Hostname: page-component-848d4c4894-p2v8j Total loading time: 0 Render date: 2024-05-01T01:47:34.126Z Has data issue: false hasContentIssue false
  • English
  • Français

Thermal dependence of bioengineered glufosinate tolerance in cotton

Published online by Cambridge University Press:  20 January 2017

James R. Mahan ,
Peter A. Dotray ,
Ginger G. Light  and
Kristy R. Dawson
Peter A. Dotray
Affiliation:
Department of Plant and Soil Science, Texas Tech University, Box 42122, Lubbock, TX 79409-2122
Ginger G. Light
Affiliation:
RR 1, Box 109, Petersburg, TX 79250
Kristy R. Dawson
Affiliation:
Honors College, 103 McClellan Hall, Box 41017, Texas Tech University, Lubbock, TX 79409-1017
Get access Rights & Permissions [Opens in a new window]

Abstract

Tolerance to glufosinate has been bioengineered into cotton through the expression of a gene encoding the enzyme phosphinothricin acetyl transferase (PAT). Studies were conducted to determine thermal limitations on herbicide efficacy in bioengineered cotton. The 50% inhibition (I50) of glufosinate of the target-site enzyme glutamine synthetase was thermally dependent with the lowest values between 25 and 35 C. Larger values of I50 were measured above and below the 25 to 35 C range. The apparent Michaelis constant KM of the enzyme PAT was relatively stable from 15 to 30 C and increased more rapidly from 30 to 45 C. The two components in combination suggest the aggregate tolerance to glufosinate would not be thermally limited between 15 and 45 C. The thermal dependence of the aggregate tolerance in cotton suggests that glufosinate would not damage the crop over a range of temperatures. This prediction is in agreement with the results of field studies carried out over a number of years, which showed the glufosinate-tolerant cotton to be undamaged by glufosinate over a wide range of temperatures.

Keywords

Glufosinatecotton, Gossypium hirsutum L. ‘SeedCo 9023’, ‘DeltaPine 458’Glutamine synthetaseMichaelis-Menten constantphosphinothricin acetyl transferase
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 54 , Issue 1 , February 2006 , pp. 1 - 5
Copyright
Copyright © Weed Science Society of America 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Literature Cited

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.CrossRefGoogle ScholarPubMed
Blair-Kerth, L. K., Dotray, P. A., Keeling, J. W., Oliver, M. J., and Quisenberry, J. E. 2001. Tolerance of transformed cotton to glufosinate. Weed Sci 49:375–380.CrossRefGoogle Scholar
Bradshaw, L. D., Padgette, S. R., Kimball, S. L., and Wells, B. H. 1997. Perspectives on glyphosate resistance. Weed Technol 11:189–198.CrossRefGoogle Scholar
De Block, M., Botterman, J., Vandewiele, M., Dockx, J., Thoen, C., Gossele, V., Rao Movva, N., Thompson, C., Van Montagu, M., and Leemans, J. 1987. Engineering herbicide resistance in plants by expression of a detoxifying enzyme. J EMBO 6:2513–2518.CrossRefGoogle Scholar
Dotray, P. A., Marshall, L. C., Parker, W. B., Wyse, D. L., Somers, D. A., and Gengenbach, B. G. 1993. Herbicide tolerance and weed control in sethoxydim-tolerant corn (Zea mays L). Weed Sci 41:213–217.CrossRefGoogle Scholar
Kingdon, H. S., Hubbard, J. S., and Stadtman, E. R. 1968. Regulation of glutamine synthetase, XI: the nature and implications of a lag phase in the Escherichia coli glutamine synthetase reaction. Biochemistry 7:2136–2142.CrossRefGoogle ScholarPubMed
Light, G. G., Dotray, P. A., and Mahan, J. R. 1999. Thermal dependence of pyrithiobac efficacy in Amaranthus palmeri . Weed Sci 47:644–650.CrossRefGoogle Scholar
Light, G. G., Dotray, P. A., and Mahan, J. R. 2001. A thermal application range for postemergence pyrithiobac applications. Weed Sci 49:543–548.CrossRefGoogle Scholar
Mahan, J. R. 1994. Thermal dependence of glutathione reductase: thermal limitations on antioxidant protection in plants. Crop Sci 34:1550–1556.CrossRefGoogle Scholar
Mahan, J. R. 2000. Thermal dependence of malate synthase activity and its relationship to the thermal dependence of seedling emergence. J. Agric. Food Chem 48:4544–4549.CrossRefGoogle Scholar
Mahan, J. R., Burke, J. J., and Orzech, K. A. 1990. Thermal dependence of the apparent KM of glutathione reductases from three plant species. Plant Physiol 93:822–824.CrossRefGoogle ScholarPubMed
Mahan, J. R., Burke, J. J., Upchurch, D. R., and Wanjura, D. W. 2000. Irrigation scheduling using biologically based optimal temperature and continuous monitoring of canopy temperature. Acta Hortic 537:375–379.CrossRefGoogle Scholar
Mahan, J. R., Dotray, P. A., and Light, G. G. 2004. Thermal dependence of enzyme function and inhibition; implications for herbicide efficacy and tolerance. Physio. Plant 120:187–195.CrossRefGoogle Scholar
Monaco, T. J., Weller, S. C., and Ashton, F. M. 2002. Weed Science Principles and Practices, 4th ed. New York: J. Wiley.Google Scholar
Shaw, W. V. 1975. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol 43:737–755.CrossRefGoogle ScholarPubMed