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Vol 46(2012) N 2 p. 270-278;
B.V. Syomin1,2*, O.G. Leonova1, T.A. Trendeleva3, R.A. Zvyagilskaya3, Y.V. Ilyin2, V.I. Popenko2

Effect of Nucleocapsid on Multimerization of gypsy Structural Protein GAG

1Kovalenko All-Russian Institute of Experimental Veterinary Medicine, Moscow 109391 Russia
2Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991 Russia
3Bach Institute of Biochemistry, Russian Academy of Sciences, 119071 Moscow Russia

*bsyomin@yandex.ru
Received - 2011-06-09; Accepted - 2011-09-08

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.

gypsy, retrovirus, retrotransposon, virus-like particle, structural protein, Gag, bacterial system of expression



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