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

FEBS Letters
K I IvanovJ C Atabekov


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.


Apr 17, 1992·Cell·C M DeomR N Beachy
Jan 1, 1990·Advances in Virus Research·J G Atabekov, M E Taliansky
Jan 1, 1984·Advances in Virus Research·J G Atabekov, Dorokhov YuL
Jan 1, 1980·Bio Systems·J G Atabekov, M E Taliansky
Mar 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·V CitovskyP Zambryski

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Sep 23, 1998·The Plant Journal : for Cell and Molecular Biology·T W KahnR N Beachy
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