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Nucleic Acids Research, 1978, Vol. 5, No. 12 4711-4724
© 1978

Articles

An electron microscope study of the proteins attached to polio virus RNA and its replicative form (RF)

Madeline Wu*, Norman Davidson* and Eckard Wimmer**

*Department of Chemistry, California Institute of Technology Pasadena, CA 91125 **Department of Microbiology, School of Basic Health Sciences, State University of New York at Stony Brook Stony Brook, Long Island, NY 11794, USA

Received August 25, 1978. A recently described method (Wu, M. and Davidson, N. (1978), Nucleic Acids Research 5, in press) for visualizing proteins attached to nucleic acids in the electron microscope has been applied to study proteins attached to poliovirion RNA and to the viral double-stranded intracellular RE form. A protein is found at the 5' end of the plus strand virion RNA, and protein components are found at both ends of the duplex RF. In the RF as usually extracted, there is frequently a larger or compound protein aggregate at the end which contains the 3' end of the plus strand and the 5' end of the minus strand. Banding in CsCl-guanidinium hydrochloride in the presence of sarkosyl causes dissociation of some components of this aggregate, leaving both ends labeled with the covalently bound VPg. These results confirm and extend previous biochemical studies of proteins bound to poliovirion RNA and to the RE form.


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O. C. Richards and E. Ehrenfeld
Effects of Poliovirus 3AB Protein on 3D Polymerase-catalyzed Reaction
J. Biol. Chem., May 22, 1998; 273(21): 12832 - 12840.
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