An analysis of tobacco mosaic virus replicative structures synthesized in vitro

1986 ◽  
Vol 6 (6) ◽  
pp. 455-465 ◽  
Author(s):  
Nevin Dale Young ◽  
Milton Zaitlin
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus

scholarly journals Role of the 3′ tRNA-Like Structure in Tobacco Mosaic Virus Minus-Strand RNA Synthesis by the Viral RNA-Dependent RNA Polymerase In Vitro

2000 ◽  
Vol 74 (24) ◽  
pp. 11671-11680 ◽  
Author(s):  
T. A. M. Osman ◽  
C. L. Hemenway ◽  
K. W. Buck
Keyword(s):  
Rna Polymerase ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Untranslated Region ◽  
Rna Synthesis ◽  
Central Core ◽  
Minus Strand ◽  
Stem Loop ◽  
Polymerase Binding

ABSTRACT A template-dependent RNA polymerase has been used to determine the sequence elements in the 3′ untranslated region of tobacco mosaic virus RNA that are required for promotion of minus-strand RNA synthesis and binding to the RNA polymerase in vitro. Regions which were important for minus-strand synthesis were domain D1, which is equivalent to a tRNA acceptor arm; domain D2, which is similar to a tRNA anticodon arm; an upstream domain, D3; and a central core, C, which connects domains D1, D2, and D3 and determines their relative orientations. Mutational analysis of the 3′-terminal 4 nucleotides of domain D1 indicated the importance of the 3′-terminal CA sequence for minus-strand synthesis, with the sequence CCCA or GGCA giving the highest transcriptional efficiency. Several double-helical regions, but not their sequences, which are essential for forming pseudoknot and/or stem-loop structures in domains D1, D2, and D3 and the central core, C, were shown to be required for high template efficiency. Also important were a bulge sequence in the D2 stem-loop and, to a lesser extent, a loop sequence in a hairpin structure in domain D1. The sequence of the 3′ untranslated region upstream of domain D3 was not required for minus-strand synthesis. Template-RNA polymerase binding competition experiments showed that the highest-affinity RNA polymerase binding element region lay within a region comprising domain D2 and the central core, C, but domains D1 and D3 also bound to the RNA polymerase with lower affinity.

scholarly journals Tobacco Mosaic Virus Movement Protein Functions as a Structural Microtubule-Associated Protein

2006 ◽  
Vol 80 (17) ◽  
pp. 8329-8344 ◽  
Author(s):  
Jamie Ashby ◽  
Emmanuel Boutant ◽  
Mark Seemanpillai ◽  
Adrian Sambade ◽  
Christophe Ritzenthaler ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Extract ◽  
Transport Processes ◽  
In Vitro Assays ◽  
Protein Functions ◽  
Intercellular Spread

ABSTRACT The cell-to-cell spread of Tobacco mosaic virus infection depends on virus-encoded movement protein (MP), which is believed to form a ribonucleoprotein complex with viral RNA (vRNA) and to participate in the intercellular spread of infectious particles through plasmodesmata. Previous studies in our laboratory have provided evidence that the vRNA movement process is correlated with the ability of the MP to interact with microtubules, although the exact role of this interaction during infection is not known. Here, we have used a variety of in vivo and in vitro assays to determine that the MP functions as a genuine microtubule-associated protein that binds microtubules directly and modulates microtubule stability. We demonstrate that, unlike MP in whole-cell extract, microtubule-associated MP is not ubiquitinated, which strongly argues against the hypothesis that microtubules target the MP for degradation. In addition, we found that MP interferes with kinesin motor activity in vitro, suggesting that microtubule-associated MP may interfere with kinesin-driven transport processes during infection.

In vitro and in vivo aggregation of the defective PM2 tobacco mosaic virus protein

1966 ◽  
Vol 19 (1) ◽  
pp. 140-IN8 ◽  
Author(s):  
Albert Siegel ◽  
G.J. Hills ◽  
Roy Markham
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Protein

On in vitro and in vivo binding of tobacco mosaic virus to cytoplasmic membranes

1984 ◽  
Vol 179 (6) ◽  
pp. 507-516 ◽  
Author(s):  
Barbara Pustowoit ◽  
Wladimir Pustowoit ◽  
Gottfried Schuster
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
In Vivo Binding ◽  
Cytoplasmic Membranes

scholarly journals Visualization by atomic force microscopy of tobacco mosaic virus movement protein–RNA complexes formed in vitro

2001 ◽  
Vol 82 (6) ◽  
pp. 1503-1508 ◽  
Author(s):  
O. I. Kiselyova ◽  
I. V. Yaminsky ◽  
E. M. Karger ◽  
O. Yu. Frolova ◽  
Y. L. Dorokhov ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Structural Conversion ◽  
Force Microscopy ◽  
Rna Transcripts ◽  
Atomic Force ◽  
Rna Complexes

The structure of complexes formed in vitro by tobacco mosaic virus (TMV)-coded movement protein (MP) with TMV RNA and short (890 nt) synthetic RNA transcripts was visualized by atomic force microscopy on a mica surface. MP molecules were found to be distributed along the chain of RNA and the structure of MP–RNA complexes depended on the molar MP:RNA ratios at which the complexes were formed. A rise in the molar MP:TMV RNA ratio from 20:1 to 60–100:1 resulted in an increase in the density of the MP packaging on TMV RNA and structural conversion of complexes from RNase-sensitive ‘beads-on-a-string’ into a ‘thick string’ form that was partly resistant to RNase. The ‘thick string’-type RNase-resistant complexes were also produced by short synthetic RNA transcripts at different MP:RNA ratios. The ‘thick string’ complexes are suggested to represent clusters of MP molecules cooperatively bound to discrete regions of TMV RNA and separated by protein-free RNA segments.

scholarly journals Reconstitution of Tobacco Mosaic Virus in vitro Inhibition by Coat Proteins of Other Strains

1969 ◽  
Vol 45 (10) ◽  
pp. 919-924 ◽  
Author(s):  
Yuko OHASHI ◽  
Takeshi OHNO ◽  
Yuzo NOZU ◽  
Yoshimi OKADA
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Coat Proteins ◽  
In Vitro Inhibition

scholarly journals In Vitro Secondary Structure of the Genomic RNA of Satellite Tobacco Mosaic Virus

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e54384 ◽  
Author(s):  
Shreyas S. Athavale ◽  
J. Jared Gossett ◽  
Jessica C. Bowman ◽  
Nicholas V. Hud ◽  
Loren Dean Williams ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Genomic Rna ◽  
Satellite Tobacco Mosaic Virus

scholarly journals Enhancing effect of the 3′-untranslated region of tobacco mosaic virus RNA on protein synthesis in vitro

FEBS Letters ◽  
1994 ◽  
Vol 354 (3) ◽  
pp. 271-273 ◽  
Author(s):  
Vladimir V. Zeyenko ◽  
Lyubov A. Ryabova ◽  
Daniel R. Gallie ◽  
Alexander S. Spirin
Keyword(s):  
Protein Synthesis ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Untranslated Region ◽  
Enhancing Effect ◽  
Virus Rna

Mixed assembly of tobacco mosaic virus in vitro

Virology ◽  
1972 ◽  
Vol 47 (3) ◽  
pp. 773-779 ◽  
Author(s):  
Haruo Onda
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus
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