Structure of the poly(G) polymerase component of the bacteriophage f2 replicase.
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.
D002247:Carbon Isotopes; D002482:Cellulose; D002499:Centrifugation, Density Gradient; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D003090:Coliphages / Q000032:analysis / Q000201:enzymology*; D004586:Electrophoresis; D006160:Guanosine Triphosphate; D009691:Nucleic Acid Denaturation; D011119:Polynucleotides; D012313:RNA; D012316:RNA Nucleotidyltransferases / Q000032:analysis* / Q000302:isolation & purification; D012260:Ribonucleases / Q000032:analysis; D012293:Rifampin / Q000494:pharmacology; D013698:Templates, Genetic; D014316:Tritium; D014764:Viral Proteins / Q000032:analysis; D014779:Virus Replication
D002247:Carbon Isotopes; D011119:Polynucleotides; D014764:Viral Proteins; D014316:Tritium; D012313:RNA; D006160:Guanosine Triphosphate; D002482:Cellulose; D012316:RNA Nucleotidyltransferases; D012260:Ribonucleases; D012293:Rifampin