48 results about "Chaperonin" patented technology

The invention discloses an aspergillus niger recombinant bacterium AnCT-XynB-K-agdA and application thereof, and belongs to the technical field of microbiology and bioengineering. According to the invention, Aspergillus niger AnCat is taken as an expression host, firstly, an acid protease regulatory factor prtT is knocked out to obtain a defective strain, and then different chaperonins are subjected to fusion expression by optimizing integration sites of a laccase lcc9 expression cassette, so that the high-expression laccase chaperonin is obtained. According to the method, an expression vector pC3-5 'agdA-PcitA-XynB-L-lcc9-hph-3' agdA is constructed, a recombinant bacterium AnCT-XynB-K-agdA is further obtained, the enzyme activity of the extracellular laccase subjected to shake flask fermentation reaches 1821.2 U / L, and finally, the recombinant efficient expression of the laccase Lcc9 in aspergillus niger is realized.

This article describes a method for preventing or treating severe asthma by administering peptides associated with chaperone protein 60.1.

The invention provides a composition comprising a Plasmodium species multimeric protein capable of forming a nanoparticle and at least one antigen of interest, wherein the multimeric protein comprises a monomer chosen from Plasmodium species pyridoxal 5'-phosphate synthase (PLP), chaperone 60 protein (Cpn60), and caseinolytic protease (Clp). In embodiments, the invention provides the composition wherein the monomers assemble to form a multimeric nanoparticle and / or which comprises an adjuvant. The invention further provides a nucleic acid encoding the multimeric protein and the at least one antigen of interest, E. coli comprising the nucleic acid, and the use of such in a method for producing the inventive multimeric protein and the at least one antigen of interest. Also provided are a method and use of the inventive multimeric protein and the at least one antigen of interest for immunizing a subject against Plasmodium species.

Disclosed herein are compounds and methods of use thereof effective for the treatment of neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), a disease that affects nerve cells in the brain and spinal cord, eventually causing loss of muscle strength. The compounds of the disclosure include, cutamesine, a synthetic sigma receptor agonist selective for the 81 receptor, and also a chaperone protein of the central nervous system that plays a key role in the modulation of calcium ions and apoptosis, as well as a sapogenin, such as smilagenin, a non-peptide neurotrophic factor that aids in the reversal of free radical neurotoxicity.

The invention relates to the field of biotechnology and medicine, and discloses a polypeptide targeting molecular chaperonin TRIC / CCT and application thereof. The sequence of the polypeptide is consistent with or truncated from the C-terminal sequence of a CCT subunit, and the polypeptide can be competitively combined with CRL4-DCAF12 ubiquitin ligase, so that the ubiquitination of the CCT subunit is reduced, and the formation of a TRIC / CCT compound is inhibited; the polypeptide inhibits the formation of a TRIC / CCT compound and blocks the activation of key metastasis promoting signal channels such as YAP, STAT3 and mTOR, thereby inhibiting the metastasis of lung cancer. According to systematic in-vivo and in-vitro experiments, the compound has excellent performance in the aspect of inhibiting lung cancer cell migration and metastasis, has the characteristics of clear target spot, clear action mechanism and the like, and provides a new treatment strategy for developing a new generation of lung cancer metastasis resisting medicines.

A transformed microorganism having an ability to produce a polyhydroxyalkanoate includes a polyhydroxyalkanoate synthase gene and a gene encoding a chaperone belonging to the ClpB family. The gene encoding the chaperone belonging to the ClpB family is a gene which has been introduced into the transformed microorganism or whose expression has been enhanced in the transformed microorganism. The chaperone belonging to the ClpB family may be derived from the genus Cupriavidus, Escherichia, or Saccharomyces. A polyhydroxyalkanoate can be produced by culturing the transformed microorganism.

Provided are a mutant of a small molecular chaperone protein MOG1-encoding gene and use thereof. The mutant is more effective than a wild-type MOG1 in enhancing myocardial sodium current, and the mutant of the small molecular chaperone protein MOG1-encoding gene and a mutant of the small molecular chaperone protein MOG1 are used in the preparation of medicaments for the treatment of diseases such as Brugada syndrome, arrhythmia, dilated cardiomyopathy, or heart failure.

