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Effect of nucleocapsid on multimerization of <Emphasis Type="Italic">gypsy</Emphasis> structural protein GAG
Authors:B V Syomin  O G Leonova  T A Trendeleva  R A Zvyagilskaya  Yu V Ilyin  V I Popenko
Institution:1.Kovalenko All-Russian Institute of Experimental Veterinary Medicine,Moscow,Russia;2.Engelhardt Institute of Molecular Biology,Russian Academy of Sciences,Moscow,Russia;3.Bach Institute of Biochemistry,Russian Academy of Sciences,Moscow,Russia
Abstract:The structural protein (Gag) of Drosophila retrovirus gypsy contains capsid and nucleocapsid domains. Gag forms virus-like particles in a bacterial cell; furthermore, its capsid alone is able to form aggregates. However, aggregates assembled from the capsid vary in size and are less organized than particles formed by a full-length Gag. The nucleocapsid determines the organization and structure of the particles, which is ensured by the amino acid residues at its N-terminal (a nucleocapsid proximal part). The assembly of the particle occurs in the presence of any RNAs or single-stranded DNA oligonucleotides.
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