THE IMMOBILIZED MOVEMENT PROTEINS OF 2 TOBAMOVIRUSES FORM STABLE RIBONUCLEOPROTEIN COMPLEXES WITH FULL-LENGTH VIRAL GENOMIC RNA

The movement proteins of two tobamoviruses (tobacco mosaic virus, TMV, common strain U1 and cruciferous TMV strain) containing aminoterminal hexahistidine affinity tags were overexpressed in Escherichia coli an d purified by metal chelate affinity chromatography. Purified recombin ant proteins were immobilized to a Ni2+-chelate adsorbent and their ab ility to interact with full-length genomic TMV RNA was tested, Here we report that binding of viral RNA to hexahistidine fusion movement pro teins results in the formation of stable ribonucleoprotein complexes.