Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase

Biochemistry

Volumn 38, Issue 16, 1999, Pages 5222-5231

  Pang, Siew Siew ^a   Duggleby, Ronald G ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

ACETOLACTATE SYNTHASE; POTASSIUM DIHYDROGEN PHOSPHATE; PROTEIN SUBUNIT; VALINE;

ARTICLE; DISSOCIATION CONSTANT; DNA SEQUENCE; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME PURIFICATION; ENZYME RECONSTITUTION; ENZYME STRUCTURE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; SACCHAROMYCES CEREVISIAE; STRUCTURE ANALYSIS;

ACETOLACTATE SYNTHASE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINO ACIDS, BRANCHED-CHAIN; BASE SEQUENCE; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PHOSPHATES; POTASSIUM COMPOUNDS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; VALINE;

EID: 0000660166     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi983013m     Document Type: Article

References (87)

1. Gollop, N., Damn, B., Barak, Z., and Chipman, D. M. (1989) Biochemistry 28, 6310-6317.
2. Gjermansen, C., Nilsson-Tillgren, T., Petersen, J. G. L., Kielland-Brandt, M. C., Sigsgaard, P., and Holmberg, S. (1988) J. Basic Microbiol. 28, 175-183.
3. Chang, Y.-Y., Wang, A.-Y., and Cronan, J. E., Jr. (1993) J. Biol. Chem. 268, 3911-3919.
4. Macheroux, P., Schonbrunn, E., Svergun, D. I., Volkov, V. V., Koch, M. H. J., Bornemann, S., and Thorneley, R. N. F. (1998) Biochem. J. 335, 319-27.
5. Cobb, A. (1992) Herbicides and Plant Physiology, pp 131-140, Chapman and Hall, London.
6. Ray, T. B. (1989) in Target Sites of Herbicide Action (Böger, P., and Sandmann, G., Eds.), pp 114-122, CRC Press, Boca Raton, FL.
7. Stidham, M. A. (1991) in Herbicides (Baker, N. R., and Percivial, M. P., Eds.), pp 247-266, Elsevier Science Publishers, Amsterdam.
8. Stidham, M. A., and Singh, B. K. (1991) in The Imidazolinone Herbicides (Shaner, D. L., and O'Connor, S. L., Eds.), pp 71-90, CRC Press, Boca Raton, FL.
9. Umbarger, H. E. (1987) in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F. C., Ingraham, J. L., Low, K. B., Magasanik, B., Schaechter, M., and Umbarger H. E., Eds.), pp 352-367, American Society for Microbiology, Washington, DC.
10. Barak, Z., Chipman, D. M., and Gollop, N. (1987) J. Bacteriol. 169, 3750-3756.
11. Barak, Z., Calvo, J. M., and Schloss, J. V. (1988) Methods Enzymol. 166, 455-458.
12. Eoyang, L., and Silverman, P. M. (1984) J. Bacteriol. 157, 184-189.
13. Eoyang, L., and Silverman, P. M. (1988) Methods Enzymol. 166, 435-445.
14. Grimminger, H., and Umbarger, H. E. (1979) J. Bacteriol. 137, 846-853.
15. Schloss, J. V., Van Dyk, D. E., Vasta, J. F., and Kutny, R. M. (1985) Biochemistry 24, 4952-4959.
16. Hill, C. M., and Duggleby, R. G. (1998) Biochem. J. 335, 653-661.
17. Lawther, R. P., Wek, R. C., Lopes, J. M., Pereira, R., Taillon, B. E., and Hatfield, G. W. (1987) Nucl. Acids Res. 15, 2137-2155.
18. Squires, C. H., DeFelice, M., Devereux, J., and Calvo, J. M. (1983) Nucl. Acids Res. 11, 5299-5313.
