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Volumn 50, Issue 34, 2011, Pages 7330-7340

Characterization of the unfolding process of the tetrameric and dimeric forms of Cratylia mollis seed lectin (CRAMOLL 1): Effects of natural fragmentation on protein stability

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL PROPERTIES; CHEMICAL CROSS-LINKING; HIGH TEMPERATURE; LEGUMINOSAE; MONOMERIC INTERMEDIATE; PH-DEPENDENT; PROTEIN STABILITY; SEED COTYLEDONS; SUGAR-BINDING ACTIVITY; TETRAMERS; UNFOLDING PROCESS;

EID: 80051974926     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200320x     Document Type: Article
Times cited : (21)

References (51)
  • 2
    • 0025222989 scopus 로고
    • Legume lectins - A large family of homologous proteins
    • Sharon, N. and Lis, H. (1990) Legume lectins - a large family of homologous proteins FASEB J. 4, 3198-3208 (Pubitemid 120012565)
    • (1990) FASEB Journal , vol.4 , Issue.14 , pp. 3198-3208
    • Sharon, N.1    Lis, H.2
  • 3
    • 0033120809 scopus 로고    scopus 로고
    • Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins
    • DOI 10.1002/(SICI)1097-0134(1999 0401)35:1<58::AID-PROT6>3.0.CO;2-A
    • Prabu, M. M., Suguma, K., and Vijayan, M. (1999) Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins Proteins: Struct., Funct., Genet. 35, 58-69 (Pubitemid 29128153)
    • (1999) Proteins: Structure, Function and Genetics , vol.35 , Issue.1 , pp. 58-69
    • Prabu, M.M.1    Suguna, K.2    Vijayan, M.3
  • 5
    • 0029437098 scopus 로고
    • Purification of a glucose/manose specific Lectin, isoforma 1, from seeds of Cratylia mollis Mart. (Camaratu bean)
    • Correia, M. T. S. and Coelho, L. C. B. B. (1995) Purification of a glucose/manose specific Lectin, isoforma 1, from seeds of Cratylia mollis Mart. (Camaratu bean) Appl. Biochem. Biotechnol. 55, 261-273
    • (1995) Appl. Biochem. Biotechnol. , vol.55 , pp. 261-273
    • Correia, M.T.S.1    Coelho, L.C.B.B.2
  • 7
    • 0031144784 scopus 로고    scopus 로고
    • Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase
    • PII S0144861797000349
    • Lima, V. L. M., Correia, M. T. S., Cechinel, Y. M. N., Sampaio, C. A. M., Owen, J. S., and Coêlho, L. C. B. B. (1997) Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase Carbohydr. Polym. 33, 27-32 (Pubitemid 127376673)
    • (1997) Carbohydrate Polymers , vol.33 , Issue.1 , pp. 27-32
    • Lima, V.L.M.1    Correia, M.T.S.2    Cechinel, Y.M.N.3    Sampaio, C.A.M.4    Owen, J.S.5    Coelho, L.C.B.B.6
  • 9
    • 0035480468 scopus 로고    scopus 로고
    • A novel model to characterize the electric double layer of lectins from Cratylia mollis (Camaratu bean) and Canavalia ensiformis adsorbed on metallic surface
    • DOI 10.1016/S0144-8617(00)00299-X, PII S014486170000299X
    • Souza, S. R., Correia, M. T. S., Pessoa, M. M. A., Kennedy, J. F., Lima-Filho, J. L., and Coelho, L. C. B. B. (2001) A novel model to characterize the electric double layer of lectins from Cratylia mollis (Camaratu bean) and Canavalia ensiformis adsorbed on metallic surface Carbohydr. Polym. 46, 191-193 (Pubitemid 32605623)
    • (2001) Carbohydrate Polymers , vol.46 , Issue.2 , pp. 191-193
    • Souza, S.R.1    Correia, M.T.S.2    Pessoa, M.M.A.3    Kennedy, J.F.4    Lima-Filho, J.L.5    Coelho, L.C.B.B.6
  • 10
    • 1542513237 scopus 로고    scopus 로고
    • Mitogenic activity of Cratylia mollis lectin on human lymphocytes
    • DOI 10.1016/j.biologicals.2003.12.001, PII S1045105603001027
    • Maciel, E. V., Araújo-Filho, V. S., Nakazawa, M., Gomes, Y. M., Coelho, L. C., and Correia, M. T. (2004) Mitogenic activity of Cratylia mollis lectin on human lymphocytes Biologicals 32, 57-60 (Pubitemid 38333185)
    • (2004) Biologicals , vol.32 , Issue.1 , pp. 57-60
