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Volumn 383, Issue 1, 2004, Pages 53-61

Amino acid residues conferring herbicide in tobacco acetohydroxy acid synthase

Author keywords

Acetohydroxy acid synthase; Conserved amino acids; Herbicide; Homology modelling; Site directed mutagenesis; Tobacco

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CATALYSIS; ENZYMES; MUTAGENESIS; TOBACCO; YEAST;

EID: 6344260343     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040720     Document Type: Article
Times cited : (12)

References (41)
  • 2
    • 0021106947 scopus 로고
    • Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli
    • Gollop, N., Chipman, D. M. and Barak, Z. (1983) Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli. Biochim. Biophys. Acta 748, 34-39
    • (1983) Biochim. Biophys. Acta , vol.748 , pp. 34-39
    • Gollop, N.1    Chipman, D.M.2    Barak, Z.3
  • 3
    • 0022356249 scopus 로고
    • Purification and, properties of Salmonella typhimurium acetolactate synthase isozyme II from Escherichia coli HB101/pDU
    • Schloss, J. V., Dyk, K. E. V., Vasta, J. F. and Kutny, B. M. (1985) Purification and, properties of Salmonella typhimurium acetolactate synthase isozyme II from Escherichia coli HB101/pDU. Biochemistry 24, 4952-4959
    • (1985) Biochemistry , vol.24 , pp. 4952-4959
    • Schloss, J.V.1    Dyk, K.E.V.2    Vasta, J.F.3    Kutny, B.M.4
  • 4
    • 0018409914 scopus 로고
    • Acetohydroxyacid synthase I of Escherichia coli: Purification and properties
    • Grimminger, H. and Umbarger, H. E. (1979) Acetohydroxyacid synthase I of Escherichia coli: purification and properties. J. Bacteriol. 137, 846-853
    • (1979) J. Bacteriol. , vol.137 , pp. 846-853
    • Grimminger, H.1    Umbarger, H.E.2
  • 5
    • 0016124816 scopus 로고
    • Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast
    • Ryan, E. D. and Kohlhow, G. B. (1974) Subcellular localization of isoleucine-valine biosynthetic enzymes in yeast. J. Bacteriol. 120, 631-637
    • (1974) J. Bacteriol. , vol.120 , pp. 631-637
    • Ryan, E.D.1    Kohlhow, G.B.2
  • 6
    • 0023626886 scopus 로고
    • Physiological implications of the specficity of acetohydroxyacid synthase isozymes of enteric bacteria
    • Barak, Z., Chipman, D. M. and Gollop, N. (1987) Physiological implications of the specficity of acetohydroxyacid synthase isozymes of enteric bacteria. J. Bacteriol. 169, 3750-3756
    • (1987) J. Bacteriol. , vol.169 , pp. 3750-3756
    • Barak, Z.1    Chipman, D.M.2    Gollop, N.3
  • 7
  • 8
    • 0032212916 scopus 로고    scopus 로고
    • Mutagenesis of Escherichia coli acetohydroxyacid synthase isoenzyme II and characterization of three herbicide-insensitive forms
    • Hill, C. M. and Duggleby, R. G. (1998) Mutagenesis of Escherichia coli acetohydroxyacid synthase isoenzyme II and characterization of three herbicide-insensitive forms. Biochem. J. 335, 653-661
    • (1998) Biochem. J. , vol.335 , pp. 653-661
    • Hill, C.M.1    Duggleby, R.G.2
  • 9
    • 0000639366 scopus 로고
    • Isolation and characterization of plant genes coding for acetolacetate synthase, the target enzyme for two classes of herbicides
    • Mazur, B. J., Chui, C.-F. and Smith, J. K. (1987) Isolation and characterization of plant genes coding for acetolacetate synthase, the target enzyme for two classes of herbicides. Plant Physiol. 75, 1110-1117
    • (1987) Plant Physiol. , vol.75 , pp. 1110-1117
    • Mazur, B.J.1    Chui, C.-F.2    Smith, J.K.3
  • 10
    • 0026519162 scopus 로고
    • Multiple resistance to sulfonylureas and imidazolinones conferred by an acetohydroxyacid synthase gene with separate mutations for selective resistance
    • Hattori, J., Rutledge, R. G., Miki, B. L. and Baum, B. R. (1992) Multiple resistance to sulfonylureas and imidazolinones conferred by an acetohydroxyacid synthase gene with separate mutations for selective resistance. Mol. Gen. Genet. 232, 167-173
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 167-173