The invention relates to double stranded ribonucleic acid (dsRNAi) agents and compositions targeting the SCAP gene, as well as methods of inhibiting expression of a SCAP gene and methods of treating subjects having a SCAP-associated disorder, such as nonalcoholic fatty liver disease (NAFLD) or nonalcoholic steatohepatitis (NASH), using such dsRNAi agents and compositions.

This invention relates to the field of biotechnology, and more particularly to the application of the wheat molecular chaperone protein TaBiP1 in the control of wheat scab. This invention is the first to discover that overexpression of the wheat molecular chaperone protein TaBiP1 can significantly reduce the infection severity of wheat scab. Compared with the transgenic recipient parent Fielder, TaBiP1-overexpressing plants significantly reduce wheat scab infection and can be used to create new scab-resistant germplasm. In this invention, the TaBiP1 gene in recipient wheat is edited using CRISPR / Cas9 gene editing technology to obtain transgenic plants. bip1 The resistance of wheat to Fusarium head blight was weaker than that of Fielder, which confirms the positive significance of TaBiP1 in enhancing wheat resistance to Fusarium head blight.

The invention belongs to the technical field of globular protein synthesis, and particularly relates to a chaperonin-assisted recombinant human hFGF-2 protein preparation method and application thereof, the chaperonin-assisted recombinant human hFGF-2 protein preparation method comprises the following steps: S1, constructing a recombinant vector TrxA-6H-DDDDK-hFGF2 containing an hFGF-2 fusion protein coding sequence; s2, transforming the recombinant vector into an escherichia coli host cell for induced expression to obtain an expression thallus; s3, crushing the expression thalli to obtain a cell lysis supernatant; s4, taking the supernate, carrying out nickel column affinity chromatography, carrying out desalination treatment on the fusion protein by adopting gel chromatography, and collecting a fusion protein eluent; s5, performing enterokinase cutting treatment on the fusion protein to obtain an enzyme-digested product; s6, performing heparin affinity chromatography on the enzyme digestion product, and collecting hFGF-2 protein eluent; and S7, carrying out dialysis treatment on the protein eluent to obtain the recombinant hFGF-2 protein.

The application discloses a method for removing chaperone and application thereof. The method for removing chaperone comprises the following steps: after a sample containing a target recombinant protein is loaded on an affinity chromatography column, a washing liquid containing urea and KCl is used to flush the affinity chromatography column, so as to remove the chaperone combined with the target recombinant protein. The method of the application can effectively remove the chaperone of about 60 kDa from an escherichia coli host bacterium by combined washing of urea and KCl, and has the advantages of simple operation, low cost, good chaperone removal effect for various recombinant proteins with different molecular weights, wide universality, and the like, and can significantly improve the purity and quality of the recombinant protein.

This invention discloses a sucrose isomerase site mutant, a genetically engineered bacterium, and a method for catalyzing the production of isomaltulose. This invention utilizes PROSS online analysis combined with sequence alignment analysis to screen key amino acid sites related to catalytic activity in sucrose isomerases. Through site-directed mutagenesis, the mutant WT-Gro7-Q474T was obtained, with a maximum specific enzyme activity of 683 U / mg. k cat (s ‑1 The concentration reached 718. By optimizing protein expression conditions, including temperature, IPTG concentration, bacterial concentration, and time, and combining this with the method of co-expression of molecular chaperone proteins, a highly efficient heterologous expression system for sucrose isomerase was established. This invention established an optimal isomaltulose-catalyzed reaction system: in a 2 L reactor, with 1 L of reaction solution and a substrate concentration of 800 g / L sucrose, after 6 hours of reaction, all sucrose was converted, yielding isomaltulose 792.50 g / L, with a conversion rate >99.5%.

Methods and compositions for enhancing heterologous protein expression in plants are provided. The invention is directed to the co-expression of a heterologous protein of interest with a specific endoplasmic reticulum (ER)-resident molecular chaperone protein. Co-expressing chaperones such as a native soybean protein disulfide isomerase-like protein (Glyma.01G003700, Glyma.04g247900, Glyma.03G218300, or Glyma.18G204000), or a heterologous mammalian chaperone (bovine DNAJB12) with casein proteins in soybean cells resulted in a significant increase in casein accumulation, with up to 4-fold enhancement observed. The methods are broadly applicable for improving the yield of complex recombinant proteins, including milk proteins, therapeutic proteins, and industrial enzymes, in plant-based production systems, thereby overcoming common limitations related to protein folding and stability.

