An electron microscope study of the proteins attached to polio virus RNA and its replicative form (RF)
- Creators
- Wu, Madeline
- Davidson, Norman
- Wimmer, Eckard
Abstract
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.
Additional Information
Copyright © 1978 Oxford University Press. Received August 25, 1978. We learned, after initiating this work, that electron microscopic labeling studies of the protein(s) attached to polio RF were independently being carried out by Dr. Jerry Manning and collaborators. Their results will be reported independently. We thank Dr. Timothy J.R. Harris and Nancy Reich for providing us with the poliovirus RNS's. This research has been supported by grants GM 20927 (ND), GM 10991 (ND), and AI 15122 (EW) from the United States Public Health Service and grant BMS 75-05378 (EW) from the NSF.Files
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Additional details
- Eprint ID
- 4056
- Resolver ID
- CaltechAUTHORS:WUMnar78b
- Created
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2006-07-26Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field