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

Brooks, Andrew J., Johansson, Magnus, John, Anna V., Xu, Yibin, Jans, David A. and Vasudevan, Subhash G. (2002) 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. Journal of Biological Chemistry, 277 39: 36399-36407. doi:10.1074/jbc.M204977200

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Author Brooks, Andrew J.
Johansson, Magnus
John, Anna V.
Xu, Yibin
Jans, David A.
Vasudevan, Subhash G.
Title 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
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2002-01-01
Sub-type Article (original research)
DOI 10.1074/jbc.M204977200
Open Access Status File (Publisher version)
Volume 277
Issue 39
Start page 36399
End page 36407
Total pages 9
Place of publication Bethesda, MD
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Subject 060506 Virology
060108 Protein Trafficking
060111 Signal Transduction
110804 Medical Virology
Abstract 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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Sat, 31 Jan 2009, 00:25:59 EST by Sophie Jordan on behalf of Institute for Molecular Bioscience