    • Maciel, E.V.M.1    Araujo-Filho, V.S.2    Nakazawa, M.3    Gomes, Y.M.4    Coelho, L.C.B.B.5    Correia, M.T.S.6
  • 12
    • 47249087220 scopus 로고    scopus 로고
    • Electrochemical evaluation of lectin-sugar interaction on gold electrode modified with colloidal gold and polyvinyl butyral
    • Oliveira, M. D. L., Correia, M. T. S., Coelho, L. C. B. B., and Diniz, F. B. (2008) Electrochemical evaluation of lectin-sugar interaction on gold electrode modified with colloidal gold and polyvinyl butyral Colloids Surf., B 66, 13-19
    • (2008) Colloids Surf., B , vol.66 , pp. 13-19
    • Oliveira, M.D.L.1    Correia, M.T.S.2    Coelho, L.C.B.B.3    Diniz, F.B.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfeld, R. A., Lewis, U. J., and Williams, D. E. (1962) Disk electrophoresis of basic proteins and peptides on polyacrylamide gels Nature 195, 281-283
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 21
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6, 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 23
    • 0023055734 scopus 로고
    • Pressure dissociation and conformational drift of the β dimer of tryptophan synthase
    • Silva, J. L., Moles, E. W., and Weber, G. (1986) Pressure dissociation and conformational drift of the β dimer of tryptophan synthase Biochemistry 25, 5781-5786
    • (1986) Biochemistry , vol.25 , pp. 5781-5786
    • Silva, J.L.1    Moles, E.W.2    Weber, G.3
  • 24
    • 0023051519 scopus 로고
    • Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure
    • Royer, C. A., Weber, G., Daly, T. J., and Matthews, K. S. (1986) Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure Biochemistry 25, 8308-8315
    • (1986) Biochemistry , vol.25 , pp. 8308-8315
    • Royer, C.A.1    Weber, G.2    Daly, T.J.3    Matthews, K.S.4
  • 25
    • 0002893631 scopus 로고
    • Folding Proteins
    • in (Creighton, T. E. Ed.) pp, IRL Press, Oxford.
    • Jaenicke, R. and Rudolph, R. (1989) Folding Proteins, in Protein Structure a Practical Approach (Creighton, T. E., Ed.) pp 191-223, IRL Press, Oxford.
    • (1989) Protein Structure A Practical Approach , pp. 191-223
    • Jaenicke, R.1    Rudolph, R.2
  • 26
    • 0017303493 scopus 로고
    • Formation of hybrid concanavalin A molecules by subunit exchange
    • Fraser, A. R., Wang, J. L., and Edelman, G. (1976) Formation of hybrid concanavalin A molecules by subunit exchange J. Biol. Chem. 251, 4622-4628
    • (1976) J. Biol. Chem. , vol.251 , pp. 4622-4628
    • Fraser, A.R.1    Wang, J.L.2    Edelman, G.3
  • 27
    • 0014589353 scopus 로고
    • Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties
    • Rosen, C. G. and Weber, G. (1969) Dimer formation from 1-amino-8-naphthalenesulfonate catalyzed by bovine serum albumin. A new fluorescent molecule with exceptional binding properties Biochemistry 8, 3915-3920
    • (1969) Biochemistry , vol.8 , pp. 3915-3920
    • Rosen, C.G.1    Weber, G.2
  • 29
    • 34250862659 scopus 로고    scopus 로고
    • An aggregation-prone intermediate species is present in the unfolding pathway of the monomeric portal protein of bacteriophage P22: Implications for portal assembly
    • DOI 10.1021/bi700006d
    • Braga, C. A., Carvalho, D., Lara, F. A., Cortines, J. R., Moore, S. D., Prevelige, P. E., Jr., and Foguel, D. (2007) An aggregation-prone intermediate species is present in the unfolding pathway of the monomeric portal protein of bacteriophage P22: implications for portal assembly Biochemistry 46, 7353-7364 (Pubitemid 46986362)
    • (2007) Biochemistry , vol.46 , Issue.25 , pp. 7353-7364
    • Braga, C.A.C.A.1    Carvalho, D.2    Lara, F.A.3    Cortines, J.R.4    Moore, S.D.5    Prevelige Jr., P.E.6    Foguel, D.7
  • 30
    • 59449086309 scopus 로고    scopus 로고
