The immobilized movement proteins of two 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 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.
Ivanov
K I
KI
Department of Virology, Moscow State University, Russian Federation.
Ivanov
P A
PA
Timofeeva
E K
EK
Dorokhov
Y L
YL
Atabekov
J G
JG
D000327:Adsorption; D002614:Chelating Agents; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006639:Histidine; D009532:Nickel; D010455:Peptides / Q000235:genetics; D053830:Plant Viral Movement Proteins; D012367:RNA, Viral / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism*; D014027:Tobacco Mosaic Virus / Q000737:chemistry* / Q000235:genetics; D014764:Viral Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D002614:Chelating Agents; D010455:Peptides; D053830:Plant Viral Movement Proteins; D012367:RNA, Viral; D011993:Recombinant Fusion Proteins; D012261:Ribonucleoproteins; D014764:Viral Proteins; C033223:polyhistidine; D006639:Histidine; D009532:Nickel