The internal domain of hordeivirus movement protein TGB1 forms in vitro filamentous structures.
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).
Makarov
V V
VV
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Russia.
Obraztsova
E A
EA
Solovyev
A G
AG
Morozov
S Yu
SY
Taliansky
M E
ME
Yaminsky
I V
IV
Kalinina
N O
NO
D018625:Microscopy, Atomic Force; D053830:Plant Viral Movement Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010942:Plant Viruses / Q000378:metabolism; D031785:Poa / Q000821:virology; D017434:Protein Structure, Tertiary; D012367:RNA, Viral / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D053830:Plant Viral Movement Proteins; D012367:RNA, Viral; D011994:Recombinant Proteins