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The influenza viral genome is composed of eight ribonucleoprotein particles formed by a complex of negative-sense RNA bound to a viral nucleoprotein. Each RNP carries with it an RNA polymerase complex. When the nucleoprotein binds to the viral RNA, it is able to expose the nucleotide bases which allow the viral polymerase to transcribe RNA. At ...
These vaccines functioned by either expressing the rabies virus internal structural nucleoprotein (RCN-N) or by expressing the rabies virus glycoprotein (RCN-G). [ 11 ] RCN, and all poxviridae viruses, are especially useful in creating vaccines because they create cost-effective, stable, multivalent vaccines that are easy to manufacture, and ...
In the cytoplasm, ribosomal RNA and protein combine to form a nucleoprotein called a ribosome. The ribosome binds mRNA and carries out protein synthesis. Several ribosomes may be attached to a single mRNA at any time. [27] Nearly all the RNA found in a typical eukaryotic cell is rRNA. Transfer-messenger RNA (tmRNA) is found in many bacteria and ...
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). [1] The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm.
The nucleocapsid (N) protein is a protein that packages the positive-sense RNA genome of coronaviruses to form ribonucleoprotein structures enclosed within the viral capsid. [2] [3] The N protein is the most highly expressed of the four major coronavirus structural proteins. [2]
The P40 nucleoprotein from BoDV-1 is multi-helical in structure and can be divided into two subdomains, each of which has an alpha-bundle topology. [4] The nucleoprotein assembles into a planar homotetramer, with the RNA genome either wrapping around the outside of the tetramer or possibly fitting within the charged central channel of the tetramer.
Homologous recombination is the proposed mechanism whereby the DNA virus human herpesvirus-6 integrates into human telomeres. [ 92 ] When two or more viruses, each containing lethal genomic damage, infect the same host cell, the virus genomes can often pair with each other and undergo homologous recombinational repair to produce viable progeny.
In humans, RAD51 is a 339-amino acid protein that plays a major role in homologous recombination of DNA during double strand break repair.In this repair process, an ATP-dependent DNA strand exchange takes place in which a template strand invades base-paired strands of homologous DNA molecules.