A siRNA characterised by having a sequence selected from the group comprised of: - SEQ ID NO. 1 : 5 ' CUCUUUCCCUUGAAUAAGC 3 '; - SEQ ID NO. 2 : 5 ' UGAUUCCCAAAGCUCACAG 3 '; and - a sequence including at least 16 contiguous nucleotides differing by no more than 3 nucleotides from SEQ ID No. 1 or SEQ ID No. 2, to silence TRAPl-low SEQ ID N°3. The use of the 5 'UTR SEQ ID N°4 region of the TRAPl-low transcript SEQ ID N°3 or a portion of that 5 'UTR region selected from the group comprised of: - the SEQ ID No. 6 portion of said 5 ' UTR region comprising nucleotide positions 1 through 644; - a portion of said region 5 ' UTR comprising the portion of SEQ ID No. 6 extended by a predetermined number of nucleotide positions beyond nucleotide position 644 along said region 5 'UTR.

The application discloses a plant coding gene and protein with improved cadmium resistance and promoted biomass and a transgenic strain. The application carries out RNA-seq sequencing on switchgrass under cadmium stress treatment, screens a differential expression gene with the highest up-regulation fold, and genome annotation shows that the gene codes a member of a heat shock protein 70 family (Hsp70), a chaperone BiP (Binding Protein) protein, and the gene is named as PvBiP2. An overexpression vector of the gene is constructed and is transferred into a cadmium-sensitive yeast mutant strain (ycf1), and the growth condition of the transgenic yeast on a cadmium-containing culture medium is obviously better than that of a control group. Overexpression of the PvBiP2 gene in switchgrass is found to significantly improve the cadmium resistance of the transgenic switchgrass and promote the biomass of the switchgrass.

The present invention relates to an inhibitor of heat shock protein 90, and discloses a bivalent inhibitor based on heat shock protein 90, a preparation method, and an application thereof. The compound has a structural formula as shown in Formula I: A-L-B Formula I, or a pharmaceutically acceptable salt, solvate, or optical isomer thereof, wherein A and B are ATP inhibitors of heat shock protein 90, and the motif structure of L is a flexible linking group of PEG and alkane, or a rigid linking group having an aryl, heteroalkyl, or heteroaryl group. The bivalent inhibitor can effectively inhibit the activity of the molecular chaperone protein HSP90, hinder the folding and modification of substrate proteins, degrade substrate proteins through the ubiquitin-proteasome pathway, induce non-native dimerization of HSP90, and interfere with protein-protein interactions associated with HSP90. At the same time, it also reduces the heat shock effect caused by HSP90 inhibition, and exhibits potent activity in degrading substrate proteins.

The application discloses a kind of recombinant engineering bacteria for co-expression BIP production antitumor ginseng peptide, the engineering bacteria is preserved in China general microbiological bacterial strain preservation center, and the preservation number is CGMCC NO:29804, and the preservation date is January 29, 2024.The engineering bacteria of the application is by genetic means, with pichia pastoris GS115 as host bacteria, simultaneously express the ginseng polypeptide gene with strong anti-colon cancer activity and the molecular chaperone protein BIP that can help protein correct folding and secretion, realize stable and efficient production of recombinant antitumor ginseng peptide F0630.

The invention discloses a bacillus amyloliquefaciens genetically engineered bacterium with high antibiotic resistance as well as a construction method and application thereof, the construction of the engineered bacterium comprises the following steps: bacillus amyloliquefaciens is taken as a starting strain, an RNA (Ribonucleic Acid) molecular chaperonin hfq coding gene is knocked out, and the nucleotide sequence of the RNA molecular chaperonin hfq is shown as SEQ ID NO.1. The RNA molecular chaperonin hfq is obtained through cloning, the tolerance of engineering bacteria to erythromycin and ampicillin is increased by 2.44 times and 3.79 times by knocking out the gene or reducing the expression of the gene, and the enhancement of the antibiotic resistance of bacillus is crucial to the threat of drug-resistant bacteria, the improvement of environmental adaptability and the development of biotechnology application. By strengthening the resistance gene, drug-resistant pathogens can be efficiently inhibited, the antibacterial curative effect can be improved, the metabolic activity can be maintained in a complex antibiotic environment, and the pollution repair and industrial fermentation efficiency can be guaranteed.

