Supramolecular Complexes of the Agrobacterium tumefaciens Virulence Protein VirE2

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I. V. Volokhina¹, Yu. S. Gusev¹, S. I. Mazilov², and M. I. Chumakov^1,2*

¹Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, pr. Entuziastov 13, 410049 Saratov, Russia; fax: (452) 970-383; E-mail: chumakov@ibppm.sgu.ru

²Faculty of Nonlinear Processes, Chernyshevskii Saratov State University, ul. Astrakhanskaya 83, 410012 Saratov, Russia; fax: (452) 514-540

^* To whom correspondence should be addressed.

Received April 6, 2011; Revision received June 10, 2011

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Virulence protein VirE2 from Agrobacterium tumefaciens is involved in plant infection by transferring a fragment of agrobacterial Ti plasmid ssT-DNA in complex with VirE2-VirD2 proteins into the plant cell nucleus. The VirE2 protein interactions with ssDNA and formation of VirE2 protein complexes in vitro and in silico have been studied. Using dynamic light scattering we found that purified recombinant protein VirE2 exists in buffer solution in the form of complexes of 2-4 protein molecules of 12-18 nm size. We used computer methods to design models of complexes consisting of two and four individual VirE2 proteins, and their dimensions were estimated. Dimensions of VirE2 complexes with ssDNA (550 and 700 nucleotide residues) were determined using transmission electron microscopy and dynamic light scattering. We found that in vitro, upon interaction with ssDNA recombinant protein, VirE2 is able to alter conformation of the latter by shortening the initial length of the ssDNA.

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KEY WORDS: Agrobacterium tumefaciens, virulence protein VirE2, supramolecular complexes, T-DNA, pores, bioinformatics

DOI: 10.1134/S0006297911110095

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