Infectious Barley stripe mosaic virus RNA transcribed in Vitro from full-length genomic cDNA clones

Virology ◽  
1989 ◽  
Vol 171 (2) ◽  
pp. 342-349 ◽  
Author(s):  
I.T.D. Petty ◽  
B.G. Hunter ◽  
N. Wei ◽  
A.O. Jackson
FEBS Letters ◽  
1994 ◽  
Vol 354 (3) ◽  
pp. 271-273 ◽  
Author(s):  
Vladimir V. Zeyenko ◽  
Lyubov A. Ryabova ◽  
Daniel R. Gallie ◽  
Alexander S. Spirin

2008 ◽  
Vol 82 (10) ◽  
pp. 4991-5006 ◽  
Author(s):  
Hyoun-Sub Lim ◽  
Jennifer N. Bragg ◽  
Uma Ganesan ◽  
Diane M. Lawrence ◽  
Jialin Yu ◽  
...  

ABSTRACT Barley stripe mosaic virus (BSMV) encodes three movement proteins in an overlapping triple gene block (TGB), but little is known about the physical interactions of these proteins. We have characterized a ribonucleoprotein (RNP) complex consisting of the TGB1 protein and plus-sense BSMV RNAs from infected barley plants and have identified TGB1 complexes in planta and in vitro. Homologous TGB1 binding was disrupted by site-specific mutations in each of the first two N-terminal helicase motifs but not by mutations in two C-terminal helicase motifs. The TGB2 and TGB3 proteins were not detected in the RNP, but affinity chromatography and yeast two-hybrid experiments demonstrated that TGB1 binds to TGB3 and that TGB2 and TGB3 form heterologous interactions. These interactions required the TGB2 glycine 40 and the TGB3 isoleucine 108 residues, and BSMV mutants containing these amino acid substitution were unable to move from cell to cell. Infectivity experiments indicated that TGB1 separated on a different genomic RNA from TGB2 and TGB3 could function in limited cell-to-cell movement but that the rates of movement depended on the levels of expression of the proteins and the contexts in which they are expressed. Moreover, elevated expression of the wild-type TGB3 protein interfered with cell-to-cell movement but movement was not affected by the similar expression of a TGB3 mutant that fails to interact with TGB2. These experiments suggest that BSMV movement requires physical interactions of TGB2 and TGB3 and that substantial deviation from the TGB protein ratios expressed by the wild-type virus compromises movement.


Virology ◽  
1983 ◽  
Vol 129 (2) ◽  
pp. 344-349 ◽  
Author(s):  
A.A. Agranovsky ◽  
V.V. Dolja ◽  
J.G. Atabekov

Virology ◽  
1983 ◽  
Vol 127 (1) ◽  
pp. 1-14 ◽  
Author(s):  
V.V. Dolja ◽  
N.A. Lunina ◽  
R.-M. Leiser ◽  
T. Stanarius ◽  
S.N. Belzhelarskaya ◽  
...  

1986 ◽  
Vol 83 (14) ◽  
pp. 5043-5047 ◽  
Author(s):  
T. Meshi ◽  
M. Ishikawa ◽  
F. Motoyoshi ◽  
K. Semba ◽  
Y. Okada

1985 ◽  
Vol 152 (3) ◽  
pp. 625-631 ◽  
Author(s):  
Pim LINDHOUT ◽  
Lyda NEELEMAN ◽  
Hans TOL ◽  
Lous VLOTEN-DOTING

2005 ◽  
Vol 86 (6) ◽  
pp. 1827-1833 ◽  
Author(s):  
R. Koenig ◽  
S. Barends ◽  
A. P. Gultyaev ◽  
D.-E. Lesemann ◽  
H. J. Vetten ◽  
...  

The complete nucleotide sequence of the genomic RNA of the new virus Nemesia ring necrosis virus (NeRNV), which is widespread in various ornamental plant species belonging to the Scrophulariaceae and Verbenaceae, has been determined. Based on its gene content, the folding properties of its 5′-untranslated region and in vitro translation experiments, NeRNV RNA is a typical tymovirus RNA. Its 3′ end, however, differs greatly from those of the valine-specific tymoviral RNAs that have been analysed previously. It can be folded into an upstream pseudoknot domain and a histidine-specific tRNA-like structure, a combination that, so far, has been found only in tobamoviral RNAs. The identity elements found in NeRNV RNA for recognition by yeast histidyl-tRNA synthetase are more similar to those of yeast tRNAHis than the ones found in tobacco mosaic virus RNA. As a result NeRNV RNA can be charged with histidine even more efficiently than tobacco mosaic virus RNA.


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