    • Trapping the monomer of a non-amyloidogenic variant of transthyretin. Exploring its possible use as a therapeutic strategy against transthyretin amyloidogenic diseases
    • Palhano, F. L., Leme, L. P., Busnardo, R. G., and Foguel, D. (2009) Trapping the monomer of a non-amyloidogenic variant of transthyretin. Exploring its possible use as a therapeutic strategy against transthyretin amyloidogenic diseases J. Biol. Chem. 284, 1443-1453
    • (2009) J. Biol. Chem. , vol.284 , pp. 1443-1453
    • Palhano, F.L.1    Leme, L.P.2    Busnardo, R.G.3    Foguel, D.4
  • 31
    • 0020479621 scopus 로고
    • Hydrophobic binding properties of the lectin from lima beans (Phaseolus lunatus)
    • Roberts, D. D. and Goldstein, I. J. (1982) Hydrophobic binding properties of the lectin from lima beans (Phaseolus lunatus) J. Biol. Chem. 257, 11274-11277
    • (1982) J. Biol. Chem. , vol.257 , pp. 11274-11277
    • Roberts, D.D.1    Goldstein, I.J.2
  • 32
    • 4444362186 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
    • DOI 10.1021/bi048864a
    • Foguel, D. and Silva, J. L. (2004) New Insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies Biochemistry 43, 11361-11370 (Pubitemid 39186958)
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11361-11370
    • Foguel, D.1    Silva, J.L.2
  • 33
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • DOI 10.1038/386463a0
    • Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., and Huber, R. (1997) Structure of 20S proteasome from yeast at 2.4 Å resolution Nature 386, 463-471 (Pubitemid 27164066)
    • (1997) Nature , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5    Bartunik, H.D.6    Huber, R.7
  • 35
    • 0035748547 scopus 로고    scopus 로고
    • The biochemical properties and phylogenies of phosphofructokinases from extremophiles
    • DOI 10.1007/s007920100215
    • Ronimus, R. S. and Morgan, H. W. (2001) The biochemical properties and phylogenies of phosphofructokinases from extremophiles Extremophiles 5, 357-373 (Pubitemid 33737386)
    • (2001) Extremophiles , vol.5 , Issue.6 , pp. 357-373
    • Ronimus, R.S.1    Morgan, H.W.2
  • 38
    • 0017225059 scopus 로고
    • Valency-dependent stimulating effects of lima bean lectins on lymphocytes of different species
    • Bessler, W., Resch, K., and Ferber, E. (1976) Valency-dependent stimulating effects of lima bean lectins on lymphocytes of different species Biochem. Biophys. Res. Commun. 69, 578-585
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 578-585
    • Bessler, W.1    Resch, K.2    Ferber, E.3
  • 39
    • 0032400466 scopus 로고    scopus 로고
    • The role of valence on the high-affinity binding of Griffonia simplicifolia isolectins to type A human erythrocytes
    • DOI 10.1021/bi981744g
    • Knibbs, R. N., Takagaki, M., Blake, D. A., and Goldstein, I. J. (1998) The role of valence on the high-affinity binding of Griffonia simplicifolia isolectins to type A human erythrocytes Biochemistry 37, 16952-16957 (Pubitemid 28566772)
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 16952-16957
    • Knibbs, R.N.1    Takagaki, M.2    Blake, D.A.3    Goldstein, I.J.4
  • 40
    • 0037162419 scopus 로고    scopus 로고
    • Conformational stability of legume lectins reflect their different modes of quaternary association: Solvent denaturation studies on concanavalin A and winged bean acidic agglutinin
    • DOI 10.1021/bi020240m
    • Mitra, N., Srinivas, V. R., Ramya, T. N., Ahmad, N., Reddy, G. B., and Surolia, A. (2002) Conformational stability of legume lectins reflect their different modes of quaternary association: solvent denaturation studies on concanavalin A and winged bean acidic agglutinin Biochemistry 41, 9256-9263 (Pubitemid 34787284)
    • (2002) Biochemistry , vol.41 , Issue.29 , pp. 9256-9263
    • Mitra, N.1    Srinivas, V.R.2    Ramya, T.N.C.3    Ahmad, N.4    Reddy, G.B.5    Surolia, A.6
