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The Internal Domain of Hordeivirus Movement Protein TGB1 Forms in vitro Filamentous Structures

V. V. Makarov1, E. A. Obraztsova2, A. G. Solovyev1,3, S. Yu. Morozov1,4, M. E. Taliansky5, I. V. Yaminsky2, and N. O. Kalinina1*

1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-3181; E-mail: kalinina@genebee.msu.ru

2Physical Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-1009; E-mail: yaminsky@nanoscopy.net

3Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, 127550 Moscow, Russia; fax: (495) 977-0947; E-mail: solovyev@genebee.msu.ru

4Biological Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-4309; E-mail: morozov@genebee.msu.ru

5Scottish Crop Research Institute, Invergowrie, Dundee, DD2 5DA, Scotland, UK; fax: +(44138) 2562-426; E-mail: Michael.Taliansky@scri.ac.uk

* To whom correspondence should be addressed.

Received September 18, 2009; Revision received December 9, 2009
The 63 kDa hordeivirus movement protein TGB1 of poa semilatent virus (the PSLV TGB1 protein) forms viral ribonucleoprotein for virus transport within a plant. It was found using the dynamic laser light scattering technique that the internal domain of TGB1 protein forms in vitro high molecular weight complexes. According to results of atomic force microscopy, a part of these complexes is represented by globules of different sizes, while another part consists of extended filamentous structures. Similar properties are also characteristic of the N-terminal half of the protein and are obviously due to its internal domain moiety. The data support the hypothesis that upon viral ribonucleoprotein complex formation, the N-terminal half of the PSLV TGB1 protein plays a structural role and exhibits the ability to form multimeric filamentous structures (the ability for self-assembly).
KEY WORDS: hordeivirus, TGB1 movement protein, internal domain, filamentous structures

DOI: 10.1134/S0006297910060106