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Expression of high molecular weight polypeptides by carnation mottle virus RNA

Department of Virus Research, John Innes Institute, Colney Lane, Norwich NR4 7UH, U.K. In vitro translation of virion RNA from carnation mottle virus (CarMV) in a messenger RNA-dependent rabbit reticulocyte lysate (MDL) resulted in the synthesis of four virus-specific polypeptides of apparent M r 10...

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Bibliographic Details
Published in:Journal of general virology 1985-12, Vol.66 (12), p.2597-2604
Main Authors: Harbison, S.A, Davies, J.W, Wilson, T.M.A
Format: Article
Language:English
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Summary:Department of Virus Research, John Innes Institute, Colney Lane, Norwich NR4 7UH, U.K. In vitro translation of virion RNA from carnation mottle virus (CarMV) in a messenger RNA-dependent rabbit reticulocyte lysate (MDL) resulted in the synthesis of four virus-specific polypeptides of apparent M r 100000 (P100), 77000 (P77), 38000 (P38) and 30000 (P30). Partial peptide mapping experiments and in vitro translation in the presence of partially purified calf liver amber suppressor tRNA demonstrated that P30, P77 and P100 are a series of overlapping polypeptides generated by a double readthrough mechanism. In addition we report the infection of Chenopodium quinoa protoplasts with CarMV. The viral coat protein was detected in virus-infected protoplasts. Only one other infection-specific protein with an apparent M r of 100000 corresponded in size to any of the other in vitro translation products. Keywords: CarMV, translation, readthrough, protoplasts Received 30 April 1985; accepted 22 August 1985.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-66-12-2597