Purification and Properties of a Host Cell Protein Required for Poliovirus Replication in Vitro
- Creators
- Baron, Margaret H.
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Baltimore, David
Abstract
A host cell protein required for poliovirus RNA-dependent RNA replicase activity in vitro has been purified several thousand-fold from an uninfected HeLa cell postmitochondrial supernatant. A single protein of apparent Mr = approximately 67,000 daltons and pI 6.3 is associated with this "host factor" activity. Poly(U)-Sepharose chromatography of the template-dependent replicase isolated from poliovirus-infected cells results in the complete loss of replicase activity if a salt gradient is used to develop the column. Host factor elutes early in the salt gradient and restores replicase activity to protein fractions eluted later in the gradient. The host factor, estimated to be present at 50,000-100,000 copies/cell, interacts physically with replicase.
Additional Information
© 1982 American Society for Biochemistry and Molecular Biology. Received for publication, February 2, 1982. This research was supported by grants from the National Institute of Allergy and Infectious Diseases and from the National Cancer Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. Predoctoral scholar of the Insurance Medical Scientist Scholarship Fund and fellow of the Danforth Foundation. American Cancer Society Professor of Microbiology.Additional details
- Eprint ID
- 32500
- Resolver ID
- CaltechAUTHORS:20120717-091213541
- National Institute of Allergy and Infectious Diseases
- National Cancer Institute
- Danforth Foundation
- Created
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2012-07-17Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field