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. 1971 Aug;68(8):1838–1843. doi: 10.1073/pnas.68.8.1838

Structure of the Poly(G) Polymerase Component of the Bacteriophage f2 Replicase

Nina V Fedoroff 1, Norton D Zinder 1
PMCID: PMC389304  PMID: 5288771

Abstract

A rifampicin-resistant poly(G) polymerase has been purified from f2 sus 11-infected cells. The poly(G) polymerase is believed to represent part of the f2 replicase on the basis of several criteria. It is present only in infected cells and shares the characteristic rifampicin resistance of crude f2 replicase activity. Partially purified poly(G) polymerase preparations exhibit replicase activity, synthesizing f2 “lus”strand RNA from denatured, partially double-stranded f2 RNA template. Highly purified poly(G) polymerase preparations, although lacking replicase activity, contain a protein which is electrophoretically identical to the protein product of the viral replicase cistron.

Keywords: protein subunits

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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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