    • Hattori, J.1    Rutledge, R.G.2    Miki, B.L.3    Baum, B.R.4
  • 11
    • 0029347054 scopus 로고
    • Organization, inheritance and expression of acetohydroxyacid synthase genes in the cotton allotetraploid Gossypium hirsutum
    • Grula, J. W., Hudspeth, R. L., Hobbs, S. L. and Anderson, D. M. (1995) Organization, inheritance and expression of acetohydroxyacid synthase genes in the cotton allotetraploid Gossypium hirsutum. Plant Mol. Biol. 28, 837-846
    • (1995) Plant Mol. Biol. , vol.28 , pp. 837-846
    • Grula, J.W.1    Hudspeth, R.L.2    Hobbs, S.L.3    Anderson, D.M.4
  • 12
    • 0026845083 scopus 로고
    • Sequence of two acetohydroxyacid synthase genes from Zea mays
    • Fang, G. Y., Gross, P. R., Chen, C. H. and Lillis, M. (1992) Sequence of two acetohydroxyacid synthase genes from Zea mays. Plant Mol. Biol. 12, 1185-1187
    • (1992) Plant Mol. Biol. , vol.12 , pp. 1185-1187
    • Fang, G.Y.1    Gross, P.R.2    Chen, C.H.3    Lillis, M.4
  • 13
    • 0029154215 scopus 로고
    • A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase
    • Bernasconi, P., Woodworth, A. R., Rosen, B. A., Subramanian, M. V. and Siehl, D. L. (1995) A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase. J. Biol. Chem. 270, 17381-17385
    • (1995) J. Biol. Chem. , vol.270 , pp. 17381-17385
    • Bernasconi, P.1    Woodworth, A.R.2    Rosen, B.A.3    Subramanian, M.V.4    Siehl, D.L.5
  • 14
    • 0030601845 scopus 로고    scopus 로고
    • Rational molecular design and genetic engineering of herbicide resistance crops by structure modeling and site-directed mutagenesis of acetohydroxyacid synthase
    • Ott, K.-H., Kwagh, J.-G., Stockton, G. W., Sidrov, V. and Kekefuva, G. (1996) Rational molecular design and genetic engineering of herbicide resistance crops by structure modeling and site-directed mutagenesis of acetohydroxyacid synthase. J. Mol. Biol. 263, 359-367
    • (1996) J. Mol. Biol. , vol.263 , pp. 359-367
    • Ott, K.-H.1    Kwagh, J.-G.2    Stockton, G.W.3    Sidrov, V.4    Kekefuva, G.5
  • 15
    • 0031589993 scopus 로고    scopus 로고
    • Soluble expression in Escherichia coli and purification and characterization of wild-type recombinant tobacco acetolactate synthase
    • Chang, S.-I., Kang, M.-K., Choi, J.-D. and Namgoong, S. K. (1997) Soluble expression in Escherichia coli and purification and characterization of wild-type recombinant tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 234, 549-553
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 549-553
    • Chang, S.-I.1    Kang, M.-K.2    Choi, J.-D.3    Namgoong, S.K.4
  • 16
    • 0021195869 scopus 로고
    • The sulfonylurea herbicide sulfoneturon methyl is an extremely potent and selective inhibitor of acetolactate synthase in Salmonella typhimurium
    • LaRossa, R. A. and Schloss, J. V. (1984) The sulfonylurea herbicide sulfoneturon methyl is an extremely potent and selective inhibitor of acetolactate synthase in Salmonella typhimurium. J. Biol. Chem. 259, 8753-8757
    • (1984) J. Biol. Chem. , vol.259 , pp. 8753-8757
    • LaRossa, R.A.1    Schloss, J.V.2
  • 17
    • 0001476338 scopus 로고
    • Site of action of chlorsulfuron: Inhibition of valine and isoleucine biosynthesis of plants
    • Ray, T. B. (1984) Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis of plants. Plant Physiol. 75, 827-831
    • (1984) Plant Physiol. , vol.75 , pp. 827-831
    • Ray, T.B.1
  • 18
    • 84957869700 scopus 로고
    • Imidazolinones: Potent inhibitors of acetohydroxyacid synthase
    • Shaner, D. L., Anderson, P. C. and Stidham, M. A. (1984) Imidazolinones: potent inhibitors of acetohydroxyacid synthase. Plant Physiol. 76, 545-546
    • (1984) Plant Physiol. , vol.76 , pp. 545-546
    • Shaner, D.L.1    Anderson, P.C.2    Stidham, M.A.3
  • 22
    • 0034694823 scopus 로고    scopus 로고
    • Amino acid residues conferring herbicide tolerance in tobacco acetolactate synthase
    • Chong, C.-K. and Choi, J.-D. (2000) Amino acid residues conferring herbicide tolerance in tobacco acetolactate synthase. Biochem. Biophys. Res. Commun. 279, 462-467
