Evidence for the Role of Subgenomic RNAs in the Production of Potato Virus S coat Protein During in Vitro Translation

Foster, Gary D.; Mills, Peter R.

doi:10.1099/0022-1317-71-5-1247

Cited by 22 publications

(11 citation statements)

References 15 publications

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“…As with several other viruses that contain the triple block motif, the number of RNA species responsible for expression of 3' end genes is unclear. Although we have evidence for only two subgenomic RNA species associated with BBScV (data not shown), similar to results reported for PVS (Foster & Mills, 1990), it should be noted that the low level of replication of BBScV renders it a poor candidate for studies of gene expression. Unlike luteoviruses, in which the AUG context of the second ORF of the large subgenomic RNA tends to be in a more favourable context than the first, and is thus translated efficiently despite its internal position (Dinesh-Kumar et al, 1992), the first AUG of the BBScV triple block is the most favourable for translation (Kozak, 1989).…”

Section: T D Cavileer and Otherssupporting

confidence: 55%

Nucleotide sequence of the carlavirus associated with blueberry scorch and similar diseases

Cavileer

Halpern

Lawrence

et al. 1994

Journal of General Virology

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Section: T D Cavileer and Otherssupporting

confidence: 55%

Nucleotide sequence of the carlavirus associated with blueberry scorch and similar diseases

Cavileer

Halpern

Lawrence

et al. 1994

Journal of General Virology

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“…Evidence for the existence of subgenomic RNAs for the coat protein for a number ofcarlaviruses has been presented in the past, though these subgenomic RNAs have only been detected at low levels in comparison to genomic RNA levels [4,5,9]. For other carlaviruses it has proved difficult to detect subgenomic RNAs in both RNA from infected tissue and RNA isolated from purified virus particles, yet when extracted RNA is translated in vitro coat protein is one of the first and most abundant products to appear.…”

Section: Introductionmentioning

confidence: 98%

“…This positive-sense and single-stranded RNA, with a Mr between 2.3 and 2.6 x 10 6 (7-7.8 kb) has a 3'-terminal poly (A) tract and contains a 5' terminal cap structure [2,3]. Genomic RNA appears to encode a large molecular mass product of 190K estimated from translation results for potato virus S (PVS), Helenium virus S (HelVS), American hop latent virus (AHLV) and carnation latent virus (CLV) [4,5,8,15], and a product of 223K from sequence analysis of potato virus M (PVM) [25]. This product is presumably the repticase as it has been shown to contain three conserved domains in a sequence typical of other replicases of animal alphaviruses, plant potexviruses, tymoviruses, tobamoviruses, tobraviruses and furoviruses [18].…”

Section: Introductionmentioning

confidence: 99%

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

Turner

Bate

Twell

et al. 1994

Archives of Virology

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Evidence has suggested that the subgenomic RNA of the carlavirus potato virus S is an efficient message for the coat protein, even though evidence suggests it is uncapped at its 5' terminus. We have investigated the effect of the upstream region of the coat protein gene of potato virus S on the level of reporter gene expression in vitro. The region of 101 nucleotides upstream of the coat protein, designated VTE (viral translational enhancer) was found to increase levels of translation in comparison to a synthetic leader when linked to the beta-glucuronidase (GUS) reporter gene in vitro in rabbit reticulocyte and wheat germ lysate. VTE was also able to increase translation of the reporter gene luciferase (LUC) in vitro above the levels obtained for both a synthetic leader and a leader obtained from a plant gene isolated from Arabidopsis thaliana. The level of enhancement was evident with both capped and uncapped transcripts. When the VTE sequence was deleted to 20 nucleotides of the upstream region, thus removing the nucleotide block homologous among carlaviruses, the ability to enhance levels of translation was removed. In vitro translation studies indicated that the translational enhancement activity of VTE was at least partially cap independent. Translation of VTE linked to reporter genes in the presence of cap analogue was relatively unaffected whereas synthetic leader and a plant leader constructs were both more sensitive. In vitro competition analysis revealed that when short RNA transcripts representing the 101 nucleotides of VTE were added in trans to functional VTE leader LUC constructs there was a marked decrease in the level of translation when compared with a synthetic leader added in trans. These results suggest that the upstream region of the coat protein ORF of potato virus S promotes translation in a cap-independent manner that may involve the binding of proteins and/or ribosomes to the 101 nucleotides of the VTE sequence.

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“…Reports concerning the virion-associated RNA in potato carlavirus S (PVS) also are at variance. Foster and Mills [9] found two subgenomic RNAs in RNA preparations from an Irish isolate of PVS. In contrast, Monis and De Zoeten [24] observed no subgenomic RNAs in RNA isolated from purified virions of the Andean strain of PVS (PVS-An) propagated in Chenopodium quinoa.…”

Section: Discussionmentioning

confidence: 98%

“…The 34 k CP is encoded by the genome-size R N A of the Andean (An) strain of PVS [24]. By contrast, a subgenomic (1.3 kb) R N A directs synthesis of the CP in an Irish isolate of PVS [9].…”

Section: Introductionmentioning

confidence: 96%

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

Tavantzis

1991

Archives of Virology

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Genomic-size RNA isolated from purified potato carlavirus M (PVM) was translated in both the reticulocyte and the wheat germ cell-free, messenger-dependent systems. The PVM RNA translated the same set of major products in both in vitro systems. The Mr values of the most prominent polypeptides observed consistently were 185,000 (P185), 147,000 (P147), 94,000 (P94), 87,000 (P87), 72,000 (P72), 67,000 (P67), 52,000 (P52), 46,000 (P46), 35,000 (P35) and 25,000 (P25). Relatively low amounts of a translation product of Mr 200,000 (P200) were often detectable in both systems. The P35 polypeptide displayed the same molecular weight and one-dimensional peptide map as the virus coat protein (CP), and was precipitated by antibodies raised against PVM and PVM CP. The kinetics of appearance of the in vitro synthesized polypeptides suggested that primary translation products of high molecular weight undergo post-translational proteolytic cleavage.

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Evidence for the Role of Subgenomic RNAs in the Production of Potato Virus S coat Protein During in Vitro Translation

Cited by 22 publications

References 15 publications

Nucleotide sequence of the carlavirus associated with blueberry scorch and similar diseases

Nucleotide sequence of the carlavirus associated with blueberry scorch and similar diseases

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

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

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