This disclosure provides an E. coli strain, which lacks thioredoxin reductase activity encoded by trxB and thioredoxin 1 activity encoded by trxA, and glutathione reductase activity encoded by gor. Said E. coli strain expresses a mutated AhpC protein having glutathione reductase activity and a cytosolic prokaryotic disulfide isomerase. The E. coli strain has an oxidative cytosol and can be used to efficiently produce proteins having disulfide bonds.

Metabolic activity is exhibited against a larger number of compounds having different acting properties. A cytochrome P450 gene encodes a protein having an amino acid sequence of any of SEQ ID NOS: 2, 4, 6, and 8.

A genetically modified phototrophic cell for in-vivo production of hydrogen. The phototrophic cell has been genetically modified to the effect that a) at least one of the native photosystem I components has been deleted, b) the native hydrogenase has been deleted, and c) at least one fusion protein is expressed, comprising i. a hydrogenase or hydrogenase component and ii. at least one PSI component, with the proviso that the PSI is complemented by expression of the at least one fusion protein, and the hydrogenase component itself, or together with at least one further hydrogenase component expressibly introduced into the cell, has hydrogenase activity.

The present invention provides isolated FAD2, FAD3, FAB1 and FAE1 genes and FAD2, FAD3, FAB1 and FAE1 protein sequences of Camelina species, e.g., Camelina sativa, mutations in Camelina FAD2, FAD3, FAB1 and FAE1 genes, and methods of using the same. In addition, methods of altering Camelina seed composition and/or improving Camelina seed oil quality are disclosed. Furthermore, methods of breeding Camelina cultivars to produce plants having altered or improved seed oil and/or meal quality are provided.

The present invention provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

An object of the present invention is to provide an evaluation system capable of detecting an extracellular purinergic receptor ligand minimally invasively, chronologically and systemically, and the present invention provides a genetically modified non-human animal expressing a first fusion protein and a second fusion protein for detecting an extracellular purinergic receptor ligand, in which the first fusion protein comprises a membrane protein that binds to a purinergic receptor ligand, and a first reporter protein, and the second fusion protein comprises a protein that binds to the membrane protein bound to the ligand, and a second reporter protein; and a cell thereof.

Microalgal mutant to produce high-value essential LCPUFA oils including eicosadienoic acid (EDA), dihomo-γ-linoleic acid (DGLA), arachidonic acid (ARA), and eicosapentaenoic acid (EPA) in various ratios in are provided.

The present disclosure belongs to the technical field of genetic modification of an enzyme preparation and particularly relates to a preparation method of a high-stability superoxide dismutase with a transmembrane capability. The method includes the following steps: extracting mRNA from Geobacillus stearothermophilus, synthesizing cDNA by a reverse transcription method, amplifying a large number of coding regions of the cDNA by designing a specific primer, ligating the coding regions to an E. coli expression vector, and transforming the coding regions into engineering bacteria BL21 (DE3). A point mutation technology is used to enhance stability of the superoxide dismutase and a flexible polypeptide linker GGGSGGGS (SEQ ID NO: 11) is designed, such that a soluble fusion expression of a transmembrane peptide YGRKKRRQRRR (SEQ ID NO: 10) and the superoxide dismutase is successfully realized.

The invention relates to compositions including polynucleotides encoding polypeptides which have been chemically modified by replacing the uridines with 1-methyl-pseudouridine to improve one or more of the stability and/or clearance in tissues, receptor uptake and/or kinetics, cellular access by the compositions, engagement with translational machinery, mRNA half-life, translation efficiency, immune evasion, protein production capacity, secretion efficiency, accessibility to circulation, protein half-life and/or modulation of a cell's status, function, and/or activity.

A DNA fragment to encode a nitrogen fixation enzyme includes a base sequence of SEQ ID NO:1 or a base sequence having not less than 50% identity with the SEQ ID NO:1.