A Comparison between the Capsid Proteins and the Products of in vitro Translation of Three Strains of Potato Virus X

The 5' non-translated aft-leader sequence of potato virus X RNA consists of two regions: the a sequence (41 nucleotides with no G) and the fl sequence (42 nucleotides upstream from AUG). The aft-leader has been shown to enhance strongly the expression of adjacent genes in chimeric mRNAs. This phenomenon has been postulated to be due to the unpaired conformation of the 5'-terminal 30 nucleotides and/or to the presence within the a region of the CCACC pentanucleotide complementary to the T-terminal conserved structure of 18S rRNA. Different derivatives of aft-leader have been constructed for use in determining the contribution of separate elements of the aft sequence to translational enhancement. It was found that deletion of the a sequence large fragment which was supposed to be unfolded did not reduce the A~fl-leader enhancement activity. Moreover, translational enhancement was greater for this derivative. Deletion of the fl sequence resulted in a considerable increase in activity of the aleader showing that the fl region was dispensable for translation. Disruption or 'masking' of CCACC led to inactivation of the aft-leader as a translational enhancer. Thus, we identified the CCACC pentanucleotide as the primary motif responsible for the translation enhancing ability of cot-leader.

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“…The translational strategy of PVX RNA has been studied (Wodnar-Filipowicz et al, 1980;Adams et al, 1987;Morozov et al, 1990Morozov et al, , 1991.…”

Section: Introductionmentioning

confidence: 99%

Effects of sequence elements in the potato virus X RNA 5' non-translated beta-leader on its translation enhancing activity

Tomashevskaya

Solovyev

Карпова

et al. 1993

Journal of General Virology

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Nucleotide sequence and in vitro translation of the coat protein gene of cymbidium mosaic virus

Neo

Wong

1993

Virus Genes

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The nucleotide sequence of the coat protein gene of cymbidium mosaic virus (CyMV) has been determined from a cDNA clone that encompassed the 3'-region of the virus genome. The 0.75 kb coat protein open reading frame (ORF) codes for a 24kD polypeptide. The coat protein coding region was separated from the 3'-poly(A) terminal of the viral genome by an 80 base noncoding region. The derived amino acid sequence of this ORF showed considerable homology with other potexvirus coat protein sequences, notably with narcissus mosaic virus (NMV), potato virus X (PVX), and white clover mosaic virus (WClMV). In vitro expression of the CyMV coat protein gene was carried out by T7 RNA polymerase on the linearized cDNA clone template, followed by in vitro translation of the purified transcript in wheat germ extract. One of the translated products was found to comigrate with the coat protein of the virus at about 24 kD, as determined by NaDodSO4-PAGE. This translated product was also found to crossreact with antibodies raised against CyMV.

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Anomalous electrophoretic behavior of the major potato virus X RNA translation product

Karasev

Miroshnichenko

Rozanov

1989

Journal of Virological Methods

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A Comparison between the Capsid Proteins and the Products of in vitro Translation of Three Strains of Potato Virus X

Cited by 7 publications

References 17 publications

Effects of sequence elements in the potato virus X RNA 5' non-translated beta-leader on its translation enhancing activity

Effects of sequence elements in the potato virus X RNA 5' non-translated beta-leader on its translation enhancing activity

Nucleotide sequence and in vitro translation of the coat protein gene of cymbidium mosaic virus

Anomalous electrophoretic behavior of the major potato virus X RNA translation product

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