Abstract
Cell-to-cell and long-distance transport of some plant viruses requires coordinated action of three movement proteins encoded by triple gene block (TGB). The largest of TGB proteins, TGBp1, is a member of the superfamily I of DNA/RNA helicases and possesses a set of conserved helicase sequence motifs necessary for virus movement. A recombinant His-tagged form of TGBp1 of two hordeiviruses and potato virus X, a potexvirus, produced in Escherichia coli had unwinding activity on a partially duplexed RNA, but not DNA substrate. The helicase activity of these proteins was dependent on Mg2+ and ATP. The isolated C-terminal half of the PSLV TGBp1 retaining all helicase motifs was also able to unwind RNA duplex.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Amino Acid Sequence
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DNA / metabolism
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Genes, Viral / physiology
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Molecular Sequence Data
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Mosaic Viruses / enzymology*
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Mosaic Viruses / genetics
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Plant Viral Movement Proteins
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Plant Viruses / enzymology
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Plant Viruses / genetics
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Potexvirus / enzymology
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Potexvirus / genetics
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RNA Helicases / genetics
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RNA Helicases / metabolism*
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RNA Viruses / enzymology*
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RNA Viruses / genetics
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RNA, Double-Stranded / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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Plant Viral Movement Proteins
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RNA, Double-Stranded
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Recombinant Fusion Proteins
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Viral Proteins
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DNA
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TGBp1 protein, Poa semilatent virus
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Adenosine Triphosphatases
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RNA Helicases