Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Glutamine synthetase mutant with glufosinate resistance and application and cultivation method of glutamine synthese mutant

A glutamine and synthetase technology, applied in the biological field, can solve the problems of interfering with plant nitrogen metabolism, affecting plant growth and development, consumer resistance, etc., and achieve the effect of broad application prospects

Active Publication Date: 2019-09-13
SICHUAN GEVOTO BIOTECH CO LTD
View PDF3 Cites 16 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] 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
[0005] 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 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
Overexpression of wild-type GS in plants can reduce the sensitivity of transgenic plants to glufosinate-ammonium, but the degree of tolerance is not enough for commercial application

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 resistance and application and cultivation method of glutamine synthese mutant
  • Glutamine synthetase mutant with glufosinate resistance and application and cultivation method of glutamine synthese mutant
  • Glutamine synthetase mutant with glufosinate resistance and application and cultivation method of glutamine synthese mutant

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0090] This example provides a plurality of glutamine synthetase (hereinafter referred to as GS) mutants derived from rice (Oryza sativa), and these GS mutants are respectively named: OsA, OsC, OsD, OsE, OsF, OsG, OsH, OsI, OsK, OsP, OsT, OsV, OsY; these GS mutants are compared with the rice wild-type GS (ie reference sequence, SEQ ID NO.1), corresponding to the 59th position of the rice wild-type GS has a mutation, specifically The mutation types are shown in Table 1 below and figure 1 , the length of these GS mutants and the type of amino acid residues at the remaining positions are the same as those of rice wild-type GS.

[0091] Table 1

[0092]

Embodiment 2

[0094] This example provides another GS mutant derived from rice, which is named OsGR. OsGR is compared with the rice wild-type GS (ie, the reference sequence, SEQ ID NO.1), corresponding to the 59th position of the rice wild-type GS and the 296th position have mutations, the specific mutation types are shown in Table 2 and figure 2 ; The length of OsGR and the amino acid residues of other sites are the same as those of rice wild-type GS (SEQ ID NO.1). That is, the 59th position of rice wild-type GS (SEQ ID NO.1) itself was mutated into G and the 296th position was mutated into R to obtain OsGR.

[0095] This embodiment also provides a GS mutant derived from wheat (Triticum aestivum), named TaGR, comparing TaGR with rice wild-type GS (ie, reference sequence, SEQ ID NO.1), corresponding to the first sequence of rice wild-type GS There are mutations at positions 59 and 296, and the specific mutation types are shown in Table 2 and figure 2 ; The length of TaGR and the types o...

Embodiment 3

[0104] This example provides a variety of additional GS mutants derived from rice, and these GS mutants are named: OA, OD, OE, OG, OI, OK, OM, OP, OQ, OR, OS, OT, OV. Comparing these GS mutants with rice wild-type GS (i.e. reference sequence, SEQID NO.1), there is a mutation corresponding to the 296th position of rice wild-type GS, and the specific mutation types are shown in Table 3 and image 3 , 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 (SEQ ID NO.1).

[0105] table 3

[0106]

[0107]

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 discloses a glutamine synthetase mutant with glufosinate resistance and application and a cultivation method of the glutamine sythetase mutant, and relates to the field of biotechnology.Compared the amino acid sequence of the glutamine synthetase mutant with the reference sequence, the glutamine synthetase mutant with glufosinate resistance disclosed in the present invention has oneor two combinations of the following mutations that: (1) the mutation of the glutamine sythetase mutant corresponding to the 59th amino acid site of the reference sequence is X1, wherein X1=A, C, D,E, F, G, H, I, K, P, T, V or Y; and (2) the mutation of the glutamine sythetase mutant corresponding to the 296th amino acid site of the reference sequence is X2, and X2=A, D, E, G, I, K, M, P, Q, R,S, T or V. The glutamine synthetase mutant has the characteristic of glufosinate resistance, and can be used to cultivate new varieties of plants with glufosinate resistance.

Description

technical field [0001] The invention relates to the field of biotechnology, in particular to a glutamine synthetase mutant with glufosinate-ammonium resistance and its application and cultivation method. Background technique [0002] Glufosinate (glufosinate, glufosinate ammonium, trade name Basta) is a glutamine synthetase (GS) inhibitor developed by Aventis (now Bayer), its active ingredient is phosphinothricin (referred to as PPT), chemical name It is (RS)-2-amino-4-(hydroxymethylphosphinyl)ammonium butyrate. The product was launched in 1986, and sales have increased year by year. The target enzyme of glufosinate-ammonium is GS. Under normal circumstances, GS can form λ-glutamyl phosphate from ATP and glutamate. However, after PPT treatment, PPT first combined with ATP, and the phosphorylated PPT occupied the 8 reaction centers of GS molecule, which changed the spatial configuration of GS and inhibited the activity of GS. PPT inhibits all known forms of GS. As a resul...

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): C12N9/00C12N15/52C12N15/82A01H5/00A01H6/46
CPCC12N9/93C12Y603/01002C12N15/8277Y02A40/146
Inventor 邓龙群张震卢远根付颖钊唐宜向汝华冯小容胥南飞
Owner SICHUAN GEVOTO BIOTECH CO LTD
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com