[Effect of nucleocapsid on multimerization of gypsy structural protein Gag].
The structural protein (Gag) of the gypsy Drosophila retrovirus lacks matrix, but contains capsid and nucleocapsid domains. The Gag forms virus-like particles in a bacterial cell; besides, its capsid alone is able to form aggregates. However, aggregates assembled from the capsid were variable in size and displayed much less organization than particles formed by the whole Gag. The nucleocapsid exerts influence on the organization and structure of particles, and this function is directed by sequence of amino acid residues at its N-terminus (a nucleocapsid proximal part). The particle assembling occurs in the presence of any RNAs or single stranded DNA oligonucleotides.
B V
BV
Semin
O G
OG
Leonova
T A
TA
Trendeleva
R A
RA
Zviagil'skaia
Iu V
IuV
Il'in
V I
VI
Popenko
D000818:Animals; D002213:Capsid / Q000378:metabolism*; D004331:Drosophila melanogaster; D004926:Escherichia coli / Q000235:genetics; D015683:Gene Products, gag / Q000235:genetics / Q000378:metabolism*; D055503:Protein Multimerization / Q000502:physiology*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012190:Retroviridae / Q000235:genetics / Q000378:metabolism*
D015683:Gene Products, gag; D011994:Recombinant Proteins