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A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-beta and the viral helicase, NS3.
2001 (English)In: Journal of General Virology, ISSN 0022-1317, E-ISSN 1465-2099, Vol. 82, no 4, 735-745 p.Article in journal (Refereed) Published
Abstract [en]

The dengue virus RNA-dependent RNA polymerase, NS5, and the protease/helicase, NS3, are multidomain proteins that have been shown to interact both in vivo and in vitro. A hyperphosphorylated form of NS5 that does not interact with NS3 has been detected in the nuclei of virus-infected cells, presumably as the result of the action of a functional nuclear localization sequence within the interdomain region of NS5 (residues 369-405). In this study, it is shown by using the yeast two-hybrid system that the C-terminal region of NS3 (residues 303-618) interacts with the N-terminal region of NS5 (residues 320-368). Further, it is shown that this same region of NS5 is also recognized by the cellular nuclear import receptor importin-beta. The interaction between NS5 and importin-beta and competition by NS3 with the latter for the same binding site on NS5 were confirmed by pull-down assays. The direct interaction of importin-beta with NS5 has implications for the mechanism by which this normally cytoplasmic protein may be targetted to the nucleus.

Place, publisher, year, edition, pages
2001. Vol. 82, no 4, 735-745 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:sh:diva-6069DOI: 10.1099/0022-1317-82-4-735PubMedID: 11257177OAI: oai:DiVA.org:sh-6069DiVA: diva2:395570
Available from: 2011-02-07 Created: 2011-02-07 Last updated: 2017-07-20Bibliographically approved

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Citation style
  • apa
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  • Other locale
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