Glutamine synthetase mutant with glufosinate-ammonium resistance, recombinant gene, recombinant vector and application thereof

A glutamine and recombinant gene technology, applied in the field of bioengineering, can solve the problems of non-inhibition, achieve the effect of improving resistance and broad application prospects

Pending Publication Date: 2022-03-01
CROPEDIT BIOTECHNOLOGY INC
View PDF4 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, the main anti-glufosinate-ammonium genes are derived from the bacterial Pat gene and Bar gene, both of which can encode glufosinate-ammonium acetylase, which can acetylate PPT, and the acetylated product does not inhibit glutamine Synthetic enzyme activity

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Glutamine synthetase mutant with glufosinate-ammonium resistance, recombinant gene, recombinant vector and application thereof
  • Glutamine synthetase mutant with glufosinate-ammonium resistance, recombinant gene, recombinant vector and application thereof
  • Glutamine synthetase mutant with glufosinate-ammonium resistance, recombinant gene, recombinant vector and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0033] This embodiment provides multiple glutamine synthetase (glutaminesynthetase, GS) mutants derived from rice (Oryza sativa), these GS mutants are named: OS_WT, OS_RA, OS_RC, OS_RH, OS_RI, OS_RK, OS_RM, OS_RN , OS_RP, OS_RQ, OS_RT, OS_RV; these GS mutants are compared with the rice wild-type GS amino acid sequence (SEQID NO.1), corresponding to the 311th amino acid sequence (OS_WT) of the rice wild-type GS mutation, specifically mutation type see figure 1 , the gray shading is position 311, the length of these GS mutants and the amino acid residue types of the remaining positions are the same as those of rice wild-type GS.

Embodiment 2

[0035] This example provides the corn glutamine synthetase mutant ZmGS1_RK, compared with the rice wild-type GS amino acid sequence (SEQ ID NO.1), such as figure 2 Alignment of the amino acid sequences of the wild-type GS of rice, corn and rapeseed shown with the amino acid sequences of the corresponding mutants. The 311th position corresponding to the amino acid sequence of rice wild-type GS is mutated, the specific mutation R311K; the length of ZmGS1_RK and the amino acid residue types of other positions are the same as those of maize wild-type GS (SEQ ID NO.2).

Embodiment 3

[0037]This example provides rapeseed glutamine synthetase mutant BnGS1_RK, compared with rice wild-type GS (SEQ ID NO.1), corresponding to the 311th position of the rice wild-type GS amino acid sequence mutation, the specific mutation R311K; BnRK The length and the amino acid residue types of the remaining positions are the same as those of the rapeseed wild-type GS amino acid sequence (SEQ ID NO.3).

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The invention provides a glutamine synthetase mutant with glufosinate-ammonium resistance and a preparation method of the glutamine synthetase mutant. Arginine (R) corresponding to the 311 position of an amino acid sequence of rice wild-type glutamine synthetase in glutamine synthetase of a target plant is mutated into any one of alanine (A), cysteine (C), histidine (H), isoleucine (I), lysine (K), phenylalanine (M), asparaginic acid (N), proline (P), glutamine (Q), threonine (T) and valine (V). The invention also provides a recombinant gene, a recombinant vector and a recombinant engineering bacterium for coding the glutamine synthetase mutant, and application of the recombinant gene, the recombinant vector and the recombinant engineering bacterium. The mutant provided by the invention can improve the resistance of various plants to glufosinate-ammonium, keeps the biological enzyme catalytic activity of the plants, and can be applied to the cultivation of glufosinate-ammonium-resistant plant varieties.

Description

technical field [0001] The invention relates to the technical field of bioengineering, in particular to a glutamine synthetase mutant with glufosinate-ammonium resistance, nucleic acid molecule and application. Background technique [0002] Glutamine synthetase (GS) is a key enzyme in plant nitrogen metabolism, which catalyzes the conversion of glutamate and NH4 + Synthesis of glutamine, conversion of inorganic nitrogen into organic nitrogen. One glutamine synthetase is located in the cytoplasm, called cytoplasmic GS (GS1); the other is located in the chloroplast (or plastid), called plastid GS (GS2). [0003] Glufosinate ammonium (Glufosinate ammonium, trade name Basta), successfully developed by Hearst in the 1980s (later owned by Bayer), is a broad-spectrum contact herbicide with weak systemic effect. Its active ingredient is phosphinothricin (referred to as PPT), and its chemical name is (RS)-2-amino-4-(hydroxymethylphosphinyl)ammonium butyrate. Glutamine synthetase i...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(China)
IPC IPC(8): C12N9/00
CPCC12N9/93C12N15/81C12Y603/01002C12N15/8277C12N15/902A01H1/02A01H4/00A01H1/1235
Inventor 吴艳斌吴业春靳海霞周玉娇王金羽
Owner CROPEDIT BIOTECHNOLOGY INC
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products