Deoxyribonucleic acid coding for glutathione-S-transferase and i

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease

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4352523, 43525233, 435410, 4353201, 536 231, 536 232, 536 236, 800278, 800300, C12N 910, C07H 2104

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059687967

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BRIEF SUMMARY
The present invention relates to a novel deoxyribonucleic acid (DNA) and its use for the transformation of vectors, host organisms and plants and for producing plants which have increased resistance to herbicides.
The genetic modification of plants so that they have increased resistance to particular herbicides has already been disclosed. This makes it possible to employ herbicides which have low selectivity but otherwise advantageous properties in crops of those plants which, in the original non-transgenic form, would be damaged by these herbicides. Thus, the provision of herbicide-resistant plants increases the selection of herbicides which can be employed, and in many cases it is also possible to make do with relatively low herbicide application rates, for example if control of the unwanted plants can take place only after their emergence when the particular damage threshold is reached. There is thus a considerable need to produce novel crop plants which have increased resistance to other herbicides.
Glutathione S-transferases are multifunctional proteins which make a considerable contribution to the detoxification of cytotoxic substances. The enzymes catalyze the conjugation of reduced glutathione to electrophilic hydrophobic substrates which may be of natural or synthetic origin.
The physiological substrates of glutathione S-transferases in plants and their role in plant metabolism are not known in detail. However, it has been demonstrated that these enzymes are involved in the detoxification and thus in the mechanism of selectivity of a number of important herbicides from the group of thiocarbamates, chloroacetanilides and S-triacines: Mozer T. J., Tiemeier D. C., Jaworski E. G., Biochemistry 22:1068-1072 (1983); Moore R. E., Davies M. S., O'Connell K. M., Harding E. I., Wiegand R. C., Tiemeier D. C., Nucleic Acids Res. 14:7227-7235 (1983); Grove G., Zarlengo R. P., Timmermann K. P., Li N., Tam M. F., Tuc C. P. D., Nucleic Acids Res. 16:425-438 (1988).
The novel deoxyribonucleic acid which codes for the novel protein glutathione S-transferase IIIc ("GSTIIIc" hereinafter), which has the amino-acid sequence listed in SEQ ID NO: 2, has now been found (the novel DNA according to the invention being referred to as "GSTIIIc DNA" hereinafter).
It has furthermore been found that plants into whose genome the novel GSTIIIc DNA has been incorporated have an increased resistance, by comparison with the corresponding "starting plants", to herbicides, preferably heteroaryloxyacetamide herbicides.
The novel GSTIIIc DNA was isolated from maize (Zea mais) of the Mutin variety. This DNA codes for the protein GSTIIIc with the amino-acid sequence shown in SEQ ID NO: 2. In plant cells, 2 molecules of the protein GSTIIIc spontaneously form the dimeric active enzyme (referred to as "GSTIIIc enzyme" hereinafter), which ensures detoxification of the herbicide employed and thus makes the plants resistant to the herbicide.
The GSTIIIc DNA which is preferred according to the invention has the sequence listed in SEQ ID NO: 1.
Likewise preferred according to the invention is the GSTIIIc DNA as is contained on the vector plasmids pET3a-GSTIIIc and pSS-GSTIIIc described hereinafter.
The novel GSTIIIc DNA can be in the form of a single strand or in the form of the double strand which additionally contains a strand complementary to the particular single strand.
In a preferred embodiment of the present invention, the GSTIIIc DNA has a promoter which is effective in plants inserted upstream at the 5' end. The usual promoters which are effective in plants can be used for this purpose. An example which may be mentioned is the promoter of the gene of the small subunit of ribulose-1,5-biphosphate carboxylase (rbsc) (compare EMBO Journal, vol. 5 No. 9, 2063-2071 (1986)). Promoters from plant viruses are preferably employed, mention being made of the CaMV 35S RNA promoter as example. The known construct of the CaMV 35S enhancer and the CaMV 35S promoter which follows in the 5'-3' sequence ("CaMV 35S double promoter") is particularly preferab

REFERENCES:
patent: 5589614 (1996-12-01), Bridges et al.
patent: 5714365 (1998-02-01), Van Assche et al.
Moore et al. "Cloning and expression of a cDNA encoding a maize glutathion-S-transferase in E. coli" Nucleic Acid Res. 14, 7227-7235, 1986.
Grove et al. "Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family" Nucleic Acid Res. 16, 425-438, 1988.

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