scholarly journals Protein–protein- and protein–RNA-binding properties of the movement protein and VP25 coat protein of Apple latent spherical virus

Virology ◽  
2006 ◽  
Vol 352 (1) ◽  
pp. 178-187 ◽  
Author(s):  
Masamichi Isogai ◽  
Kentaro Watanabe ◽  
Yusuke Uchidate ◽  
Nobuyuki Yoshikawa
Keyword(s):  
Coat Protein ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Properties ◽  
Apple Latent Spherical Virus

scholarly journals Potato virus X RNA-mediated assembly of single-tailed ternary ‘coat protein–RNA–movement protein’ complexes

2006 ◽  
Vol 87 (9) ◽  
pp. 2731-2740 ◽  
Author(s):  
O. V. Karpova ◽  
O. V. Zayakina ◽  
M. V. Arkhipenko ◽  
E. V. Sheval ◽  
O. I. Kiselyova ◽  
...  
Keyword(s):  
Coat Protein ◽  
Potato Virus ◽  
Rna Binding ◽  
Movement Protein ◽  
Infected Plant ◽  
Potato Virus X ◽  
Translation System ◽  
Transport Form

Different models have been proposed for the nature of the potexvirus transport form that moves from cell to cell over the infected plant: (i) genomic RNA moves as native virions; or (ii) in vitro-assembled non-virion ribonucleoprotein (RNP) complexes consisting of viral RNA, coat protein (CP) and movement protein (MP), termed TGBp1, serve as the transport form in vivo. As the structure of these RNPs has not been elucidated, the products assembled in vitro from potato virus X (PVX) RNA, CP and TGBp1 were characterized. The complexes appeared as single-tailed particles (STPs) with a helical, head-like structure composed of CP subunits located at the 5′-proximal region of PVX RNA; the TGBp1 was bound to the terminal CP molecules of the head. Remarkably, no particular non-virion RNP complexes were observed. These data suggest that the CP–RNA interactions resulting in head formation prevailed over TGBp1–RNA binding upon STP assembly from RNA, CP and TGBp1. STPs could be assembled from the 5′ end of PVX RNA and CP in the absence of TGBp1. The translational ability of STPs was characterized in a cell-free translation system. STPs lacking TGBp1 were entirely non-translatable; however, they were rendered translatable by binding of TGBp1 to the end of the head. It is suggested that the RNA-mediated assembly of STPs proceeds via two steps. Firstly, non-translatable CP–RNA STPs are produced, due to encapsidation of the 5′-terminal region. Secondly, the TGBp1 molecules bind to the end of a polar head, resulting in conversion of the STPs into a translatable form.

scholarly journals RNA binding properties of the coat protein from bacteriophage GA

1991 ◽  
Vol 19 (23) ◽  
pp. 6499-6503 ◽  
Author(s):  
Jonatha M. Gott ◽  
Larry J. Wilhelm ◽  
C. Uhlenbeck Olke
Keyword(s):  
Coat Protein ◽  
Rna Binding ◽  
Binding Properties

scholarly journals Mapping the RNA-binding domain on the Apple chlorotic leaf spot virus movement protein

2005 ◽  
Vol 86 (1) ◽  
pp. 225-229 ◽  
Author(s):  
Masamichi Isogai ◽  
Nobuyuki Yoshikawa
Keyword(s):  
Leaf Spot ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Sequence Specificity ◽  
Nucleic Acid Binding ◽  
Spot Virus ◽  
Uv Crosslinking ◽  
Chlorotic Leaf ◽  
Rna Binding Domain

The RNA-binding properties of the cell-to-cell movement protein (MP) of Apple chlorotic leaf spot virus were analysed. MP was expressed in Escherichia coli and was used in UV-crosslinking analysis, using a digoxigenin–UTP-labelled RNA probe and gel-retardation analysis. The analyses demonstrated that MP bound cooperatively to single-stranded RNA (ssRNA). When analysed for NaCl dependence of the RNA-binding activity, the majority of the MP could bind ssRNA even in binding buffer with 1 M NaCl. Furthermore, competition binding experiments showed that the MP bound preferentially to ssRNA and single-stranded DNA without sequence specificity. MP deletion mutants were used to identify the RNA-binding domain by UV-crosslinking analysis. Amino acid residues 82–126 and 127–287 potentially contain two independently active, single-stranded nucleic acid-binding domains.

scholarly journals A Survey of Resistance to Tomato bushy stunt virus in the Genus Nicotiana Reveals That the Hypersensitive Response Is Triggered by One of Three Different Viral Proteins

2013 ◽  
Vol 26 (2) ◽  
pp. 240-248 ◽  
Author(s):  
Carlos A. Angel ◽  
James E. Schoelz
Keyword(s):  
Coat Protein ◽  
Hypersensitive Response ◽  
Rna Silencing ◽  
Mutational Analysis ◽  
Movement Protein ◽  
Viral Proteins ◽  
Tomato Bushy Stunt Virus ◽  
Necrosis Virus ◽  
Nicotiana Glutinosa ◽  
Cucumber Necrosis Virus

In this study, we screened 22 Nicotiana spp. for resistance to the tombusviruses Tomato bushy stunt virus (TBSV), Cucumber necrosis virus, and Cymbidium ringspot virus. Eighteen species were resistant, and resistance was manifested in at least two different categories. In all, 13 species responded with a hypersensitive response (HR)-type resistance, whereas another five were resistant but either had no visible response or responded with chlorotic lesions rather than necrotic lesions. Three different TBSV proteins were found to trigger HR in Nicotiana spp. in an agroinfiltration assay. The most common avirulence (avr) determinant was the TBSV coat protein P41, a protein that had not been previously recognized as an avr determinant. A mutational analysis confirmed that the coat protein rather than the viral RNA sequence was responsible for triggering HR, and it triggered HR in six species in the Alatae section. The TBSV P22 movement protein triggered HR in two species in section Undulatae (Nicotiana glutinosa and N. edwardsonii) and one species in section Alatae (N. forgetiana). The TBSV P19 RNA silencing suppressor protein triggered HR in sections Sylvestres (N. sylvestris), Nicotiana (N. tabacum), and Alatae (N. bonariensis). In general, Nicotiana spp. were capable of recognizing only one tombusvirus avirulence determinant, with the exceptions of N. bonariensis and N. forgetiana, which were each able to recognize P41, as well as P19 and P22, respectively. Agroinfiltration failed to detect the TBSV avr determinants responsible for triggering HR in N. arentsii, N. undulata, and N. rustica. This study illustrates the breadth and variety of resistance responses to tombusviruses that exists in the Nicotiana genus.

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