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Volumn 27, Issue 2, 2004, Pages 89-100

Effect of specific mutations in helix α7 of domain I on the stability and crystallization of Cry3A in Bacillus thuringiensis

Author keywords

Bacillus thuringiensis; Cry1C; Cry3A; Crystallization; Domain substitution; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; CRYSTALLIZATION; INCLUSIONS; INSECT CONTROL; MUTAGENESIS; SYNTHESIS (CHEMICAL);

EID: 16544374775     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (35)
  • 1
    • 0031720057 scopus 로고    scopus 로고
    • Bacillus thuringiensis and its pesticidal crystal proteins
    • Schnepf, E., Crickmore, N., Van Rie, J., et al. (1998) Bacillus thuringiensis and its pesticidal crystal proteins. Microbiol. Mol. Biol. Rev. 62, 775-806.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 775-806
    • Schnepf, E.1    Crickmore, N.2    Van Rie, J.3
  • 2
    • 0012664487 scopus 로고    scopus 로고
    • A perspective on pathogens as biological control agents for insect pests
    • (Bellows, T. S. ed.), Academic Press, San Diego
    • Federici, B. A. (1999) A perspective on pathogens as biological control agents for insect pests. In Handbook of Biological Control (Bellows, T. S. ed.), Academic Press, San Diego, pp. 517-548.
    • (1999) Handbook of Biological Control , pp. 517-548
    • Federici, B.A.1
  • 3
    • 4244144005 scopus 로고
    • The crystal δ-endotoxins of Bacillus thuringiensis: Models for their mechanism of action on the insect gut
    • Knowles, B. H. and Dow, J. A. T. (1993) The crystal δ-endotoxins of Bacillus thuringiensis: models for their mechanism of action on the insect gut. BioEssays 15, 469-476.
    • (1993) BioEssays , vol.15 , pp. 469-476
    • Knowles, B.H.1    Dow, J.A.T.2
  • 4
    • 0021568799 scopus 로고
    • Fate of the insecticidal, proteinaceous parasporal crystal of Bacillus thuringiensis in soil
    • West, A. W. (1984) Fate of the insecticidal, proteinaceous parasporal crystal of Bacillus thuringiensis in soil. Soil Biol. Biochem. 16, 357-360.
    • (1984) Soil Biol. Biochem. , vol.16 , pp. 357-360
    • West, A.W.1
  • 5
    • 0025238783 scopus 로고
    • Characterization of the cysteine residues and disulfide linkages in the protein crystal of Bacillus thuringiensis
    • Bietlot, H. P., Vishnubhatla, I., Carey, P. R., Pozsgay, M., and Kaplan, H. (1990) Characterization of the cysteine residues and disulfide linkages in the protein crystal of Bacillus thuringiensis. Biochem. J. 267, 309-316.
    • (1990) Biochem. J. , vol.267 , pp. 309-316
    • Bietlot, H.P.1    Vishnubhatla, I.2    Carey, P.R.3    Pozsgay, M.4    Kaplan, H.5
  • 6
    • 0022217541 scopus 로고
    • Characterized full-length and truncated plasmid clones of the crystal protein of Bacillus thuringiensis subsp. kurstaki HD-73 and their toxicity to Manduca sexta
    • Adang, M. J., Staver, M. J., Rocheleau, T. A., Leighton, J., Barker, R. F., and Thompson, D. V. (1985) Characterized full-length and truncated plasmid clones of the crystal protein of Bacillus thuringiensis subsp. kurstaki HD-73 and their toxicity to Manduca sexta. Gene 36, 289-300.
    • (1985) Gene , vol.36 , pp. 289-300
    • Adang, M.J.1    Staver, M.J.2    Rocheleau, T.A.3    Leighton, J.4    Barker, R.F.5    Thompson, D.V.6
  • 7
    • 0033771034 scopus 로고    scopus 로고
    • Molecular genetic manipulation of truncated Cry1C protein synthesis in Bacillus thuringiensis to improve stability and yield
    • Park, H. W., Bideshi, D. K., and Federici, B. A. (2000) Molecular genetic manipulation of truncated Cry1C protein synthesis in Bacillus thuringiensis to improve stability and yield. Appl. Environ. Microbiol. 66, 4449-4455.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4449-4455
    • Park, H.W.1    Bideshi, D.K.2    Federici, B.A.3
  • 8
    • 0030222056 scopus 로고    scopus 로고
    • Influence of the 20-kDa protein from Bacillus thuringiensis ssp. israelensis on the rate of production of truncated Cry1C proteins
    • Rang, C., Bes, M., Lullien-Pellerin, V., Wu, D., Federici, B. A., and Frutos, R. (1996) Influence of the 20-kDa protein from Bacillus thuringiensis ssp. israelensis on the rate of production of truncated Cry1C proteins. FEMS Microbiol. Lett. 141, 261-264.
