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Published on: July 28, 2016
The internal domain of hordeivirus movement protein TGB1 forms in vitro filamentous structures
V V Makarov1, E A Obraztsova, A G Solovyev
1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Russia.
Abstract:
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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