19. Wek, R. C., Hauser, C. A., and Hatfield, G. W. (1985) Nucl. Acids Res. 13, 3995-4010.
20. Alexander-Caudle, C., Latinwo, L. M., and Jackson, J. H. (1990) J. Bacteriol. 172, 3060-3065.
21. Jackson, J. H., Davis, E. J., Madu, A. C., and Braxter, S. E. (1981) Mol. Gen. Genet. 181, 417-419.
22. Jackson, J. H., Herring, P. A., Patterson, E. B., and Blatt, J. M. (1993) Biochimie 75, 759-765.
23. Robinson, C. L., and Jackson, J. H. (1982) Mol. Gen. Genet. 186, 240-246.
24. Hill, C. M., Pang, S. S., and Duggleby, R. G. (1997) Biochem. J. 327, 891-898.
25. DeFelice, M., Guardiola, J., Esposito, B., and Iaccarino, M. (1974) J. Bacteriol. 120, 1068-1077.
26. Sella, C., Weinstock, O., Barak, Z., and Chipman, D. M. (1993) J. Bacteriol. 175, 5339-5343.
27. Vyazmensky, M., Sella, C., Barak, Z., and Chipman, D. M. (1996) Biochemistry 35, 10339-10346.
28. Eoyang, L., and Silverman, P. M. (1986) J. Bacteriol. 166, 901-904.
29. Ricca, E., Limauro, D., Lago, C. T., and DeFelice, M. (1988) J. Bacteriol. 170, 5197-5199.
30. Weinstock, O., Sella, C., Chipman, D. M., and Barak, Z. (1992) J. Bacteriol. 174, 5560-5566.
31. Cassady, W. E., Leiter, E. H., Bergquist, A., and Wagner, R. P. (1972) J. Cell Biol. 53, 66-72.
32. Ryan, E. D., and Kohlhaw, G. B. (1974) J. Bacteriol. 120, 631-637.
33. Jones, A. V., Young, R. M., and Leto, K. (1985) Plant Physiol. 77, S-293.
34. Reith, M., and Munholland, J. (1993) Curr. Genet. 23, 59-65.
35. Ohta N., Sato, N., Ueda, K., and Kuroiwa, T. (1997) J. Plant Res. 110, 235-245.
36. Douglas, S. E., and Penny, S. L. (1998) J. Mol. Evol. In press.
37. Mazur, B. J., Chui, C.-F., and Smith, J. K. (1987) Plant Physiol. 85, 1110-1117.
38. Hattori, J., Rutledge, R. G., Miki, B. L., and Baum, B. R. (1992) Can. J. Bot. 70, 1957-1963.
39. Grula, J. W., Hudspeth, R. L., Hobbs, S. L., and Anderson, D. M. (1995) Plant Mol. Biol. 28, 837-846.
40. Fang, L. Y., Gross, P. R., Chen, C. H., and Lillis, M. (1992) Mol. Biol. 18, 1185-1187.
41. Falco, S. C., Dumas, K. S., and Livak, K. J. (1985) Nucl. Acids Res. 13, 4011-4027.
42. Bekkaoui, F., Nadin-Davis, S. A., and Crosby, W. L. (1993) Curr. Genet. 24, 544-547.
43. Durner, J., and Böger, P. (1990) Plant Physiol. 93, 1027-1031.
44. Muhitch, M. J., Shaner, D. L., and Stidham, M. A. (1987) Plant Physiol. 83, 451-456.
45. Southan, M. D., and Copeland, L. (1996) Physiol. Plant. 98, 824-832.
46. Chang, A. K., and Duggleby R. G. (1997) Biochem. J. 327, 161-169.
47. Chang, S.-I., Kang, M.-K., Choi, J.-D., and Namgoong, S. K. (1997) Biochem. Biophys. Res. Commun. 234, 549-553.
48. Dumas, R., Biou, V., and Douce, R. (1997) FEBS Lett. 408, 156-160.
49. Singh, B. K., Stidham, M. A., and Shaner, D. L. (1988) Anal. Biochem. 171, 173-179.
50. Duggleby, R. G. (1997) Gene 190, 245-249.
51. Bork, P., Ouzounis, C., Sander, C., Scharf, M., Schneider, R., and Sonnhammer, E. (1992) Protein Sci. 1, 1677-1690.
