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PMID: 1167603 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

RNA polymerase associated with virions of pike fry rhabdovirus.

Journal of virology ·Vol. 15 ·No. 2 ·1975-02-00 ·Pages 338-47

Roy P, Clark HF, Madore HP, Bishop DH

Abstract

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.

MeSH Terms
Animals Cell Line Cell-Free System Cricetinae Cyprinidae DNA-Directed RNA Polymerases/metabolism Electrophoresis, Polyacrylamide Gel Fishes/microbiology Glycoproteins/biosynthesis Kidney Molecular Weight Nucleoproteins/biosynthesis Phosphoproteins/biosynthesis Protein Kinases/metabolism RNA Viruses/enzymology RNA, Viral/biosynthesis Temperature Transcription, Genetic Viral Plaque Assay Viral Proteins/biosynthesis
Chemicals
Glycoproteins Nucleoproteins Phosphoproteins RNA, Viral Viral Proteins Protein Kinases DNA-Directed RNA Polymerases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Roy P
Clark H F
Madore H P
Bishop D H
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25 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1975-02-00
Pages
338-47
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC354458
Subset
IM
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