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PMID: 5288771 Published · ppublish English Journal Article

Structure of the poly(G) polymerase component of the bacteriophage f2 replicase.

Fedoroff NV, Zinder ND

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.

MeSH Terms
Carbon Isotopes Cellulose Centrifugation, Density Gradient Chromatography Chromatography, DEAE-Cellulose Coliphages/analysis,enzymology Electrophoresis Guanosine Triphosphate Nucleic Acid Denaturation Polynucleotides RNA RNA Nucleotidyltransferases/analysis,isolation & purification Ribonucleases/analysis Rifampin/pharmacology Templates, Genetic Tritium Viral Proteins/analysis Virus Replication
Chemicals
Carbon Isotopes Polynucleotides Viral Proteins Tritium RNA Guanosine Triphosphate Cellulose RNA Nucleotidyltransferases Ribonucleases Rifampin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fedoroff N V
Zinder N D
References (24)
24 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1971-08-00
Pages
1838-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389304
Subset
IM
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