The protein subunit of the satellite tobacco necrosis virus

Roy, Dipanjan; Fraenkel‐Conrat, H.; Lesnaw, Judith A.; Me, Reichmann

doi:10.1016/0042-6822(69)90384-5

Cited by 16 publications

(4 citation statements)

References 7 publications

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“…This possibility follows from the observation that the only other reported example of a message correctly translated in vitro to yield a recognizable protein product in both a procaryotic and a eucaryotic system is the biosynthesis of hemoglobin (Laycock and Hunt, 1969; Schweet et al, 1958). Alternately, current coding stoichiometry based upon the monocistrony of STNV-RNA, the 1200 nucleotides within STNV-RNA (Reichmann, 1964), and the approximately 200 amino acids in STNV coat protein (Roy et al, 1969;Lesnaw and Reichmann, 1969;Rees et al, 1970) emphasize that only half of STNV-RNA appears to be translated. Perhaps structural features of the untranslated portion(s) of STNV-RNA, acting by themselves or in combination with translated portions of STNV-RNA, provide the potential for correct in vitro translation in such varied systems.…”

Section: Discussionmentioning

confidence: 99%

“…This initial assumption was based upon the satellite property of STNV,* 1 the immunological properties of the system, and the apparent 3:1 ratio of STNV-RNA nucleotides to STNV coat protein amino acids. The more recent observations that STNV coat protein is smaller than originally envisioned (Roy et al, 1969; Lesnaw and Reichmann, 1969) force one to be aware of the possible polycistronic character of STNV-RNA. Yet the small size of the viral RNA (with its resultant limited coding potential) and the observation (Clark et al, 1965) that, in vitro, STNV-RNA codes as a monocistronic message for STNV coat protein emphasize the uniqueness of the STNV system.…”

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confidence: 99%

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Translation of satellite tobacco necrosis virus ribonucleic acid. I. Characterization of in vitro procaryotic and eucaryotic translation products

Klein¹,

Nolan²,

Lazar³

et al. 1972

Biochemistry

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Translation of satellite tobacco necrosis virus ribonucleic acid. I. Characterization of in vitro procaryotic and eucaryotic translation products

Klein¹,

Nolan²,

Lazar³

et al. 1972

Biochemistry

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“…We chose to characterize the translation products of STNV-RNA using more discriminating techniques which have become available since the original report appeared. The RNA of STNV is a convenient messenger for this kind of work in that it is small (0.4 X 106) and can code maximally for only one small protein in addition to the viral coat protein (Roy et al, 1969). Since the completion of this work, an interesting study of the translation of STNV-RNA in E. coli and wheat embryo cell-free systems has appeared (Klein et al, 1972;Lundquist et al, 1972).…”

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confidence: 99%

Fidelity of translation of satellite tobacco necrosis virus ribonucleic acid in a cell-free Escherichia coli system

Rice¹,

Fraenkel‐Conrat²

1973

Biochemistry

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The polypeptides synthesized in an E. coli cell-free system under the direction of the small RNA of the satellite tobacco necrosis virus were compared with the authentic coat protein of this virus. Many of the tryptic peptides obtained from the two types of proteins moved identically upon highresolution cation exchange column chromatography, but distinct qualitative and quantitative differences between the two peptide patterns were also evident.

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“…6 In view of these results and the limited information contained in the satellite tobacco necrosis virus genome7' 8 it is likely that the STNV-RNA utilizes at least a portion of the TNV-RNA replicase, and has an identical recognition sequence. Since the coat proteins of the two viruses are unrelated,9' 10 any homologies in the two RNA's are likely to reflect RNA replicase recognition sites.…”

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confidence: 99%

Identity of the 5′-Terminal RNA Nucleotide Sequence of the Satellite Tobacco Necrosis Virus and Its Helper Virus: Possible Role of the 5′-Terminus in the Recognition by Virus-Specific RNA Replicase

Lesnaw¹,

Reichmann²

1970

Proc. Natl. Acad. Sci. U.S.A.

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Abstract. A pancreatic ribonuclease digest of 14C-labeled tobacco necrosis virus RNA was fractionated according to charge by column chromatography. Individual fractions were dephosphorylated with alkaline phosphatase and rechromatographed. The fraction, originally containing oligonucleotides with seven negative charges, separated into two components corresponding to five (-5) and two negative charges (-2). The -5 fraction was derived from the internal oligonucleotides while the -2 fraction must have originated from a 5'-pyrophosphorylated terminal trinucleotide. The sequence of this terminal trinucleotide was determined by column chromatography on DEAE-cellulose in a triethyl ammonium carbonate gradient, using the appropriate markers. The radioactivity chromatographed with a (ApGp)U marker. The order of the Ap and Gp was determined after ribonuclease T1 and alkaline phosphatase digestion. The radioactivity in the product chromatographed with an ApG marker. The 5'-terminus of tobacco necrosis virus RNA was therefore determined as ppApGpUp . . ., which is identical to the terminus of the RNA of its satellite virus as previously determined (J. llMol. Biol., 38, 59 (1968); Science, 160, 1452 (1968)).The 5' pyrophosphate in both viruses was probably formed by an in vivo enzymatic removal of a y-phosphate from a triphosphate, and its presence in both viruses suggested a common site of synthesis. The identity of the 5'-terminal sequences is considered not to be fortuitous and is discussed from the standpoint of their role as a recognition site for the virus-specific RNA replicase.Sequence studies of the mRNA's of viral origin'-' surprisingly failed to reveal the presence of a protein-chain initiating codon near the 5'-terminus. It must therefore be concluded that these nucleotide sequences are not part of a cistron and their biological role remains obscure. De Wachter and Fiers'showed that the 5'-terminal sequence of Q#-RNA was identical to the sequence of the "little variant"4 reported by Bishop.5 In view of the template activity of the little variant, the conservation of the 5'-terminus would suggest its possible role as a recognition site-for Q,-RNA replicase.Experiments with partly purified extracts of plants infected with tobacco necrosis virus (TNV) in our laboratory, showed that labeled nucleotides were incorporated into high molecular weight RNA under the direction of both TNV-140

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The protein subunit of the satellite tobacco necrosis virus

Cited by 16 publications

References 7 publications

Translation of satellite tobacco necrosis virus ribonucleic acid. I. Characterization of in vitro procaryotic and eucaryotic translation products

Translation of satellite tobacco necrosis virus ribonucleic acid. I. Characterization of in vitro procaryotic and eucaryotic translation products

Fidelity of translation of satellite tobacco necrosis virus ribonucleic acid in a cell-free Escherichia coli system

Identity of the 5′-Terminal RNA Nucleotide Sequence of the Satellite Tobacco Necrosis Virus and Its Helper Virus: Possible Role of the 5′-Terminus in the Recognition by Virus-Specific RNA Replicase

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