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In vitro properties of hordeivirus TGB1 protein forming ribonucleoprotein complexesстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 27 января 2016 г.
- Авторы: Makarov V.V., Makarova S.S., Makhotenko A.V., Obraztsova E.A., Kalinina N.O.
- Журнал: Journal of General Virology
- Том: 96
- Номер: 10
- Год издания: 2015
- Издательство: Society for General Microbiology
- Местоположение издательства: United Kingdom
- Первая страница: 3422
- Последняя страница: 3431
- DOI: 10.1099/jgv.0.000252
- Аннотация: Hordeivirus movement protein encoded by the first gene of the triple gene block (TGB1 protein, TGBp1) interacts in vivo with viral genomic and subgenomic RNAs to form ribonucleoprotein (RNP) particles that are considered to be a form of viral genome (non-virion transport form) capable of cell-to-cell and long-distance transport in infected plants. The structures of these RNPs have not been elucidated. The poa semilatent virus (PSLV) TGBp1 contains a structured C-terminal NTPase/helicase domain (HELD) and an N-terminal extension region consisting of two domains - a completely intrinsically disordered extreme N-terminal domain (NTD) and an internal domain (ID) with structure resembling a partially disordered molten globule. Here we characterize the structures assembled in vitro by the full-length PSLV TGBp1 alone or in the presence of viral RNA. The PSLV TGBp1 is capable of multimerization and self-assembly into extended high molecular weight complexes. These complexes disassemble to apparent monomers upon incubation with ATP. Upon incubation with viral RNA, the PSLV TGBp1 in vitro forms RNP structures that appear as filamentous particles resembling virions of helical filamentous plant viruses in morphology and dimensions. By comparing the biophysical characteristics of PSLV TGBp1 and its domains in the presence and absence of RNA, we show that the internal domain (ID) plays the main structural role in the self-interactions and RNA interactions of TGBp1 leading to the assembly of virus-like RNP particles.
- Добавил в систему: Макаров Валентин Владимирович