74 results about "Leucine zipper" patented technology

A dimeric protein comprising a first fusion protein and a second fusion protein, wherein the first fusion protein comprises a targeting domain, a leucine zipper domain, and an antigen; and wherein the second fusion protein comprises a targeting domain, a leucine zipper domain, and optionally an antigen. Nucleic acid vectors encoding proteins of the invention are provided, particularly for use in nucleic acid vaccination.

A new transcription factor coding gene induced by water deficit or abscisic acid of Helianthus annuus, having a homeodomain associated to a leucine zipper, was characterized. The transcription factor is useful to be cloned in DNA constructions for transforming host cells and plants. The transgenic plants comprising the transcription factor gene are tolerant and resistant to harmful environmental conditions such as water stress and high salinity. A nucleic acid promoting sequence is also provided wherein the sequence is induced by water deficit or abscisic acid. Constructions, host cells and transgenic plants that comprise the transcription factor gene are provided.

The present invention relates to compounds, compositions, and methods for the study, diagnosis, and treatment of traits, diseases and conditions that respond to the modulation of Bach1 gene expression and / or activity, and / or modulate a Bach1 gene expression pathway. Specifically, the invention relates to double-stranded nucleic acid molecules including small nucleic acid molecules, such as short interfering nucleic acid (siNA), short interfering RNA (siRNA), double-stranded RNA (dsRNA), micro-RNA (miRNA), and short hairpin RNA (shRNA) molecules that are capable of mediating or that mediate RNA interference (RNAi) against Bach1 gene expression.

The invention discloses a novel coronavirus S protein receptor binding domain fusion protein containing an oligomerization structural domain and application of the novel coronavirus S protein receptor binding domain fusion protein, and particularly discloses a novel coronavirus S protein RBD fusion protein which is composed of at least one copy of RBD polypeptide derived from a novel coronavirus S protein, the oligomerization structural domain and / or an endogenous adjuvant, the endogenous adjuvant is an RS09 adjuvant, and the oligomerization structural domain is selected from a bacteriophage trimerization structural domain (Foldon domain), a GCN4 leucine zipper sequence or a human collagen trimerization structural domain. The novel coronavirus RBD fusion protein can be used for preparing vaccines for preventing novel coronavirus infection and infection-induced diseases.

The present invention relates generally to the field of molecular biology and concerns a method for improving plant growth characteristics relative to corresponding wild type plants. More specifically, the present invention concerns a method for improving plant growth characteristics comprising modulating expression in a plant of a nucleic acid encoding a class I homeodomain leucine zipper (HDZip) hox5 polypeptide or a homologue thereof; or comprising modulating expression in a plant of a nucleic acid encoding a nitrate transporter protein (NRT) or a homologue thereof; or comprising modulating expression in a plant of a nucleic acid encoding a polypeptide denoted Yield Enhancing Protein 16 (YEP16); or comprising modulating expression in a plant of a Group I glycogen synthase kinase (Group I shaggy-like kinase) or a homologue thereof. The present invention also concerns plants having modulated expression of a nucleic acid encoding a class I HDZip hox5 polypeptide or a homologue thereof; or having modulated expression of a nucleic acid encoding a NRT protein or a homologue thereof; or having modulated expression of a nucleic acid encoding a polypeptide denoted YEP16; or having modulated expression of a Group I shaggy-like kinase or a homologue thereof, which plants have improved growth characteristics relative to corresponding wild type plants. The invention also provides constructs useful in the methods of the invention.

The present invention describes a rapid and efficient in vivo library-versus-library screening strategy for identifying optimally interacting pairs of heterodimerizing polypeptides. It allows for the screening of a protein library against a second protein library, rather than against a single bait protein, and thus has numerous applications in the study of protein-protein interactions. Additionally, it allows for the application of different selection stringencies. Two leucine zipper libraries, semi-randomized at the positions adjacent to the hydrophobic core, were genetically fused to either one of two designed fragments of the enzyme murine dihydrofolate reductase (mDHFR), and cotransformed into E. coli. Interaction between the library polypeptides was required for reconstitution of the enzymatic activity of mDHFR, allowing bacterial growth. Analysis of the resulting colonies revealed important biases in the zipper sequences relative to the original libraries, which are consistent with selection for stable, heterodimerizing pairs. Using more weakly associating mDHFR fragments, we increased the stringency of selection. We enriched the best performing leucine zipper pairs by multiple passaging of the pooled, selected colonies in liquid culture, as the best pairs allowed for better bacterial propagation. This competitive growth allowed small differences among the pairs to be amplified, and different sequence positions were enriched at different rates. We applied these selection processes to a library-versus-library sample of 2.0×106 combinations, and selected a novel leucine zipper pair which may be appropriate for use in further in vivo heterodimerization strategies.

This invention relates to the biotechnology area, and provides a kind of TRAIL chimeric protein, DNA sequence encoding this chimeric protein, vectors comprising this DNA, host cells or transgenic animals that contain one of the vectors, and preparation methods for the said chimeric protein and its applications. The said TRAIL fusion protein from the N to C terminal comprises human leucine zipper sequence, human TRAIL protein, human TRAIL extracellular domain or a fragment thereof. The chimeric protein has significantly enhanced stability, prolonged half-life in animals, increased efficacy and thus has broad application future.