  • 41
    • 0023494191 scopus 로고
    • Structure and thermal stability of phage T4 lysozyme
    • Alber, T. and Matthews, B. W. (1987) Structure and thermal stability of phage T4 lysozyme Methods Enzymol. 154, 511-533
    • (1987) Methods Enzymol. , vol.154 , pp. 511-533
    • Alber, T.1    Matthews, B.W.2
  • 42
    • 0028947236 scopus 로고
    • Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride
    • Agashe, V. R. and Udgaonkar, J. B. (1995) Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride Biochemistry 34, 3286-3299
    • (1995) Biochemistry , vol.34 , pp. 3286-3299
    • Agashe, V.R.1    Udgaonkar, J.B.2
  • 43
    • 0035882421 scopus 로고    scopus 로고
    • Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization
    • DOI 10.1016/S0304-4165(01)00153-2, PII S0304416501001532
    • Srinivas, V. R., Reddy, G. B., Ahmad, N., Swaminathan, C. P., Mitra, N., and Surolia, A. (2001) Legume lectin family, the 'natural mutants of the quaternary state', provide insights into the relationship between protein stability and oligomerization Biochim. Biophys. Acta 1527, 102-111 (Pubitemid 32710135)
    • (2001) Biochimica et Biophysica Acta - General Subjects , vol.1527 , Issue.3 , pp. 102-111
    • Srinivas, V.R.1    Reddy G.Bhanuprakash2    Ahmad, N.3    Swaminathan, C.P.4    Mitra, N.5    Surolia, A.6
  • 47
    • 33947321454 scopus 로고    scopus 로고
    • Crystal structures of Cratylia floribunda seed lectin at acidic and basic pHs. Insights into the structural basis of the pH-dependent dimer-tetramer transition
    • DOI 10.1016/j.jsb.2006.08.014, PII S1047847706002772
    • Del Sol, F. G., Cavada, B. S., and Calvete, J. J. (2007) Crystal structures of Cratylia floribunda seed lectin at acidic and basic pHs. Insights into the structural basis of the pH-dependent dimer-tetramer transition J. Struct. Biol. 158, 1-9 (Pubitemid 46441889)
    • (2007) Journal of Structural Biology , vol.158 , Issue.1 , pp. 1-9
    • Del Sol, F.G.1    Cavada, B.S.2    Calvete, J.J.3
  • 48
    • 33846005807 scopus 로고    scopus 로고
    • Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin
    • DOI 10.1529/biophysj.106.092668
    • Sinha, S. and Surolia, A. (2007) Attributes of glycosylation in the establishment of the unfolding pathway of soybean agglutinin Biophys. J. 92, 208-216 (Pubitemid 46048429)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 208-216
    • Sinha, S.1    Surolia, A.2
  • 49
    • 80051969419 scopus 로고    scopus 로고
    • Products of nitrate assimilation are deposited in plants as storage proteins
    • in (Heldt, H.-W. Ed.) 3 rd ed. pp, Elsevier Academic Press, San Diego.
    • Heldt, H.-W. (2005) Products of nitrate assimilation are deposited in plants as storage proteins, in Plant Biochemistry (Heldt, H.-W., Ed.) 3 rd ed., pp 353-361, Elsevier Academic Press, San Diego.
    • (2005) Plant Biochemistry , pp. 353-361
    • Heldt, H.-W.1
  • 50
    • 0016662479 scopus 로고
    • The covalent and three-dimensional structure of concanavalin A. IV, atomic coordinates, hydrogen bonding, and quaternary structure
    • Reeke, G. N., Jr., Becker, J. W., and Edelman, G. M. (1975) The covalent and three-dimensional structure of concanavalin A. IV, atomic coordinates, hydrogen bonding, and quaternary structure J. Biol. Chem. 250, 1525-1547
    • (1975) J. Biol. Chem. , vol.250 , pp. 1525-1547
    • Reeke Jr., G.N.1    Becker, J.W.2    Edelman, G.M.3
  • 51
    • 80052015326 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 0.99rc6, DeLano Scientific LLC, San Carlos, CA.
    • DeLano, W. (2006) The PyMOL Molecular Graphics System, Version 0.99rc6, DeLano Scientific LLC, San Carlos, CA.
    • (2006)
    • Delano, W.1


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