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The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin beta 1 and importin alpha/beta-recognized nuclear localization signals.
James Cook University.
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2002 (Engelska)Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, nr 39, s. 36399-36407Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Dengue virus NS5 protein is a multifunctional RNA-dependent RNA polymerase that is essential for virus replication. We have shown previously that the 37- amino acid interdomain spacer sequence (residues (369)X(2)KKX(14)KKKX(11)RKX(3)405) of Dengue2 NS5 contains a functional nuclear localization signal (NLS). In this study, beta-galactosidase fusion proteins carrying point mutations of the positively charged residues or truncations of the interdomain linker region (residues 369-389 or residues 386-405) were analyzed for nuclear import and importin binding activities to show that the N-terminal part of the linker region (residues 369-389, a/bNLS) is critical for nuclear localization and is recognized with high affinity by the conventional NLS-binding importin alpha/beta heterodimeric nuclear import receptor. We also show that the importin beta-binding site (residues 320-368, bNLS) adjacent to the a/bNLS, previously identified by yeast two-hybrid analysis, is functional as an NLS, recognized with high affinity by importin beta, and able to target beta-galactosidase to the nucleus. Intriguingly, the bNLS is highly conserved among Dengue and related flaviviruses, implying a general role for the region and importin beta in the infectious cycle.

Ort, förlag, år, upplaga, sidor
2002. Vol. 277, nr 39, s. 36399-36407
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Medicin och hälsovetenskap
Identifikatorer
URN: urn:nbn:se:sh:diva-6067DOI: 10.1074/jbc.M204977200ISI: 000178275100080PubMedID: 12105224OAI: oai:DiVA.org:sh-6067DiVA, id: diva2:395562
Tillgänglig från: 2011-02-07 Skapad: 2011-02-07 Senast uppdaterad: 2017-12-11Bibliografiskt granskad

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