Purification and Separation of Tobacco Mosaic Virus and Southern Bean Mosaic Virus by Agar-gel Filtration

Nature ◽  
1962 ◽  
Vol 194 (4823) ◽  
pp. 114-116 ◽  
Author(s):  
R. L. STEERE ◽  
G. K. ACKERS
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Gel Filtration ◽  
Agar Gel ◽  
Southern Bean Mosaic Virus

scholarly journals Oligomerization and Activity of the Helicase Domain of the Tobacco Mosaic Virus 126- and 183-Kilodalton Replicase Proteins

2003 ◽  
Vol 77 (6) ◽  
pp. 3549-3556 ◽  
Author(s):  
Sameer P. Goregaoker ◽  
James N. Culver
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Protein Interaction ◽  
Gel Filtration ◽  
Helicase Domain ◽  
Protein Protein Interaction ◽  
Replicase Proteins

ABSTRACT A protein-protein interaction within the helicase domain of the Tobacco mosaic virus (TMV) 126- and 183-kDa replicase proteins was previously implicated in virus replication (S. Goregaoker, D. Lewandowski, and J. Culver, Virology 282:320-328, 2001). To further characterize the interaction, polypeptides covering the interacting portions of the TMV helicase domain were expressed and purified. Biochemical characterizations demonstrated that the helicase domain polypeptides hydrolyzed ATP and bound both single-stranded and duplexed RNA in an ATP-controlled fashion. A TMV helicase polypeptide also was capable of unwinding duplexed RNA, confirming the predicted helicase function of the domain. Biochemically active helicase polypeptides were shown by gel filtration to form high-molecular-weight complexes. Electron microscopy studies revealed the presence of ring-like oligomers that displayed six-sided symmetry. Taken together, these data demonstrate that the TMV helicase domain interacts with itself to produce hexamer-like oligomers. Within the context of the full-length 126- and 183-kDa proteins, these findings suggest that the TMV replicase may form a similar oligomer.

THE INCORPORATION OF p-FLUOROPHENYLALANINE INTO TOBACCO MOSAIC VIRUS

1962 ◽  
Vol 40 (8) ◽  
pp. 999-1004 ◽  
Author(s):  
P. M. Townsley
Keyword(s):  
Amino Acid ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Leaf Tissue ◽  
Free Fraction ◽  
Natural Amino Acid ◽  
Agar Gel ◽  
Tobacco Leaf ◽  
Zone Electrophoresis ◽  
Reduced Rate

Disks of diseased tobacco leaf tissue were treated with phenylalanine and with the analogue p-fluorophenylalanine. The expressed sap was separated into its components by agar gel zone electrophoresis. p-Fluorophenylalanine was shown to be incorporated into TMV at a reduced rate as compared with the natural amino acid phenylalanine. The analogue inhibited incorporation of phosphorus, a reversal probably due to the increase in phenylalanine observed in the soluble amino-acid-free fraction.

THE ELECTROPHORETIC ANALYSIS OF PLANT VIRUS PREPARATIONS

1959 ◽  
Vol 37 (1) ◽  
pp. 119-126 ◽  
Author(s):  
P. M. Townsley
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Plant Extracts ◽  
Plant Virus ◽  
Potato Virus X ◽  
Electrophoretic Analysis ◽  
Agar Gel ◽  
Zone Electrophoresis ◽  
Staining Methods ◽  
Protein Staining

Zone electrophoresis in agar gel has been used for separating tobacco mosaic virus and potato virus X from crude plant extracts and reaction mixtures. The viruses were located within the gel by autoradiographic, serological, and protein-staining methods.

THE INCORPORATION OF p-FLUOROPHENYLALANINE INTO TOBACCO MOSAIC VIRUS

1962 ◽  
Vol 40 (1) ◽  
pp. 999-1004
Author(s):  
P. M. Townsley
Keyword(s):  
Amino Acid ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Leaf Tissue ◽  
Free Fraction ◽  
Natural Amino Acid ◽  
Agar Gel ◽  
Tobacco Leaf ◽  
Zone Electrophoresis ◽  
Reduced Rate

Disks of diseased tobacco leaf tissue were treated with phenylalanine and with the analogue p-fluorophenylalanine. The expressed sap was separated into its components by agar gel zone electrophoresis. p-Fluorophenylalanine was shown to be incorporated into TMV at a reduced rate as compared with the natural amino acid phenylalanine. The analogue inhibited incorporation of phosphorus, a reversal probably due to the increase in phenylalanine observed in the soluble amino-acid-free fraction.

THE ELECTROPHORETIC ANALYSIS OF PLANT VIRUS PREPARATIONS

1959 ◽  
Vol 37 (1) ◽  
pp. 119-126 ◽  
Author(s):  
P. M. Townsley
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Plant Extracts ◽  
Plant Virus ◽  
Potato Virus X ◽  
Electrophoretic Analysis ◽  
Agar Gel ◽  
Zone Electrophoresis ◽  
Staining Methods ◽  
Protein Staining

Zone electrophoresis in agar gel has been used for separating tobacco mosaic virus and potato virus X from crude plant extracts and reaction mixtures. The viruses were located within the gel by autoradiographic, serological, and protein-staining methods.

ZONE ELECTROPHORESIS OF TOBACCO MOSAIC VIRUS

1959 ◽  
Vol 37 (8) ◽  
pp. 1025-1031 ◽  
Author(s):  
P. M. Townsley
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Ribonuclease Activity ◽  
Agar Gel ◽  
Zone Electrophoresis

An apparatus is described for the preparative zone electrophoresis of tobacco mosaic virus in agar gel. The isolated virus does not have any detectable ribonuclease activity.

ZONE ELECTROPHORESIS OF TOBACCO MOSAIC VIRUS

1959 ◽  
Vol 37 (1) ◽  
pp. 1025-1031 ◽  
Author(s):  
P. M. Townsley
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Ribonuclease Activity ◽  
Agar Gel ◽  
Zone Electrophoresis

An apparatus is described for the preparative zone electrophoresis of tobacco mosaic virus in agar gel. The isolated virus does not have any detectable ribonuclease activity.

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