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 261-264
    • Rang, C.1    Bes, M.2    Lullien-Pellerin, V.3    Wu, D.4    Federici, B.A.5    Frutos, R.6
  • 9
    • 0021939882 scopus 로고
    • Only part of the protoxin gene of Bacillus thuringiensis subsp. berliner 1715 is necessary for insecticidal activity
    • Wabiko, H., Held, G. A., and Bulla, Jr., L. A. (1985) Only part of the protoxin gene of Bacillus thuringiensis subsp. berliner 1715 is necessary for insecticidal activity. Appl. Environ. Microbiol. 49, 706-708.
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 706-708
    • Wabiko, H.1    Held, G.A.2    Bulla Jr., L.A.3
  • 10
    • 0031717489 scopus 로고    scopus 로고
    • Revision of the nomenclature for the Bacillus thuringiensis pesticidal crystal proteins
    • Crickmore, N., Zeigler, D. R., Feitelson, J., et al. (1998) Revision of the nomenclature for the Bacillus thuringiensis pesticidal crystal proteins. Microbiol. Mol. Biol. Rev. 62, 807-813.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 807-813
    • Crickmore, N.1    Zeigler, D.R.2    Feitelson, J.3
  • 11
    • 0028820391 scopus 로고
    • How does Bacillus thuringiensis produce so much insecticidal crystal protein?
    • Agaisse, H. and Lereclus, D. (1995) How does Bacillus thuringiensis produce so much insecticidal crystal protein? J. Bacteriol. 177, 6027-6032.
    • (1995) J. Bacteriol. , vol.177 , pp. 6027-6032
    • Agaisse, H.1    Lereclus, D.2
  • 12
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • Li, J., Carroll, J., and Ellar, D. J. (1991) Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353, 815-821.
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 13
    • 0029619216 scopus 로고
    • Bacillus thuringiensis CryIA(a) insecticidal toxin: Crystal structure and channel formation
    • Grochulski, P., Masson, L., Borisova, S., et al. (1995) Bacillus thuringiensis CryIA(a) insecticidal toxin: crystal structure and channel formation. J. Mol. Biol. 254, 447-464.
    • (1995) J. Mol. Biol. , vol.254 , pp. 447-464
    • Grochulski, P.1    Masson, L.2    Borisova, S.3
  • 14
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • Morse, R. J., Yamamoto, T., and Stroud, R. M. (2001) Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure 9, 409-417.
    • (2001) Structure , vol.9 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 15
    • 0032937987 scopus 로고    scopus 로고
    • Domain III of the Bacillus thuringiensis delta-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N
    • de Maagd, R. A., Bakker, P. L., Masson, L., et al. (1999) Domain III of the Bacillus thuringiensis delta-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N. Mol. Microbiol. 31, 463-471.
    • (1999) Mol. Microbiol. , vol.31 , pp. 463-471
    • De Maagd, R.A.1    Bakker, P.L.2    Masson, L.3
  • 16
    • 0032884932 scopus 로고    scopus 로고
    • Identification of Bacillus thuringiensis delta-endotoxin Cry1C domain III amino acid residues involved in insect specificity
    • de Maagd, R. A., Bakker, P., Staykov, N., Dukiandjiev, S., Stiekema, W., and Bosch, D. (1999) Identification of Bacillus thuringiensis delta-endotoxin Cry1C domain III amino acid residues involved in insect specificity. Appl. Environ. Microbiol. 65, 4369-4374.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4369-4374
    • De Maagd, R.A.1    Bakker, P.2    Staykov, N.3    Dukiandjiev, S.4    Stiekema, W.5    Bosch, D.6
  • 17
    • 0029930607 scopus 로고    scopus 로고
    • Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition
    • de Maagd, R. A., Kwa, M. S., van der Klei, H., et al. (1996) Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition. Appl. Environ. Microbiol. 62, 1537-1543.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1537-1543
    • De Maagd, R.A.1    Kwa, M.S.2    Van Der Klei, H.3
  • 18
    • 0004098818 scopus 로고    scopus 로고
    • Identification of residues in Domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity
    • Lee, M. K., You, T. K., Gould, F., and Dean, D. H. (1999) Identification of residues in Domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity. Appl Environ. Microbiol. 65, 4513-4520.
