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Rhodopseudomonas palustris GroEL protein and preparation method and application thereof

A swamp erythropseudomonas, protein technology, applied in the directions of botanical equipment and methods, applications, chemical instruments and methods, etc., to achieve the effects of non-toxicity to humans and animals, inhibition of pathogenicity, and simple and convenient application

Pending Publication Date: 2019-10-01
HUNAN PLANT PROTECTION INST
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  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

[0007] In view of the problem that there is no effective prevention and treatment of blast fungus in the existing biopesticides, the invention provides a Rhodopseudomonas palustris GroEL protein and its preparation method and application, which can effectively inhibit blast fungus oryzae

Method used

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  • Rhodopseudomonas palustris GroEL protein and preparation method and application thereof
  • Rhodopseudomonas palustris GroEL protein and preparation method and application thereof
  • Rhodopseudomonas palustris GroEL protein and preparation method and application thereof

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Effect test

Embodiment 1

[0036] The preparation method of Rhodopseudomonas palustris GroEL protein,

[0037] Include the following steps:

[0038] (1) Prokaryotic expression of Rhodopseudomonas palustris GROEL gene in Escherichia coli

[0039] Constructing the vector: connecting the nucleotide sequence of the Rhodopseudomonas palustris GROEL gene to the PET32a plasmid containing the ampicillin resistance gene;

[0040] 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;

[0041] 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 stationary phase; then inoculate the b...

Embodiment 2

[0045] Application of GroEL Protein from Rhodopseudomonas palustris in Inhibiting Magnaporthe grisea

[0046] (1) Application of Rhodopseudomonas palustris GroEL protein in inhibiting the formation of conidia of blast fungus oryzae

[0047] Select the Rhodopseudomonas palustris GroEL protein prepared in Example 1 (final concentrations are respectively 0 μg / ml, 50 μg / ml, 100 μg / ml, 200 μg / ml, 500 μg / ml), and add it to the conidia of Magnaporthe oryzae Liquid (1×10 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;

[0048] Such as figure 2 As shown, the results show that the final concentration of Rhodopseudomonas palustris GroEL protein treatment with a final concentration of 500ug / mL has a significant ...

Embodiment 3

[0053] Referring to Example 2 "Application of Rhodopseudomonas palustris CroEL Protein in Inhibiting the Formation of Pyricularia Oryzae Conidia Appresses", after the prokaryotic expression, the concentration of 500ug / mL 3-hydroxyacyl dehydratase FabA, foreign Membrane protein assembly factor BamA and GroEL 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 2454bp, and the protein molecular weight is 93.5kD.

[0054] Such as Figure 4 As shown, after the GroEL protein was processed, the conidial appressorium formation rate of Magnaporthe grisea only reached about 75%, which was significantly lower than that of the CK control (** represents a very significan...

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Abstract

The invention discloses a rhodopseudomonas palustris GroEL protein and a preparation method and application thereof and belongs to the technical field of biological pesticides. The rhodopseudomonas palustris GroEL protein is obtained by prokaryotic expression of rhodopseudomonas palustris GROEL gene in escherichia coli and protein purification; the rhodopseudomonas palustris is a rhodopseudomonaspalustris LY-6 strain and is preserved at the China Center for Type CultureCollection, the preservation number is CCTCC NO:M2014525, and the preservation number is October 29, 2014. Aiming at the problem that existing biopesticides cannot effectively prevent and control magnaporthe grisea, the invention provides the rhodopseudomonas palustris GroEL protein and the preparation method and application thereof.

Description

technical field [0001] The invention belongs to the technical field of biopesticides, in particular to a Rhodopseudomonas palustris GroEL protein and its preparation method and application. Background technique [0002] Molecular chaperones are a class of functional proteins that can recognize the unstable conformation of other proteins and promote their stability by effectively binding and releasing them. At present, according to the size, structure and function of their sequences, molecular chaperones are divided into five categories: Hsp100 (Heat shock protein 100), Hsp90, Hsp70, Hsp60 and sHsp (small molecule heat shock protein). Hsp60, also known as chaperone 60 protein, is named GroEL in prokaryotes. The protein is a homo-oligomeric complex consisting of 14 subunits of the same molecular weight (57ku) forming a bicyclic cylindrical structure, and 7 subunits forming a ring , the two rings join back-to-back to form two cavities. GroEL binds the polypeptide to form a te...

Claims

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Application Information

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IPC IPC(8): C07K14/195C12N15/70A01N63/02A61P3/00
CPCC07K14/195C12N15/70A01N63/10
Inventor 陈岳吴希阳刘勇张德咏谭新球毛亮
Owner HUNAN PLANT PROTECTION INST
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