Provided are tumor-targeted protein degradation chimeras, termed chaperone-mediated protein degraders (CHAMPs) comprising a first moiety that is capable of binding to a target protein (e.g., KRAS(G12D) or proteins and a second moiety that is capable of binding a chaperone protein or proteins or protein component of chaperone complexes (e.g., HSP90). Pharmaceutical compositions comprising the disclosed CHAMPs and their uses for treating thereof, which are useful for treating cancers and related conditions are also provided.

This disclosure provides expression systems comprising secretion signals that promote production and / or secretion of proteins of interest, as well as one or more polynucleotides encoding chaperone proteins (e.g., CRT and / or PDIA3) which, as demonstrate herein, enhance production and / or secretion of proteins. Moreover, genetically modified host cells comprising these expression systems are capable of producing high levels of protein of interest, such as bovine lactoferrin (bLF), bovine lactoglobulin (bLG), or ovalbumin (Ova).

Disclosed are fusion polypeptides that are substrates for white Kunitz's transglutaminase. The fusion polypeptides comprise one or more FKBP chaperone proteins and a target polypeptide. Each of these elements is separated from adjacent elements by a linker amino acid sequence. It has been found that it is advantageous to insert a glutamic acid-containing transglutaminase recognition motif into the linker amino acid chain. The subsequent labeling reaction catalyzed by the transglutaminase surprisingly provides a labeled fusion polypeptide with superior properties compared to chemically randomly labeled fusion polypeptides of similar design. Assays and kits for detecting a target antibody in a sample in vitro are provided.

The invention discloses a redox chaperonin PDX mutant for improving steroid hydroxylation catalysis activity of cytochrome P450 and application, according to the PDX mutant provided by the invention, the efficiency of OlePM for catalyzing LCA to generate UDCA is remarkably improved, mutants such as Y34I, Y34S, Y34E, Y34H, R67G, R67D, R67A, R67S, I90L, I90M, I90E, I90V and I90S are excellent in performance, and the UDCA concentration can reach 0.13-0.21 g / L and is improved by 5-8 times compared with that reported in literatures. By improving the electron transfer efficiency of the redox chaperonin, the steroid hydroxylation performance of the cytochrome P450 is remarkably enhanced, a new biocatalyst is provided for efficient and green biosynthesis of UDCA, and the method has important industrial application value.

The application discloses a kind of RNA chaperone, coding gene and high stress resistance recombinant bacteria expressing the RNA chaperone and its preparation method, it is related to the field of bioengineering.RNA chaperone PyCsp has the activity of binding RNA.By constructing the recombinant plasmid of expression RNA molecule PyCsp chaperone, the recombinant plasmid is transferred into target bacteria to prepare recombinant bacteria, i.e., the recombinant bacteria with high stress resistance, the stress resistance is low-temperature tolerance, high-pressure tolerance or high-temperature tolerance.The application digs out a heat-resistant RNA chaperone from super-thermophilic pressure-loving microorganism (optimum growth temperature 95 DEG C).Such high-temperature-resistant RNA chaperone as stress resistance element has important application value in improving the stress resistance of microorganism to high temperature, low temperature and high hydrostatic pressure and other environmental stress conditions, and has unique advantages in improving the stress resistance of strain used in fermentation in the application scene of bioengineering related to high temperature and high pressure.

This invention relates to the field of plant genetic engineering technology, specifically to genes encoding metal chaperone proteins. OsHMD1 Applications in increasing the zinc content of rice grains. OsHMD1 The use of genes or related biological materials in at least one of the following: A1) regulating the zinc content of rice grains or preparing products that regulate the zinc content of rice grains; A2) cultivating rice with increased zinc content in grains or preparing products that increase the zinc content of rice grains; A3) preparing transgenic rice; OsHMD1 The nucleotide sequence encoding the gene is shown in SEQ ID NO.2. This invention provides a new target for elucidating the regulatory mechanism of zinc accumulation in rice, enriches the resource of functional genes for zinc enrichment in grains, and can be applied to the genetic improvement breeding of zinc-enriched rice.

