2Physical Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-1009; E-mail: firstname.lastname@example.org
3Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, 127550 Moscow, Russia; fax: (495) 977-0947; E-mail: email@example.com
4Biological Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-4309; E-mail: firstname.lastname@example.org
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