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 462-467
    • Chong, C.-K.1    Choi, J.-D.2
  • 25
    • 0038434135 scopus 로고    scopus 로고
    • Roles of conserved methionine residues in tobacco acetolactate synthse
    • Le, D. T., Yoon, M.-Y., Kim, Y.-T. and Choi, J.-D. (2003) Roles of conserved methionine residues in tobacco acetolactate synthse. Biochem. Biophys. Res. Commun. 306, 1075-1082
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 1075-1082
    • Le, D.T.1    Yoon, M.-Y.2    Kim, Y.-T.3    Choi, J.-D.4
  • 26
    • 0034827885 scopus 로고    scopus 로고
    • Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydoroxyacid synthase
    • Pang, S.-S., Guddat, L.-W. and Duggleby, R.-G. (2001) Crystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydoroxyacid synthase. Acta Crystallogr. D57, 1321-1323
    • (2001) Acta Crystallogr. , vol.D57 , pp. 1321-1323
    • Pang, S.-S.1    Guddat, L.-W.2    Duggleby, R.-G.3
  • 27
    • 0036295208 scopus 로고    scopus 로고
    • Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors
    • Pang, S.-S., Duggleby, R.-G. and Guddat, L.-W. (2002) Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors. J. Mol. Biol. 317, 249-262
    • (2002) J. Mol. Biol. , vol.317 , pp. 249-262
    • Pang, S.-S.1    Duggleby, R.-G.2    Guddat, L.-W.3
  • 28
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N. and Peitsch, M.-C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.-C.4
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 30
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/N
    • Hall, T. A. (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/N. Nucleic Acids Symp. Ser. 41, 95-99
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-99
    • Hall, T.A.1
  • 31
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0025325983 scopus 로고
    • 'Megaprimer' method of site-directed mutagenes
    • Sarkar, G. and Sommer, S. S. (1990) 'Megaprimer' method of site-directed mutagenes. Biotechniques 2, 404-407
    • (1990) Biotechniques , vol.2 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 35
    • 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 (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 84864301531 scopus 로고
    • A colorimetric determination of blood acetoin
    • Westerfeld, W. W. (1945) A colorimetric determination of blood acetoin. J. Biol. Chem. 161, 495-502
    • (1945) J. Biol. Chem. , vol.161 , pp. 495-502
    • Westerfeld, W.W.1
  • 38
    • 0024333237 scopus 로고
    • Functional expression of plant acetolactate synthase genes in Escherichia coli Proc
    • Smith, J. K., Schloss, J. V. and Mazur, B. J. (1989) Functional expression of plant acetolactate synthase genes in Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 86, 4179-4183
    • (1989) Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4179-4183
    • Smith, J.K.1    Schloss, J.V.2    Mazur, B.J.3
  • 39
    • 0000238336 scopus 로고
    • A simple method for fuction minimization
    • Neider, J. A. and Mead, R. (1965) A simple method for fuction minimization, Comput. J. 7, 308-313
    • (1965) Comput. J. , vol.7 , pp. 308-313
    • Neider, J.A.1    Mead, R.2
  • 40
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • Kelly, S.-M. and Price, N.-C. (1997) The application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta 1338, 161-185
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 161-185
    • Kelly, S.-M.1    Price, N.-C.2
  • 41
    • 0037470165 scopus 로고    scopus 로고
    • Molecular basis of sulfonylurea herbicide inhibition of acetohydroxy acid synthase
    • Pang, S. S., Guddat, L. W. and Duggleby, R. G. (2003) Molecular basis of sulfonylurea herbicide inhibition of acetohydroxy acid synthase. J. Biol. Chem. 278, 7639-7644
    • (2003) J. Biol. Chem. , vol.278 , pp. 7639-7644
    • Pang, S.S.1    Guddat, L.W.2    Duggleby, R.G.3


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