Patent classifications
C12N9/0069
INTERNAL PROTEIN TAGS
Provided herein are substantially non-luminescent peptide/polypeptide tags that are inserted internally within a protein of interest or between N-terminal and C-terminal peptides/polypeptides. Interaction of the internally-inserted tag with a complement polypeptide/peptide that is also substantially non-luminescent results in the formation a bioluminescent reporter complex.
Recombinant polynucleotide coding for polypeptide comprising reporter moiety, substrate moiety and destabilizing moiety, host cell comprising same and use of same
Provided are a recombinant polynucleotide encoding a polypeptide including a reporter moiety, a substrate moiety, and a destabilization moiety, a host cell including the same, and use thereof to measure the level of a protease by using the recombinant polynucleotide.
MUCONIC ACID-PRODUCING TRANSFORMED MICROORGANISM AND USE THEREOF
The objective of the present invention is to provide a microorganism that makes it possible to produce muconic acid from a lignin-derived aromatic compound with sufficient economic efficiency and without depending on the type of lignin, and a method of producing muconic acid using the microorganism. The objective can be achieved by a transformed microorganism wherein the host microorganism is a microorganism of the genus Pseudomonas that has pcaH gene, pcaG gene, catA gene, and catB gene on its chromosome, and that can assimilate an aromatic compound derived from syringyl lignin; and wherein the transformed microorganism lacks at least one gene selected from the group consisting of pcaH gene and pcaG gene on its chromosome, lacks catB gene on its chromosome, and expresses aroY gene inserted; and a method of producing muconic acid using the transformed microorganism and the like.
GUANIDINE DEGRADATION ENZYME AND METHODS OF USE
Presented herein are Synechococcus strains engineered to express the bacterial ethylene-forming enzyme (EFE) that exhibit unstable ethylene production due to toxicity and genomic instability induced by accumulation of the EFE-byproduct guanidine. Co-expression of EFE and Sll1077 significantly enhanced genomic stability and enabled the resulting Synechococcus strain GD-EFE7942 to achieve sustained high-level ethylene production. The engineered strains and methods disclosed herein are useful for guanidine degradation pathways and for ethylene bioproduction in cyanobacteria.
Herbicide resistance genes
The subject invention provides novel plants that are not only resistant to 2,4-D, but also to pyridyloxyacetate herbicides. Heretofore, there was no expectation or suggestion that a plant with both of these advantageous properties could be produced by the introduction of a single gene. The subject invention also includes plants that produce one or more enzymes of the subject invention “stacked” together with one or more other herbicide resistance genes. The subject invention enables novel combinations of herbicides to be used in new ways. Furthermore, the subject invention provides novel methods of preventing the development of, and controlling, strains of weeds that are resistant to one or more herbicides such as glyphosate. The preferred enzyme and gene for use according to the subject invention are referred to herein as AAD-12 (AryloxyAlkanoate Dioxygenase). This highly novel discovery is the basis of significant herbicide tolerant crop trait and selectable marker opportunities.
Anti-inflammatory peptides and composition comprising the same
A peptide with anti-inflammatory activity, wherein the peptide comprises SEQ ID NO: 1, the peptide has above 80% homology of amino acid sequence with above-mentioned sequence, or the peptide is the fragment of the above-mentioned peptides is described. An anti-inflammatory composition comprising the above mentioned peptides is described. According to the present invention, a peptide comprising a sequence of SEQ ID NO: 1 has outstanding efficacy in both suppressing inflammation and in prophylactic means. Therefore, the composition comprising the peptide of this invention can be used as anti-inflammatory pharmaceutical composition or as cosmetic composition, in turn, treating and preventing a variety of different types of inflammatory diseases.
HPPD variants and methods of use
In the present invention, HPPD polypeptides and plants containing them showing a full tolerance against one or more HPPD inhibitor herbicides belonging to various chemical classes are described. A set of mutant HPPD polypeptides have been designed which have either no or only a significantly reduced affinity to HPPD inhibitor herbicides and, at the same time, the rate of dissociation of the HPPD inhibitors of the mutant HPPD polypeptide is increased to such an extent that the HPPD inhibitors no longer act as slow-binding or slow, tight-binding inhibitors but, instead of this, have become fully reversible inhibitors. In particular, isolated polynucleotides encoding mutant HPPD polypeptides conferring tolerance to HPPD inhibitor herbicides belonging to various chemical classes are provided. Additionally, amino acid sequences corresponding to the polynucleotides are encompassed.
Transformed yeast producing novel 1-octen-3-ol, and preparation method therefor
The present application relates to a method for preparing transformed yeast producing 1-octen-3-ol, and yeast prepared by the method, and is useful in the cosmetic industry and the food development industry which use a Tricholoma matsutake scent.
Quantitative assessment for cap efficiency of messenger RNA
The present invention provides, among other things, methods of quantitating mRNA capping efficiency, particularly for mRNA synthesized in vitro. In some embodiments, the methods comprise chromatographic methods of quantifying capping efficiency and methylation status of the caps.
Internal protein tags
Provided herein are substantially non-luminescent peptide/polypeptide tags that are inserted internally within a protein of interest or between N-terminal and C-terminal peptides/polypeptides. Interaction of the internally-inserted tag with a complement polypeptide/peptide that is also substantially non-luminescent results in the formation a bioluminescent reporter complex.