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Updated: Mar 19, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
Data on structural transitions in domains of hordeivirus TGB1 protein forming ribonucleoprotein complex
Valentin V Makarov1, Svetlana S Makarova2, Natalia O Kalinina1
1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninsky Gory, Moscow 119992, Russia.
Abstract:
This data article is related to the research article entitled "in vitro properties of hordeivirus TGB1 protein forming ribonucleoprotein complexes" (Makarov et al., 2015 [1]), demonstrating that upon incubation with viral RNA the poa semilatent hordeivirus (PSLV) TGB1 protein (the movement 63 K protein encoded by the first gene of the triple gene block) in vitro forms RNP structures resembling filamentous virus-like particles and its internal domain (ID) performs a major structural role in this process. This article reports the additional results on the structural lability of ID and the structural transitions in the C-terminal NTPase/helicase domain (HELD) induced by interaction with tRNA and phosphorylation.
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