawat U, Anish R, Rao M. Alpha-crystallin and ATP facilitate the in vitro renaturation of xylanase: enhancement of refolding by metal ions. Protein Sci 2002; 11:2727-34.
    • (2002) Protein Sci , vol.11 , pp. 2727-2734
    • Nath, D.1    Rawat, U.2    Anish, R.3    Rao, M.4
  • 16
    • 0028899440 scopus 로고
    • Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications
    • Cherian M, Abraham EC. Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Biochem Biophys Res Commun 1995; 208:675-9.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 675-679
    • Cherian, M.1    Abraham, E.C.2
  • 17
    • 0027217891 scopus 로고
    • alpha-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract
    • Kelley MJ, David LL, Iwasaki N, Wright J, Shearer TR. alpha-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J Biol Chem 1993; 268:18844-9.
    • (1993) J Biol Chem , vol.268 , pp. 18844-18849
    • Kelley, M.J.1    David, L.L.2    Iwasaki, N.3    Wright, J.4    Shearer, T.R.5
  • 18
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW, Weleber RG. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 1998; 7:471-4.
    • (1998) Hum Mol Genet , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 20
    • 0034673151 scopus 로고    scopus 로고
    • Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function
    • Shroff NP, Cherian-Shaw M, Bera S, Abraham EC. Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function. Biochemistry 2000; 39:1420-6.
    • (2000) Biochemistry , vol.39 , pp. 1420-1426
    • Shroff, N.P.1    Cherian-Shaw, M.2    Bera, S.3    Abraham, E.C.4
  • 21
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL, Horwitz J. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci U S A 1999; 96:6137-42.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 22
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng MD, Muchowski PJ, van Den IJssel P, Wu GJ, Hutcheson AM, Clark JI, Quinlan RA. The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J Biol Chem 1999; 274:33235-43.
    • (1999) J Biol Chem , vol.274 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2    van Den, I.3    Jssel, P.4    Wu, G.J.5    Hutcheson, A.M.6    Clark, J.I.7    Quinlan, R.A.8
  • 23
    • 33744903422 scopus 로고    scopus 로고
    • Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding
    • Koteiche HA, Mchaourab HS. Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding. J Biol Chem 2006; 281:14273-9.
    • (2006) J Biol Chem , vol.281 , pp. 14273-14279
    • Koteiche, H.A.1    Mchaourab, H.S.2
  • 25
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • Mackay DS, Andley UP, Shiels A. Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur J Hum Genet 2003; 11:784-93.
    • (2003) Eur J Hum Genet , vol.11 , pp. 784-793
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 30
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci 1995; 4:2411-23.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 31
    • 0029034730 scopus 로고
    • Temperature dependent chaperone-like activity of alpha-crystallin
    • Raman B, Ramakrishna T, Rao CM. Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett 1995; 365:133-6.
    • (1995) FEBS Lett , vol.365 , pp. 133-136
    • Raman, B.1    Ramakrishna, T.2    Rao, C.M.3
  • 32
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein CH. Production of soluble recombinant proteins in bacteria. Bio/ Technology 1989; 7:1141-1149.
    • (1989) Bio/Technology , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 33
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sorensen HP, Mortensen KK. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 2005; 4:1.
    • (2005) Microb Cell Fact , vol.4 , pp. 1
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 34
    • 0029117227 scopus 로고
    • Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins
    • Raman B, Ramakrishna T, Rao CM. Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins. J Biol Chem 1995; 270:19888-92.
    • (1995) J Biol Chem , vol.270 , pp. 19888-19892
    • Raman, B.1    Ramakrishna, T.2    Rao, C.M.3
  • 35
    • 0022255566 scopus 로고
    • 4,4′-Bis[8-(phenylamino) naphthalene-1-sulfonate] binding to human thrombins: A sensitive exo site fluorescent affinity probe
    • Musci G, Metz GD, Tsunematsu H, Berliner LJ. 4,4′-Bis[8-(phenylamino) naphthalene-1-sulfonate] binding to human thrombins: a sensitive exo site fluorescent affinity probe. Biochemistry 1985; 24:2034-9.
    • (1985) Biochemistry , vol.24 , pp. 2034-2039
    • Musci, G.1    Metz, G.D.2    Tsunematsu, H.3    Berliner, L.J.4
  • 36
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • Shi L, Palleros DR, Fink AL. Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 1994; 33:7536-46.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 37
    • 0029124685 scopus 로고
    • Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin
    • Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett 1995; 369:321-5.
    • (1995) FEBS Lett , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 38
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone alpha-crystallin: Identification of binding sites in alpha B-crystallin
    • Sharma KK, Kaur H, Kester K. Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-crystallin. Biochem Biophys Res Commun 1997; 239:217-22.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 217-222
    • Sharma, K.K.1    Kaur, H.2    Kester, K.3
  • 39
    • 0032546801 scopus 로고    scopus 로고
    • Identification of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in alpha-crystallin
    • Sharma KK, Kumar GS, Murphy AS, Kester K. Identification of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in alpha-crystallin. J Biol Chem 1998; 273:15474-8.
    • (1998) J Biol Chem , vol.273 , pp. 15474-15478
    • Sharma, K.K.1    Kumar, G.S.2    Murphy, A.S.3    Kester, K.4
  • 40
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin
    • Sharma KK, Kumar RS, Kumar GS, Quinn PT. Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin. J Biol Chem 2000; 275:3767-71.
    • (2000) J Biol Chem , vol.275 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 41
    • 0000410878 scopus 로고
    • Fractionation of oxidized insulin
    • Sanger F. Fractionation of oxidized insulin. Biochem J 1949; 44:126-8.
    • (1949) Biochem J , vol.44 , pp. 126-128
    • Sanger, F.1
  • 42
    • 0030798628 scopus 로고    scopus 로고
    • Chaperone-like activity and temperature-induced structural changes of alpha-crystallin
    • Raman B, Rao CM. Chaperone-like activity and temperature-induced structural changes of alpha-crystallin. J Biol Chem 1997; 272:23559-64.
    • (1997) J Biol Chem , vol.272 , pp. 23559-23564
    • Raman, B.1    Rao, C.M.2
  • 43
    • 0034681446 scopus 로고    scopus 로고
    • Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins
    • Reddy GB, Das KP, Petrash JM, Surewicz WK. Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins. J Biol Chem 2000; 275:4565-70.
    • (2000) J Biol Chem , vol.275 , pp. 4565-4570
    • Reddy, G.B.1    Das, K.P.2    Petrash, J.M.3    Surewicz, W.K.4
  • 44
    • 0028984242 scopus 로고
    • On the thermal stability of alpha-crystallin: A new insight from infrared spectroscopy
    • Surewicz WK, Olesen PR. On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy. Biochemistry 1995; 34:9655-60.
    • (1995) Biochemistry , vol.34 , pp. 9655-9660
    • Surewicz, W.K.1    Olesen, P.R.2
  • 45
    • 0025787736 scopus 로고
    • Micellar subunit assembly in a three-layer model of oligomeric alpha-crystallin
    • Walsh MT, Sen AC, Chakrabarti B. Micellar subunit assembly in a three-layer model of oligomeric alpha-crystallin. J Biol Chem 1991; 266:20079-84.
    • (1991) J Biol Chem , vol.266 , pp. 20079-20084
    • Walsh, M.T.1    Sen, A.C.2    Chakrabarti, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.