RNA polymerase associated with virions of pike fry rhabdovirus.
The association of an RNA-dependent RNA polymerase activity with virions of pike fry rhabdovirus has been demonstrated by both in vitro and in vivo studies. The temperature optimum for the in vitro assay is around 20 C, although enzyme activity can be observed at 4 C. Preparations of pike fry virus possess a glycoprotein, a membrane protein, a nucleoprotein, an L protein, and a phosphoprotein, as well as an RNA of about 3.8 times 10-6 mol wt. A protein kinase activity has been found associated with virus preparations. In vitro RNA product analyses indicate that the virus-associated enzyme functions principally as a transcriptase synthesizing viral-complementary, heteropolymeric RNA.
D000818:Animals; D002460:Cell Line; D002474:Cell-Free System; D006224:Cricetinae; D003530:Cyprinidae; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes / Q000382:microbiology*; D006023:Glycoproteins / Q000096:biosynthesis; D007668:Kidney; D008970:Molecular Weight; D009698:Nucleoproteins / Q000096:biosynthesis; D010750:Phosphoproteins / Q000096:biosynthesis; D011494:Protein Kinases / Q000378:metabolism; D012328:RNA Viruses / Q000201:enzymology*; D012367:RNA, Viral / Q000096:biosynthesis; D013696:Temperature; D014158:Transcription, Genetic; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000096:biosynthesis
D006023:Glycoproteins; D009698:Nucleoproteins; D010750:Phosphoproteins; D012367:RNA, Viral; D014764:Viral Proteins; D011494:Protein Kinases; D012321:DNA-Directed RNA Polymerases