The invention relates to the field of plant gene functions, in particular to a fusion protein, a method for producing ferritin from plants and application. The invention provides a fusion protein. The fusion protein comprises endoplasmic reticulum chaperonin, ferritin and endoplasmic reticulum retention signal peptide from an N terminal to a C terminal, researches find that efficient expression and stable accumulation of ferritin in plant cells are realized by fusing specific signal peptide and an endoplasmic reticulum retention sequence in a target gene, the design not only improves the expression level of ferritin in the plant cells, but also improves the expression level of ferritin in the plant cells through the processing and modification effects of the endoplasmic reticulum. The stability and the biological activity of the ferritin are enhanced. Meanwhile, due to the existence of the endoplasmic reticulum retention sequence, ferritin is effectively retained in the endoplasmic reticulum, and degradation and interference in cytoplasm are avoided, so that the target protein yield is increased.

Genetically modified cells (e.g., recombinant mammalian cells) and methods for improving the expression / functional response of olfactory receptors are described herein. Genetically modified cells and methods can generally modulate the levels of chaperone proteins that help target receptors to the cell membrane. Genetically modified cells and methods can also provide a platform for use in studying the function of a broader group of chemosensory receptors, including taste receptors and TRP channels.

Provided herein are methods and host cells for producing a polypeptide containing two chains, such as an antibody, half-antibody, antibody fragment, or one-armed antibody. The methods and host cells allow for two-chain polypeptide production using expression of polynucleotides encoding the polypeptide chains from extra-chromosomal polynucleotide(s), and expression of one or more chaperone protein(s) (e.g., peptidyl-prolyl isomerases and / or protein disulfide oxidoreductases) from the host cell chromosome using non-native combination(s) of promoters and translational units encoding a chaperone protein.

This invention belongs to the field of nanobiomedicine technology, specifically relating to a mitochondrial-targeting copper-based nanoparticle (Qu@Cu-SS31) and its application in the preparation of drugs for treating myocardial infarction. The nanoparticles consist of quercetin (Que) and copper ions (Cu²⁺). + The nanoparticles, consisting of a self-assembly of the mitochondrial-targeting peptide SS31, exhibit a uniform, near-spherical morphology with an average particle size of 17.2 ± 1.6 nm. These nanoparticles specifically target cardiomyocyte mitochondria, responsively releasing Cu²⁺. + Furthermore, Qu@Cu-SS31 restores cardiomyocyte copper homeostasis by downregulating the copper metabolism negative regulator COMMD1, the copper uptake protein CTR1, and the copper chaperone protein CCS. Based on this, Qu@Cu-SS31 exhibits remarkable SOD-like and CAT-like enzyme activities, efficiently scavenging various reactive oxygen species / reactive nitrogen species and significantly reducing oxidative stress. Simultaneously, it inhibits NLRP3 inflammasome activation and Caspase-1-mediated pyroptosis, regulates the Bcl-2 / Bax balance to inhibit apoptosis, and promotes vascular endothelial growth factor expression and angiogenesis.

The invention discloses an engineering bacterium capable of efficiently secreting an anti-inflammatory nano antibody as well as a construction method and application of the engineering bacterium, and belongs to the technical field of genetic engineering. A secretory peptide coding gene obtained through site-specific mutagenesis is connected to the N end of a coding gene of the anti-inflammatory nano-antibody, a coding gene of dissolution-promoting tag protein is connected to the C end of the coding gene of the anti-inflammatory nano-antibody, a recombinant gene is obtained, the recombinant gene and the coding gene of chaperonin SecB are integrated into a carrier plasmid, and a recombinant plasmid capable of efficiently secreting the anti-inflammatory nano-antibody is obtained. And transferring the recombinant plasmid into escherichia coli to obtain the engineering bacterium capable of efficiently secreting the anti-inflammatory nano antibody. Through an overall optimization strategy of efficiently secreting the anti-inflammatory nano antibody by the engineering bacteria, the protein efficiency of the engineering bacteria can be greatly improved, and the optimization strategy can be expanded to optimization of the protein secretion efficiency of other engineering bacteria and has universality.