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Method for obtaining protein with glufosinate-ammonium resistance and mutant thereof

A glufosinate-ammonium and mutant technology, applied in the field of genetic engineering, can solve problems affecting plant growth and development, disturbing plant nitrogen metabolism, consumer resistance, etc., and achieve the effect of satisfying growth and development and normal nitrogen metabolism

Pending Publication Date: 2022-07-29
SICHUAN GEVOTO BIOTECH CO LTD
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] However, due to the wave of anti-genetics, the acceptance of genetically modified crops in the world is still low. Even in the Americas with the largest planting area of ​​genetically modified crops, genetically modified crops are mainly limited to several crops such as corn, soybeans, and cotton.
In particular, the bar gene and pat gene are derived from microorganisms, not from the crop itself, which is more likely to cause consumers' resistance
[0007] The glufosinate-ammonium acetylase encoded by bar gene and pat gene can inactivate glufosinate-ammonium by acetylation, but before glufosinate-ammonium contacts GS, it is difficult for the enzyme to inactivate glufosinate-ammonium completely, because many GS are distributed in Therefore, when glufosinate-ammonium is applied to transgenic crops with bar gene and pat gene, it will interfere with the nitrogen metabolism of plants to varying degrees, and at the same time affect the normal growth and development of plants
Although overexpression of wild-type GS in plants can reduce the sensitivity of transgenic plants to glufosinate-ammonium, the degree of tolerance is not enough for commercial application

Method used

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  • Method for obtaining protein with glufosinate-ammonium resistance and mutant thereof
  • Method for obtaining protein with glufosinate-ammonium resistance and mutant thereof
  • Method for obtaining protein with glufosinate-ammonium resistance and mutant thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0120] The rice (Oryza sativa) glutamine synthase (GS1) mutant provided in this example is obtained from the wild-type rice glutamine synthase itself (named OsGS1-WT, and the amino acid sequence is shown in SEQ ID NO.1, The 58th amino acid residue S of the coding nucleotide sequence is SEQ ID NO.5) is mutated to A, C, D, E, G, H, I, K, L, M, P, Q, R, T, Y or deletion (X) was obtained, and the obtained rice GS1 mutants were named OS58A, OS58C, OS58D, OS58E, OS58G, OS58H, OS58I, OS58K, OS58L, OS58M, OS58P, OS58Q, OS58R, OS58T, OS58Y, OS58X, respectively.

[0121] The amino acid sequence alignment of OS58A, OS58C, OS58D, OS58E, OS58G, OS58H, OS58I, OS58K, OS58L, OS58M, OS58P, OS58Q, OS58R, OS58T, OS58Y, OS58X and wild-type rice GS1 is as follows figure 2 As shown, in the figure: the position indicated by the arrow is the mutation site.

[0122] In this example, the coding sequence of each rice GS1 mutant is at the position encoding the 58th amino acid, and the codons used for t...

Embodiment 2

[0127] The soybean (Glycine max) GS1 mutant provided in this example is composed of wild-type soybean GS1 itself (named as GmGS1-WT, the amino acid sequence is shown in SEQ ID NO. 3, and the coding nucleotide sequence is SEQ ID NO. 7) The 58th position (corresponding to the 58th position of the reference sequence (SEQ ID NO. 1)) is obtained by mutating the amino acid residue S to D, E, P, and R. The obtained soybean GS1 mutants were named GS58D, GS58E, GS58P, GS58R.

[0128] The amino acid sequence alignment of soybean GS1 mutants GS58D, GS58E, GS58P, GS58R and wild-type soybean GS1 is as follows image 3 As shown, in the figure: the position indicated by the arrow is the mutation site.

[0129] In this example, the coding sequence of each soybean GS1 mutant is at the position encoding the 58th amino acid, the codons used for the corresponding amino acid are shown in the table below, and the nucleotides in the remaining positions are the same as the corresponding wild-type co...

Embodiment 3

[0133] The maize (Zea mays) GS1 mutant provided in this example is composed of wild-type maize GS1 itself (named ZmGS1-WT, the amino acid sequence is shown in SEQ ID NO.2, and the coding nucleotide sequence is SEQ ID NO.6 ) at position 58 (corresponding to position 58 of the reference sequence (SEQ ID NO. 1)) is obtained by mutating the amino acid residue S to D, E, I, K, P, R or deletion (X). The obtained maize GS1 mutants were named ZS58D, ZS58E, ZS58I, ZS58K, ZS58P, ZS58R, ZS58X, respectively.

[0134] The amino acid sequence alignment of maize GS1 mutants ZS58D, ZS58E, ZS58I, ZS58K, ZS58P, ZS58R, ZS58X and wild-type maize GS1 is as follows Figure 4 As shown, in the figure: the position indicated by the arrow is the mutation site.

[0135] In this example, the coding sequence of each maize GS1 mutant is at the position encoding the 58th amino acid, the codons used for the corresponding amino acid are shown in the following table, and the nucleotides in the remaining posit...

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Abstract

The invention discloses a method for obtaining a protein with glufosinate-ammonium resistance and a mutant thereof, and relates to the technical field of gene engineering. The glutamine synthetase mutant provided by the invention has the application potential of constructing an expression vector for transforming plants and cultivating glufosinate-ammonium-resistant crops. The glutamine synthetase mutant provided by the invention is originally derived from plants, and is easier to accept by consumers compared with glufosinate-ammonium-resistant genes such as pat or bar derived from bacteria. The glutamine synthetase mutant has glufosinate-ammonium resistance after mutation, and a plant converted with the glutamine synthetase mutant not only has glufosinate-ammonium resistance suitable for commercial application, but also can keep normal enzyme catalytic activity of glutamine synthetase, and can meet normal growth and development of the plant.

Description

technical field [0001] The present invention relates to the technical field of genetic engineering, in particular, to a method for obtaining a protein with glufosinate resistance and a mutant thereof. Background technique [0002] Glutamine synthetase (GS) is a key enzyme in plant nitrogen metabolism, which catalyzes the conversion of glutamate (Glu) to NH in the glutamate synthetase cycle. 3 Condensed to form glutamine (Gln), which is involved in the metabolism of nitrogenous compounds in plants. According to the distribution and subcellular localization of glutamine synthase, higher plant GS (belonging to GSII) isozymes can be divided into two types: one is located in the cytoplasm called cytoplasmic GS (GS1), with a molecular weight of 38- 40kDa; the other is located in the chloroplast (or plastid) called plastid-type GS (GS2), with a molecular weight of 44-45kDa. [0003] Glufosinate (glufosinate ammonium, trade name Basta) is a glutamine synthase (GS1) inhibitor devel...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12N9/00C12N15/52C12N15/70C12N15/82A01H5/00A01H6/00C12N1/21C12R1/19
CPCC12N9/93C12N15/70C12N15/8277C12Y603/01002
Inventor 邓龙群胡江博陈容张震侯青江胥南飞
Owner SICHUAN GEVOTO BIOTECH CO LTD
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