Regulation of RNA translation in potato virus X RNA-coat protein complexes: The key role of the N-terminal segment of the ... View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2006-07

AUTHORS

O. V. Karpova, M. V. Arkhipenko, O. V. Zayakina, N. A. Nikitin, O. I. Kiselyova, S. V. Kozlovsky, N. P. Rodionova, J. G. Atabekov

ABSTRACT

The efficiency of in vitro translation of the potato virus X (PVX) RNA was studied for viral ribonucleoprotein complexes (vRNP) assembled from the genomic RNA and the viral coat protein (CP). In vRNP particles the 5′-proximal RNA segments were encapsidated into the CP, which formed helical headlike structures differing in length. Translation of the PVX RNA was completely suppressed upon incubation with PVX CP and was activated within vRNPs assembled in vitro with two CP forms, differing in the modification of the N-terminal peptide containing the main phosphorylation site(s) for Thr/Ser protein kinases. It was shown that CP phosphorylation activates RNA translation within vRNPs and that the removal of the N-terminal peptide of CP suppresses activation, but CP still acts as a translational suppressor. This fact made it possible to suppose that the replacement of Ser/Thr by amino acid residues that are not subject to phosphorylation in the N-terminal peptide of CP of the mutant PVX (PVX-ST) completely inhibits RNA translation within vRNP. However, experiments disproved this assumption: PVX-ST RNA was efficiently translated within native virions, RNA of the wild-type (wt) PVX was efficiently translated in heterogeneous vRNP (wtRNA + PVX-ST CP), and the opposite result (repression of translation) was obtained for another heterogeneous vRNP (PVX-ST RNA + wtCP). Therefore, the N-terminal CP peptide located on the surface of the PVX virion or vRNP particles plays a key role in the activation of viral RNA translation. More... »

PAGES

628-634

Journal

TITLE

Molecular Biology

ISSUE

4

VOLUME

40

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0026893306040157

DOI

http://dx.doi.org/10.1134/s0026893306040157

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011786243


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