Protein synthesis in tobacco protoplasts infected with tobacco mosaic virus

Paterson, Rosemary; Knight, C.A.

doi:10.1016/0042-6822(75)90074-4

Cited by 73 publications

(16 citation statements)

References 12 publications

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“…Although the TMV-encoded 126kDa and 183 kDa polypeptides have been detected in virusinfected tissues [2,46,50], we are unaware of any quantitative data which would provide an accurate estimate of in vivo readthrough efficiency. The apparent efficiency of readthrough over the TMV stop measured in this study (ca.…”

Section: Discussionmentioning

confidence: 99%

Analysis of leaky viral translation termination codons in vivo by transient expression of improved ?-glucuronidase vectors

1990

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Plant RNA viruses commonly exploit leaky translation termination signals in order to express internal protein coding regions. As a first step to elucidate the mechanism(s) by which ribosomes bypass leaky stop codons in vivo, we have devised a system in which readthrough is coupled to the transient expression of beta-glucuronidase (GUS) in tobacco protoplasts. GUS vectors that contain the stop codons and surrounding nucleotides from the readthrough regions of several different RNA viruses were constructed and the plasmids were tested for the ability to direct transient GUS expression. These studies indicated that ribosomes bypass the leaky termination sites at efficiencies ranging from essentially 0 to ca. 5% depending upon the viral sequence. The results suggest that the efficiency of readthrough is determined by the sequence surrounding the stop codon. We describe improved GUS expression vectors and optimized transfection conditions which made it possible to assay low-level translational events.

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Section: Discussionmentioning

confidence: 99%

Analysis of leaky viral translation termination codons in vivo by transient expression of improved ?-glucuronidase vectors

1990

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“…Polyacrylamide slab gel electrophoresis under denaturing conditions (SDS-P AG E) was performed as described in (19). P olyacrylamide slab=gel electrophoresis in 5% acetic acid, 3 M urea and 0.4% Triton X 100 (AUT-PAGE) was under the conditions described in (9) except that the proteins in solution in water were adjusted by one volume of following solution: 10 mM acetic acid, 6 M urea, 0.8% Triton X 100, 40% glycerol, 2 mM DTT and 0.1% pyronin B. Electrophoresis was for 15 h at 100 volts.…”

Section: Electrophoretic Techniques All Solutions Of Acry-mentioning

confidence: 99%

HMG-like protein in barley and corn nuclei

Vincentz

Gigot

1985

Plant Mol Biol

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Chromosomal proteins have been isolated from barley (Hordeum vulgare) and corn (Zea mays) nuclei by extraction with 5% perchloric acid. In each plant, one protein was shown to belong to the HMG proteins. Their molecular weights are very close to that of HMG 14 from chicken erythrocytes, as shown by electrophoretic mobility in SDS polyacrylamide gels. In acetic acid-urea-Triton polyacrylamide gels they migrate between HMG 1,2 and HMG 14, from chicken erythrocytes. Their amino acid compositions are typical of HMG proteins, with equivalent high values of acidic and basic residues.Extraction of HMG's from purified barley chromatin fractions with 0.35 M NaCl considerably reduces histone H2 contamination and increases the yield of HMG up to 0.7% of the total histones. In this technique a second protein was extracted which is soluble in 2% Trichloroacetic acid and shows electrophoretic mobility analogous to those of HMG 14 and 17 from chicken erythrocytes. Whether or not these proteins are counterparts of the animal HMG's 1-2 or HMG's 14-17 is discussed.

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“…wt. are also synthesized (Paterson & Knight, 1975;Scalla, Boudon & Rigaud, I976). It has been shown that the two larger polypeptides are translated in vitro from the virus RNA whereas the coat protein is translated from a separate subgenomic mRNA.…”

Section: Proteins Induced By Calicivirus Infection 8imentioning

confidence: 99%

Proteins Induced by Infection with Caliciviruses

Black

Brown

1978

Journal of General Virology

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SUMMARYThree polypeptides with mol. wt. IOO (Ploo), 8o (P8o) and 65 (P65) × lO 3 were found in calicivirus infected cells. Ploo and P8o were present in sub-molar amounts compared with P65 and no precursor product relationship between the three polypeptides could be demonstrated using pulse-chase experiments or selective inhibitors of protein synthesis and of proteases. In the presence of protease inhibitors a polypeptide with mol. wt. I2O × IO 3 (PI20) was demonstrated which appeared to be the precursor of PlOO. Possible mechanisms of translation in the caliciviruses are discussed.

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Protein synthesis in tobacco protoplasts infected with tobacco mosaic virus

Cited by 73 publications

References 12 publications

Analysis of leaky viral translation termination codons in vivo by transient expression of improved ?-glucuronidase vectors

Analysis of leaky viral translation termination codons in vivo by transient expression of improved ?-glucuronidase vectors

HMG-like protein in barley and corn nuclei

Proteins Induced by Infection with Caliciviruses

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