Effect of nucleocapsid on multimerization of gypsy structural protein GAG

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 p...

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Bibliographic Details
Published in:Molecular biology (New York) 2012-04, Vol.46 (2), p.270-278
Main Authors: Syomin, B. V., Leonova, O. G., Trendeleva, T. A., Zvyagilskaya, R. A., Ilyin, Yu. V., Popenko, V. I.
Format: Article
Language:English
Subjects:
Amino acids
Biochemistry
Biomedical and Life Sciences
Human Genetics
Insects
Life Sciences
Molecular biology
Molecular Biology of the Cell
Proteins
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Summary: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.
ISSN:0026-8933
1608-3245
DOI:10.1134/S0026893312020148