    • (1999) Appl Environ. Microbiol. , vol.65 , pp. 4513-4520
    • Lee, M.K.1    You, T.K.2    Gould, F.3    Dean, D.H.4
  • 19
    • 0033653270 scopus 로고    scopus 로고
    • Domain I plays an important role in the crystallization of Cry3A in Bacillus thuringiensis
    • Park, H. W. and Federici, B. A. (2000) Domain I plays an important role in the crystallization of Cry3A in Bacillus thuringiensis. Mol. Biotechnol. 16, 97-108.
    • (2000) Mol. Biotechnol. , vol.16 , pp. 97-108
    • Park, H.W.1    Federici, B.A.2
  • 20
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Höfte, H. and Whiteley, H. R. (1989) Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53, 242-255.
    • (1989) Microbiol. Rev. , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 21
    • 0024970876 scopus 로고
    • Transformation and expression of a cloned δ-endotoxin gene in Bacillus thuringiensis
    • Lereclus, D., Arantès, O., Chaufaux, J., and Lecadet, M.-M. (1989) Transformation and expression of a cloned δ-endotoxin gene in Bacillus thuringiensis. FEMS Microbiol. Lett. 60, 211-218.
    • (1989) FEMS Microbiol. Lett. , vol.60 , pp. 211-218
    • Lereclus, D.1    Arantès, O.2    Chaufaux, J.3    Lecadet, M.-M.4
  • 22
    • 0031692397 scopus 로고    scopus 로고
    • Optimization of Cry3A yields in Bacillus thuringiensis by use of sporulation-dependent promoters in combination with the STAB-SD mRNA sequence
    • Park, H. W., Ge, B., Bauer, L. S., and Federici, B. A. (1998) Optimization of Cry3A yields in Bacillus thuringiensis by use of sporulation-dependent promoters in combination with the STAB-SD mRNA sequence. Appl. Environ. Microbiol. 64, 3932-3938.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3932-3938
    • Park, H.W.1    Ge, B.2    Bauer, L.S.3    Federici, B.A.4
  • 23
    • 0032728902 scopus 로고    scopus 로고
    • Differential enhancement of Cry2A versus Cry11A yields in Bacillus thuringiensis by use of the cry3A STAB mRNA sequence
    • Park, H. W., Bideshi, D. K., Johnson, J. J., and Federici, B. A. (1999) Differential enhancement of Cry2A versus Cry11A yields in Bacillus thuringiensis by use of the cry3A STAB mRNA sequence. FEMS Microbiol. Lett. 181, 319-327.
    • (1999) FEMS Microbiol. Lett. , vol.181 , pp. 319-327
    • Park, H.W.1    Bideshi, D.K.2    Johnson, J.J.3    Federici, B.A.4
  • 24
    • 0026684615 scopus 로고
    • Characterization of the pH-mediated solubility of Bacillus thuringiensis var. san diego native δ-endotoxin crystals
    • Koller, C. N., Bauer, L. S., and Hollingworth, R. M. (1992) Characterization of the pH-mediated solubility of Bacillus thuringiensis var. san diego native δ-endotoxin crystals. Biochem. Biophys. Res. Commun. 184, 692-699.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 692-699
    • Koller, C.N.1    Bauer, L.S.2    Hollingworth, R.M.3
  • 25
    • 0031182629 scopus 로고    scopus 로고
    • Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A delta-endotoxin may facilitate its coleopteran toxicity
    • Carroll, J., Convents, D., Van Damme, J., Boets, A., Van Rie, J., and Ellar, D. J. (1997) Intramolecular proteolytic cleavage of Bacillus thuringiensis Cry3A delta-endotoxin may facilitate its coleopteran toxicity. J. Invertebr. Pathol. 70, 41-49.
