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rdf:type |
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lifeskim:mentions |
umls-concept:C0011311,
umls-concept:C0033684,
umls-concept:C0205147,
umls-concept:C0205245,
umls-concept:C0292147,
umls-concept:C0299508,
umls-concept:C0521026,
umls-concept:C0525021,
umls-concept:C0920283,
umls-concept:C1145667,
umls-concept:C1549781,
umls-concept:C1860991,
umls-concept:C1969057,
umls-concept:C2003941
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pubmed:issue |
39
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pubmed:dateCreated |
2002-9-23
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/NS3 protein, flavivirus,
http://linkedlifedata.com/resource/pubmed/chemical/NS5 protein, flavivirus,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/beta Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36399-407
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12105224-Amino Acid Sequence,
pubmed-meshheading:12105224-Animals,
pubmed-meshheading:12105224-Binding Sites,
pubmed-meshheading:12105224-Carcinoma, Hepatocellular,
pubmed-meshheading:12105224-Cell Nucleus,
pubmed-meshheading:12105224-Dengue Virus,
pubmed-meshheading:12105224-Dimerization,
pubmed-meshheading:12105224-Dose-Response Relationship, Drug,
pubmed-meshheading:12105224-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:12105224-Fluorescent Dyes,
pubmed-meshheading:12105224-Glutathione Transferase,
pubmed-meshheading:12105224-Kinetics,
pubmed-meshheading:12105224-Microscopy, Fluorescence,
pubmed-meshheading:12105224-Models, Molecular,
pubmed-meshheading:12105224-Molecular Sequence Data,
pubmed-meshheading:12105224-Mutagenesis, Site-Directed,
pubmed-meshheading:12105224-Nuclear Localization Signals,
pubmed-meshheading:12105224-Plasmids,
pubmed-meshheading:12105224-Point Mutation,
pubmed-meshheading:12105224-Protein Binding,
pubmed-meshheading:12105224-Protein Structure, Tertiary,
pubmed-meshheading:12105224-RNA Helicases,
pubmed-meshheading:12105224-Rats,
pubmed-meshheading:12105224-Recombinant Fusion Proteins,
pubmed-meshheading:12105224-Sequence Homology, Amino Acid,
pubmed-meshheading:12105224-Serine Endopeptidases,
pubmed-meshheading:12105224-Time Factors,
pubmed-meshheading:12105224-Tumor Cells, Cultured,
pubmed-meshheading:12105224-Two-Hybrid System Techniques,
pubmed-meshheading:12105224-Viral Nonstructural Proteins,
pubmed-meshheading:12105224-alpha Karyopherins,
pubmed-meshheading:12105224-beta Karyopherins,
pubmed-meshheading:12105224-beta-Galactosidase
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pubmed:year |
2002
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pubmed:articleTitle |
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.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, James Cook University, Queensland 4811, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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