Cell-free translation ofDrosophila C virus RNA: Identification of a virus protease activity involved in capsid protein synthesis and further studies onin vitro processing of Cricket paralysis virus specified proteins
- 1 June 1983
- journal article
- research article
- Published by Springer Nature in Archiv für die gesamte Virusforschung
- Vol. 76 (2) , 101-115
- https://doi.org/10.1007/bf01311694
Abstract
Drosophila C virus RNA acted as mRNA in rabbit reticulocyte lysates and directed the synthesis of at least one capsid protein and a number of higher molecular weight proteins. Kinetic analysis by pulse-chase experiments showed that a number of high molecular weight products acted as precursors to the capsid protein(s). Various dilution experiments were performed which showed that the virus specified a protease activity essential for the correct processing of precursors to give the capsid protein(s). A similar result was obtained with Cricket paralysis virus, and mixing experiments showed that the protease activity specified by one virus could perform some of the cleavages resulting in the production of the capsid proteins of the other virus. Some of the cleavages involving the highest molecular weight precursors could not be performed by the protease activity of the other virus. We could find no evidence for intramolecular cleavage of the capsids precursors of either of the viruses.This publication has 28 references indexed in Scilit:
- Cell-free Translation of Cricket Paralysis Virus RNA: Analysis of the Synthesis and Processing of Virus-specified ProteinsJournal of General Virology, 1981
- In vitro translation of cricket paralysis virus RNAArchiv für die gesamte Virusforschung, 1981
- Processing of Cricket paralysis virus induced polypeptides inDrosophila cells: Production of high molecular weight polypeptides by treatment with iodoacetamideArchiv für die gesamte Virusforschung, 1981
- The intracellular proteins induced by cricket paralysis virus inDrosophila cells: The effect of protease inhibitors and amino acid analoguesArchiv für die gesamte Virusforschung, 1981
- Encephalomyocarditis virus‐specific polypeptide p22 possessing a proteolytic activityFEBS Letters, 1979
- End-point Dilution and Plaque Assay Methods for Titration of Cricket Paralysis Virus in Cultured Drosophila CellsJournal of General Virology, 1977
- An Efficient mRNA‐Dependent Translation System from Reticulocyte LysatesEuropean Journal of Biochemistry, 1976
- Quantitative Film Detection of 3H and 14C in Polyacrylamide Gels by FluorographyEuropean Journal of Biochemistry, 1975
- Cricket Paralysis Virus Replicates in Cultured Drosophila CellsIntervirology, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970