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Literature DB >> 2345371

Evidence for the role of subgenomic RNAs in the production of potato virus S coat protein during in vitro translation.

Abstract

Purified virus particles of potato virus S (PVS) when disrupted yielded only one readily resolved band of 7.5 kb in ethidium bromide-stained agarose gels. However Northern hybridization of viral RNA, probed with a clone specific to the viral coat protein gene, revealed a region of subgenomic RNAs of approximately 1.3 kb. Sucrose gradient fractionation of subgenomic RNA revealed that it coded for viral coat protein when translated in vitro in rabbit reticulocyte lysate. Virus particle lengths suggest that this subgenomic RNA may be encapsidated in 100 to 220 nm particles.

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Year: 1990 PMID： 2345371 DOI： 10.1099/0022-1317-71-5-1247

Source DB: PubMed Journal: J Gen Virol ISSN： 0022-1317 Impact factor: 3.891

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Cited

7 in total

7. The nucleic acid-binding zinc finger protein of potato virus M is translated by internal initiation as well as by ribosomal frameshifting involving a shifty stop codon and a novel mechanism of P-site slippage.

Authors: A Gramstat; D Prüfer; W Rohde
Journal: Nucleic Acids Res Date: 1994-09-25 Impact factor: 16.971

7 in total

Evidence for the role of subgenomic RNAs in the production of potato virus S coat protein during in vitro translation.

1. The 3'-nucleotide sequence of an ordinary strain of potato virus S.

2. Investigation of the 5' terminal structures of genomic and subgenomic RNAs of potato virus S.

3. Coat protein and protease activity as in vitro translation products of potato carlavirus M RNA.

4. Cell-free translation of carnation latent virus RNA and analysis of virus-specific dsRNA.

5. Analysis of a translational enhancer upstream from the coat protein open reading frame of potato virus S.

6. Translation of potato virus S RNA in vitro: evidence of protein processing.

7. The nucleic acid-binding zinc finger protein of potato virus M is translated by internal initiation as well as by ribosomal frameshifting involving a shifty stop codon and a novel mechanism of P-site slippage.