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Journal archive > 2007 > N 1 January-February

COMPLEX FORMATION BETWEEN RECOMBINANT POTATO VIRUS Y PROTEIN VPg
AND HETEROLOGOUS EUKARYOTIC TRANSLATION INITIATION FACTORS eIF4E

L. I. Strokovskaya1, R. Grzela2, J.?Chroboczek3, I. M. Kikhno1, L.?I.?Chaschina1, A. P. Solomko1

1Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kyiv;
e-mail: This email address is being protected from spambots. You need JavaScript enabled to view it.;
2Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw;
3Institute of Structure Biology, Grenoble, France

Genomes of some positive-strand RNA viruses do not contain cap-structure, but instead their 5?-end is covalently linked to a viral protein called VPg. Complex formation between VPg and cellular translation initiation factors (eIFs) has been extensively studied in the context of the model of this complex involvement in virus mRNA translation initiation and cellular protein translation shut down in infected cells. The potato virus (PVY) VPg was expressed in bacterial and baculovirus systems in order to investigate its binding capacity to wheat eIF4E and its isoform. Both purified recombinant eIF4E and eIF(iso)4E were identified in vitro as binding partners of the purified recombinant VPg by using affinity chromatography, as well in vivo by coexpressing of recombinant VPg and eIFs in insect cells with following complex purification using­ affinity chromatography. Besides it was shown that PVY VPg also formed a complex with endogenous insect eIF4E in vivo. PVY VPg interac­tion with eIF4E of wheat (non permissive plant for PVY), and also with so evolutionary distant partner as insect eIF4E suggests the conservation of general structural features of eIF4E implicated in the formation of the complex with VPg.

Key words: protein-protein interaction, plant viruses, eIF4E, VPg.

The original article in Russian is available for download in PDF format.

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