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

A kind of Rhodopseudomonas palustris atps2 protein and its preparation method and application

A swamp erythropseudomonas, protein technology, applied in the directions of botanical equipment and methods, biochemical equipment and methods, applications, etc., to achieve the effects of environmental friendliness, inhibition of pathogenicity, and short cultivation time

Active Publication Date: 2021-05-28
HUNAN PLANT PROTECTION INST
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] Aiming at the problem that there is no effective prevention and control of blast fungus in the existing biological pesticides, the present invention provides a Rhodopseudomonas palustris Atps2 protein and its preparation method and application, which can effectively inhibit blast fungus

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
  • A kind of Rhodopseudomonas palustris atps2 protein and its preparation method and application
  • A kind of Rhodopseudomonas palustris atps2 protein and its preparation method and application
  • A kind of Rhodopseudomonas palustris atps2 protein and its preparation method and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0034] Preparation method of Rhodopseudomonas palustris Atps2 protein,

[0035] Include the following steps:

[0036] (1) Rhodopseudomonas palustris ATPS2 Prokaryotic expression of genes in E. coli

[0037] Construction vector: Rhodopseudomonas palustris ATPS2 The nucleotide sequence of the gene is connected to the PET32a plasmid containing the ampicillin resistance gene;

[0038] Escherichia coli transformation: the plasmid constructed in the previous step is introduced into the expression competent cell BL21, spread on the LB plate containing ampicillin resistance and cultivated; the medium of the LB plate containing ampicillin resistance, the formula For: yeast extract 5g / L, peptone 10g / L, NaCl 5g / L, ampicillin 100mg / L, agar 15g / L, pH=7.0;

[0039] Expansion of transformed strains and protein induction: transfer the single colony cultivated in the previous step into a 120mL Erlenmeyer flask and culture at 37°C until the stable phase; then inoculate the bacteria in the...

Embodiment 2

[0043] Application of Atps2 Protein from Rhodopseudomonas palustris in Inhibiting Magnaporthe grisea

[0044] (1) Application of Atps2 protein from Rhodopseudomonas palustris in inhibiting the formation of conidia of Magnaporthe grisea

[0045] Select the Rhodopseudomonas palustris Atps2 protein prepared in Example 1 (final concentrations are 0 μg / ml, 50 μg / ml, 100 μg / ml, 200 μg / ml, 500 μg / ml), and add it to the conidia of Magnaporthe grisea Liquid (1 x 10 5 pcs / ml) for mixing, then 30 μl was dropped onto the hydrophobic membrane, and each group (corresponding to CK group, 50 μg / ml group, 100 μg / ml group, 200 μg / ml group, 500 μg / ml group) set 3 Repeat, observe microscopically after 8 hours and count the appressor formation rate, and evaluate the respective inhibitory effects;

[0046] Such as figure 2 As shown, the results show that the formation rate of appressoria after treatment with Rhodopseudomonas palustris Atps2 protein with a final concentration of 100 ug / mL is sig...

Embodiment 3

[0051] Referring to Example 2 "Application of Rhodopseudomonas palustris Atps2 Protein in Inhibiting the Formation of Pyricularia Oryzae Conidia Appresses", after prokaryotic expression, 3-hydroxyacyl dehydratase FabA with a concentration of 500 ug / mL was selected respectively , outer membrane protein assembly factor BamA and Atps2 protein were tested, and the appressor formation rate was counted. Among them, the 3-hydroxyacyl dehydratase FabA is derived from 3-hydroxyacyl-[acyl chain protein] dehydratase, the base pair is 525bp, and the protein molecular weight is 18.8kD; the outer membrane protein assembly factor BamA is derived from the outer membrane protein assembly factor, base The base pair is 2454 bp, and the protein molecular weight is 93.5kD.

[0052] Such as Figure 4 As shown, the formation rate of conidia of Magnaporthe grisea after treatment with Atps2 protein was less than 10%, which was significantly lower than that of CK control (** represents a very signific...

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 Rhodopseudomonas palustris Atps2 protein and its preparation method and application, and belongs to the technical field of biological pesticides; the Rhodopseudomonas palustris Atps2 protein is composed of The ATPS2 gene of Rhodopseudomonas palustris was prokaryotically expressed in Escherichia coli and obtained through protein purification; the Rhodopseudomonas palustris LY-6 strain was preserved in the China Center for Type Culture Collection, The deposit number is CCTCC NO: M2014525, and the deposit date is November 5, 2014. Aiming at the problem that the existing biopesticides do not effectively prevent and control the rice blast fungus, the present invention provides a Rhodopseudomonas palustris Atps2 protein and its preparation method and application, which can effectively inhibit the rice blast fungus.

Description

technical field [0001] The invention belongs to the technical field of biopesticides, and in particular relates to a Rhodopseudomonas palustris Atps2 protein and a preparation method and application thereof. Background technique [0002] ATP synthase is a key enzyme of energy metabolism in organisms, involved in oxidative phosphorylation and photophosphorylation reactions, widely present in chloroplasts, mitochondria and bacteria, and located on the inner membrane of mitochondria, chloroplast thylakoid membrane and plasma membrane of photosynthetic bacteria Involved in the final link of oxidative phosphorylation in the respiratory chain. ATP synthase (ATP synthase) consists of two parts, F0 and F1, and is mainly involved in the synthesis of ATP in the process of oxidative phosphorylation in animals including insects. The β subunit of ATP synthase is a less conserved subunit in ATP synthase, which mainly plays the role of connecting and fixing the assembly of F0 and F1 compl...

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 Patents(China)
IPC IPC(8): C12N9/14C12N15/70A01N63/50A01P3/00
CPCC12N9/14C12N15/70C12Y306/03014A01N63/10
Inventor 陈岳吴希阳刘勇张德咏谭新球毛亮
Owner HUNAN PLANT PROTECTION INST
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