52. Oliver, S. G., van der Aart, Q. J. M., Agostoni-Carbone, M. L., Aigle, M., Alberghina, L., Alexandraki, D., Antoine, G., Anwar, R., Ballesta, J. P. G., Benit, P., et al. (1992) Nature 357, 38-46.
53. Baudin, A., Ozier-Kalogeropoulos, O., Denouel, A., Lacroute, F., and Cullin, C. (1993) Nucl. Acids Res. 14, 3329-3330.
54. Cullin, C., Baudin-Baillieu, A., Guillemet, E., and Ozier-Kalogeropoulos, O. (1996) Yeast 12, 1511-1518.
55. Chang, A. K., and Duggleby, R. G. (1998) Biochem. J. 333, 765-777.
56. Subramanian, M. V., Loney-Gallant, V., Dias, J. M., and Mireles, L. C. (1991) Plant Physiol. 96, 310-313.
57. Huppatz, J. L., and Casida, J. E. (1985) Z. Naturforsch. 40c, 652-656.
58. Hervieu, F., and Vaucheret, H. (1996) Mol. Gen. Genet. 251, 220-224.
59. Poulsen, C., and Stougaard, P. (1989) Eur. J. Biochem. 185, 433-439.
60. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
61. Becker, D. M., and Guarente, L. (1991) Methods Enzymol. 194, 182-187.
62. Martyn, J. C., Gould, A. R., and Yu, M. (1994) Virus Res. 33, 11-25.
63. Ward, A. C. (1990) Nucl. Acids Res. 18, 5319.
64. Faulkner, J. D. B., and Minton, N. P. (1993) BioTechniques 14, 718-720.
65. Daum, G., Böhni, P. C., and Schatz, G. (1982) J. Biol. Chem. 257, 13028-13033.
66. Singh, B., Szamosi, I., Hand, J. M., and Misva, R. (1992) Plant Physiol. 99, 812-816.
67. Westerfeld, W. W. (1945) J. Biol. Chem. 161, 495-502.
68. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H. Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Anal. Biochem. 150, 76-85.
69. Laemmli, U. K. (1970) Nature 227, 680-685.
70. Duggleby, R. G. (1984) Comput. Biol. Med. 14, 447-455.
71. Zaret, K. S., and Sherman, F. (1982) Cell 28, 563-573.
72. Xiao, W., and Rank G. H. (1988) Genome 30, 984-986.
73. Magee, P. T., and Hereford, L. M. (1969) J. Bacteriol. 98, 857-862.
74. Arndt, K., and Fink, G. R. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 8516-8520.
75. Donahue, T. F., Daves, R. S., Lucchini, G., and Fink, G. R. (1983) Cell 32, 89-98.
76. Claros, M. G., and Vincens, P. (1996) Eur. J. Biochem. 241, 779-786.
77. Hartl, F. U., Pfanner, N., Nicholson, D. W., and Neupert, W. (1989) Biochim. Biophys. Acta 988, 1-45.
78. Cabrera, N., Rangel, P., Hernández-Muñoz, R., and Pérez-Montfort, R. (1997) Protein Expr. Purif. 10, 340-344.
79. Magee, P. T., and de Robichon-Szulmajster, H. (1968) Eur. J. Biochem. 3, 507-511.
80. Caroline, D. F., Harding, R. W., Kuwana, H., Satyanarayana, T., and Wagner, R. P. (1969) Genetics 62, 487-494.
81. Glatzer, L., Eakin, E., and Wagner, R. P. (1972) J. Bacteriol. 112, 453-464.
82. Takenaka, S., and Kuwana, H. (1972) J. Biochem. 72, 1139-1145.
83. Kuwana, H., and Date, M. (1975) J. Biochem. 77, 257-259.
84. Oda, Y., Nakano, Y., and Kitaoka, S. (1982) J. Gen. Microbiol. 128, 1211-1216.
85. Singh, B. K., and Shaner, D. L. (1995) Plant Cell 7, 935-944.
86. Durner, J., and Böger, P. (1988) Z. Naturforsch. 43c, 850-856.
87. Magee, P. T., and de Robichon-Szulmajster, H. (1968) Eur. J. Biochem. 3, 502-506.