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. 1974 Jan;13(1):107–112. doi: 10.1128/jvi.13.1.107-112.1974

Sendai Virion Transcriptase Complex: Polypeptide Composition and Inhibition by Virion Envelope Proteins

Preston A Marx 1, Allen Portner 1, D W Kingsbury 1
PMCID: PMC355265  PMID: 4359418

Abstract

Sendai virions, disrupted in 2% Triton X-100 in 1 M KCl, were separated into nucleocapsids and envelope proteins by centrifugation. The nucleocapsids, representing 46% of the virion proteins, had a buoyant density of 1.29 gm/cm3 in D2O sucrose. RNA-dependent transcriptase activity associated with them had a ninefold greater specific activity than transcriptase assayed in unfractionated detergent-disrupted virions. These enzyme-active nucleocapsids contained only two polypeptides, the largest virion polypeptide (molecular weight 75,000) and the nucleocapsid structure unit (molecular weight 60,000). Virion envelope proteins, either glycoproteins or nonglycosylated matrix protein, inhibited nucleocapsid-associated polymerase activity; brief heat denaturation abolished their inhibitory activity. Yeast RNA stimulated nucleocapsid-associated enzyme, suggesting that stimulatory polyanions act at the enzyme-template level.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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