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

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V. V. Makarov¹, E. A. Obraztsova², A. G. Solovyev^1,3, S. Yu. Morozov^1,4, M. E. Taliansky⁵, I. V. Yaminsky², and N. O. Kalinina^1*

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

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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).

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KEY WORDS: hordeivirus, TGB1 movement protein, internal domain, filamentous structures

DOI: 10.1134/S0006297910060106

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