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Originally published In Press as doi:10.1074/jbc.M204977200 on June 24, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36399-36407, September 27, 2002
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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*

Andrew J. BrooksDagger , Magnus JohanssonDagger , Anna V. John§, Yibin XuDagger , David A. Jans§, and Subhash G. VasudevanDagger ||

From the Dagger  Department of Biochemistry and Molecular Biology, James Cook University, Queensland 4811, § Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, the Australian National University, Canberra, Australian Capital Territory 2601, and the  Department of Biochemistry and Molecular Biology, Box 13D, Monash University, Victoria 3800, Australia

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 369X2KKX14KKKX11RKX3405) 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.


* This work was supported by a grant from the National Health and Medical Research Council of Australia.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, James Cook University, Townsville, Queensland 4811, Australia. Tel.: 61-7-47814233; Fax: 61-7-47816078; E-mail: Subhash.Vasudevan@jcu.edu.au.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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