scholarly journals Structural Properties of Carnation Mottle Virus p7 Movement Protein and Its RNA-binding Domain

2001 ◽  
Vol 276 (21) ◽  
pp. 18122-18129 ◽  
Author(s):  
Marçal Vilar ◽  
Vicent Esteve ◽  
Vicente Pallás ◽  
Jose F. Marcos ◽  
Enrique Pérez-Payá
Keyword(s):  
Structural Properties ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Mottle Virus ◽  
Rna Binding Domain ◽  
Carnation Mottle Virus

Transient Structural Ordering of the RNA-Binding Domain of Carnation Mottle Virus p7 Movement Protein Modulates Nucleic Acid Binding

ChemBioChem ◽  
2005 ◽  
Vol 6 (8) ◽  
pp. 1391-1396 ◽  
Author(s):  
Marçal Vilar ◽  
Ana Saurí ◽  
Jose F. Marcos ◽  
Ismael Mingarro ◽  
Enrique Pérez-Payá
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Mottle Virus ◽  
Nucleic Acid Binding ◽  
Structural Ordering ◽  
Rna Binding Domain ◽  
Carnation Mottle Virus

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 Mapping of the RNA-binding Domain of the Alfalfa Mosaic Virus Movement Protein

1994 ◽  
Vol 75 (11) ◽  
pp. 3199-3202 ◽  
Author(s):  
F. Schoumacher ◽  
C. Giovane ◽  
M. Maira ◽  
A. Poirson ◽  
T. Godefroy-Colburn ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Rna Binding ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Binding Domain ◽  
Virus Movement ◽  
Rna Binding Domain
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