    • (1997) J. Invertebr. Pathol. , vol.70 , pp. 41-49
    • Carroll, J.1    Convents, D.2    Van Damme, J.3    Boets, A.4    Van Rie, J.5    Ellar, D.J.6
  • 26
    • 0024320570 scopus 로고
    • Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis
    • Carroll, J., Li, J., and Ellar, D. J. (1989) Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis. Biochem. J. 261, 99-105.
    • (1989) Biochem. J. , vol.261 , pp. 99-105
    • Carroll, J.1    Li, J.2    Ellar, D.J.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 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
  • 29
    • 0028984252 scopus 로고
    • The assembly and organization of the α5 and α7 helices from the pore-forming domain of Bacillus thuringiensis δ-endotoxin: Relevance to a functional model
    • Gazit, E. and Shai, Y. (1995) The assembly and organization of the α5 and α7 helices from the pore-forming domain of Bacillus thuringiensis δ-endotoxin: relevance to a functional model. J. Biol. Chem. 270, 2571-2578.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2571-2578
    • Gazit, E.1    Shai, Y.2
  • 30
    • 0032514753 scopus 로고    scopus 로고
    • The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an "umbrella-like" structure of the pore
    • Gazit, E., Rocca, P. L., Sansom, M. S. P., and Shai, Y. (1998) The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an "umbrella-like" structure of the pore. Proc. Natl. Acad. Sci. USA 95, 12,289-12,294.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95
    • Gazit, E.1    Rocca, P.L.2    Sansom, M.S.P.3    Shai, Y.4
  • 31
    • 0035957098 scopus 로고    scopus 로고
    • Role of δ-helix seven of Bacillus thuringiensis Cry1Ab δ-endotoxin in membrane insertion, structural stability, and ion channel activity
    • Alcantara, E. P., Alzate, O., Lee, M. K., Curtiss, A., and Dean, D. H. (2001) Role of δ-helix seven of Bacillus thuringiensis Cry1Ab δ-endotoxin in membrane insertion, structural stability, and ion channel activity. Biochemistry 40, 2540-2547.
    • (2001) Biochemistry , vol.40 , pp. 2540-2547
    • Alcantara, E.P.1    Alzate, O.2    Lee, M.K.3    Curtiss, A.4    Dean, D.H.5
  • 32
    • 0032861219 scopus 로고    scopus 로고
    • Amino acid substitution in α-helix 7 of Cry1Ac delta-endotoxin of Bacillus thuringiensis leads to enhanced toxicity to Helicoverpa armigera Hubner
    • Chandra, A., Ghosh, P., Mandaokar, A. D., et al. (1999) Amino acid substitution in α-helix 7 of Cry1Ac delta-endotoxin of Bacillus thuringiensis leads to enhanced toxicity to Helicoverpa armigera Hubner. FEBS Lett. 458, 175-179.
    • (1999) FEBS Lett. , vol.458 , pp. 175-179
    • Chandra, A.1    Ghosh, P.2    Mandaokar, A.D.3
  • 33
    • 0027328978 scopus 로고
    • Structural stability of Bacillus thuringiensis δ-endotoxin homolog-scanning mutants determined by susceptibility to protease
    • Almond, B. D. and Dean, D. H. (1993) Structural stability of Bacillus thuringiensis δ-endotoxin homolog-scanning mutants determined by susceptibility to protease. Appl. Environ. Microbiol. 59, 2442-2448.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2442-2448
    • Almond, B.D.1    Dean, D.H.2
  • 34
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • Parsell, D. A. and Sauer, R. T. (1989) The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. J. Biol. Chem. 264, 7590-7595.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 35
    • 0005876924 scopus 로고
    • Bacteriophage lambda cro mutations: Effects on activity and intracellular degradation
    • Pakula, A. A., Young, V. B., and Sauer, R. T. (1986) Bacteriophage lambda cro mutations: effects on activity and intracellular degradation. Proc. Natl. Acad. Sci. USA 83, 8829-8833.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8829-8833
    • Pakula, A.A.1    Young, V.B.2    Sauer, R.T.3


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