Mutagenic analysis of potato virus X movement protein (TGBp1) and the coat protein (CP): in vitro TGBp1-CP binding and viral RNA translation activation.

Molecular Plant Pathology
O V ZayakinaJ G Atabekov

Abstract

Previously, we have shown that encapsidated Potato virus X (PVX) RNA was non-translatable in vitro, but could be converted into a translatable form by binding of the PVX movement protein TGBp1 to one end of the virion or by coat protein (CP) phosphorylation. Here, a mutagenic analysis of PVX CP and TGBp1 was used to identify the regions involved in TGBp1-CP binding and translational activation of PVX RNA by TGBp1. It was found that the C-terminal (C-ter) 10/18 amino acids region was not essential for virus-like particle (VP) assembly from CP and RNA. However, the VPs assembled from the CP lacking C-ter 10/18 amino acids were incapable of TGBp1 binding and being translationally activated. It was suggested that the 10-amino-acid C-ter regions of protein subunits located at one end of a polar helical PVX particle contain a domain accessible to TGBp1 binding and PVX remodelling. The non-translatable particles assembled from the C-ter mutant CP could be converted into a translatable form by CP phosphorylation. The TGBp1-CP binding activity was preserved unless a conservative motif IV was removed from TGBp1. By contrast, TGBp1-dependent activation of PVX RNA translation was abolished by deletions of various NTPase/helicase conservati...Continue Reading

References

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Apr 15, 2005·Molecular Plant-microbe Interactions : MPMI·Jeanmarie Verchot-Lubicz
Mar 1, 2003·Molecular Plant Pathology·Jeffrey S BattenCynthia Hemenway

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Citations

Jun 27, 2013·The Journal of Cell Biology·Jens TilsnerKarl J Oparka
Oct 17, 2007·Molekuliarnaia biologiia·E N DobrovA V Efimov
Sep 3, 2011·Virus Research·Matthaios M MathioudakisIoannis C Livieratos
Jun 18, 2016·The Journal of General Virology·A G Solovyev, V V Makarov

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