Degradation of tobacco mosaic virus with acetic acid

Fraenkel‐Conrat, H.

doi:10.1016/0042-6822(57)90038-7

Cited by 544 publications

(106 citation statements)

References 4 publications

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“…However, the addition of coat protein does not inhibit the acceptor capacity of TMV RNA or of yeast tRNA. The reconstitution of viral particles by addition of RNA and coat protein can be attained in vitro, but it requires prolonged incubation under special conditions [12]. It has been shown that assembly starts by addition of coat protein to regions of RNA.…”

Section: Tmv-rna Aminoacylation Studiesmentioning

confidence: 99%

Further studies on the enzymatic aminoacylation of TMV‐RNA by histidine

Carriquiry

Litvak

1974

FEBS Letters

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Section: Tmv-rna Aminoacylation Studiesmentioning

confidence: 99%

Further studies on the enzymatic aminoacylation of TMV‐RNA by histidine

Carriquiry

Litvak

1974

FEBS Letters

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“…This method, originally developed to purify nucleic acid-free viral proteins (Fraenkel-Conrat, 1957), was used to remove remaining nucleic acids contained in the nucleolar fraction. The resulting nucleolar proteins were solubilized in isoelectric focusing (IEF) buffer containing urea.…”

Section: Electrophoresis and Western Blotting Proceduresmentioning

confidence: 99%

Functional Proteomic Analysis of Human Nucleolus

Scherl

Couté

Déon

et al. 2002

MBoC

440

378

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The notion of a “plurifunctional” nucleolus is now well established. However, molecular mechanisms underlying the biological processes occurring within this nuclear domain remain only partially understood. As a first step in elucidating these mechanisms we have carried out a proteomic analysis to draw up a list of proteins present within nucleoli of HeLa cells. This analysis allowed the identification of 213 different nucleolar proteins. This catalog complements that of the 271 proteins obtained recently by others, giving a total of ∼350 different nucleolar proteins. Functional classification of these proteins allowed outlining several biological processes taking place within nucleoli. Bioinformatic analyses permitted the assignment of hypothetical functions for 43 proteins for which no functional information is available. Notably, a role in ribosome biogenesis was proposed for 31 proteins. More generally, this functional classification reinforces the plurifunctional nature of nucleoli and provides convincing evidence that nucleoli may play a central role in the control of gene expression. Finally, this analysis supports the recent demonstration of a coupling of transcription and translation in higher eukaryotes.

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“…TMV, a Japanese common strain OM, was purified by polyethylene glycol precipitation (12) followed by differential centrifugation. TMV protein and RNA were isolated by the acetic acid method (13) and by phenolbentonite extraction (14), respectively. TMV RNA radioactively labeled at its termini was prepared by periodate oxidation and subsequent reduction with tritiated sodium borohydride (8).…”

mentioning

confidence: 99%

Kinetics of biphasic reconstitution of tobacco mosaic virus in vitro.

Fukuda¹,

Ohno²,

Okada³

et al. 1978

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

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The kinetics of the in vitro reconstitution of tobacco mosaic virus from its RNA and protein were studied by measuring the increase in turbidity, the development of ribonuclease-resistant infectivity, the encapsidation of the terminal ends of the RNA, and the growth of rod length. Recently, several laboratories independently reached the conclusion that reconstitution starts at an internal region of the RNA, about 800-1000 nucleotides from the 3' terminus, and that the elongation occurs bidirectionally (7-10). In an early phase of the reaction, the rod elongation toward the 5' end is much favored over that toward the 3' end (9-11). The present study deals with kinetics of the bidirectional elongation of TMV rods during the reconstitution reaction, studied by measuring turbidity, infectivity, RNase resistance of the two ends of RNA, and rod length. The results show that reconstitution takes place in two successive phases that differ not only in the direction, but also in the rate of rod elongation. Rods with a length of 260 nm were identified as the product of the early process of reconstitution.MATERIALS AND METHODS Preparation of TMV, TMV Protein, TMV RNA, and Tritium-Labeled TMV RNA. TMV, a Japanese common strain OM, was purified by polyethylene glycol precipitation (12) followed by differential centrifugation. TMV protein and RNA were isolated by the acetic acid method (13) and by phenolbentonite extraction (14), respectively. TMV RNA radioactively labeled at its termini was prepared by periodate oxidation and subsequent reduction with tritiated sodium borohydride (8). Both the 5'-and the 3'-ribosyl ends of TMV RNA were labeled with about the same efficiency.The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.Reconstitution Reaction. A protein disk preparation was obtained by incubation of the protein (6.6 mg/ml) for 24 hr in 0.1 M phosphate buffer (pH 7.0) at 20°. Reconstitution reactions were carried out in the same buffer at 200 by mixing the protein disk preparation (5.6 mg/ml) with a mixture of TMV RNA (0.13 mg/ml) and tritium-labeled TMV RNA (0.05 mg/ml). At intervals, aliquots were withdrawn to determine the rod lengths, the ribonuclease resistance of tritium-labeled termini, and the infectivity.Turbidimetric Measurement during Reconstitution Reaction. The reconstitution reaction during the initial 90 min of the reaction was followed by the increase in absorbance at 310 nm with a Gilford model 250 spectrophotometer.Rod Length Measurements by Electron Microscopy. An aliquot from the reaction mixture was diluted 1:100 with icecold 0.01% (wt/vol) bovine serum albumin solution, and minute drops of the mixture were placed on carbon-coated electron microscope grids. The grids were immediately transferred to a desiccator and kept under reduced pressure overnight. The specimens were then negatively stained with 1% (wt/vol) phosphotungst...

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Degradation of tobacco mosaic virus with acetic acid

Cited by 544 publications

References 4 publications

Further studies on the enzymatic aminoacylation of TMV‐RNA by histidine

Further studies on the enzymatic aminoacylation of TMV‐RNA by histidine

Functional Proteomic Analysis of Human Nucleolus

Kinetics of biphasic reconstitution of tobacco mosaic virus in vitro.

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