The immobilized movement proteins of two tobamoviruses form stable ribonucleoprotein complexes with full-length viral genomic RNA

FEBS Letters
K I IvanovJ C Atabekov

Abstract

The movement proteins of two tobamoviruses (tobacco mosaic virus, TMV, common strain U1 and cruciferous TMV strain) containing amino-terminal hexahistidine affinity tags were overexpressed in Escherichia coli and purified by metal chelate affinity chromatography. Purified recombinant proteins were immobilized to a Ni(2+)-chelate adsorbent and their ability to interact with full-length genomic TMV RNA was tested. Here we report that binding of viral RNA to hexahistidine fusion movement proteins results in the formation of stable ribonucleoprotein complexes.

References

Apr 17, 1992·Cell·C M DeomR N Beachy
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Mar 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·V CitovskyP Zambryski

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Citations

Sep 23, 1998·The Plant Journal : for Cell and Molecular Biology·T W KahnR N Beachy
Apr 15, 2005·Molecular Plant-microbe Interactions : MPMI·Jeanmarie Verchot-Lubicz
May 1, 2003·Molecular Plant Pathology·Ulrich Melcher
Jan 21, 2001·The Journal of Biological Chemistry·K I IvanovK Mäkinen

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