scholarly journals In VivoDetection, RNA-Binding Properties and Characterization of the RNA-Binding Domain of the p7 Putative Movement Protein from Carnation Mottle Carmovirus (CarMV)

Virology ◽  
1999 ◽  
Vol 255 (2) ◽  
pp. 354-365 ◽  
Author(s):  
Jose F. Marcos ◽  
Marçal Vilar ◽  
Enrique Pérez-Payá ◽  
Vicente Pallás
Keyword(s):  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Binding Properties ◽  
Properties And Characterization ◽  
Putative Movement Protein ◽  
Rna Binding Domain

scholarly journals Characterization of an RNA-binding domain in the bacteriophage phi 29 connector.

1993 ◽  
Vol 268 (27) ◽  
pp. 20198-20204
Author(s):  
L.E. Donate ◽  
J.M. Valpuesta ◽  
C Mier ◽  
F Rojo ◽  
J.L. Carrascosa
Keyword(s):  
Rna Binding ◽  
Binding Domain ◽  
Rna Binding Domain

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.

Isolation and Characterization of WHI3, a Size-Control Gene of Saccharomyces cerevisiae

Genetics ◽  
2001 ◽  
Vol 157 (4) ◽  
pp. 1469-1480 ◽  
Author(s):  
R S Nash ◽  
T Volpe ◽  
B Futcher
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Binding ◽  
Size Control ◽  
Binding Domain ◽  
Small Cells ◽  
Yeast Saccharomyces Cerevisiae ◽  
Isolation And Characterization ◽  
Rna Binding Domain ◽  
Mating Factor

Abstract WHI3 is a gene affecting size control and cell cycle in the yeast Saccharomyces cerevisiae. The whi3 mutant has small cells, while extra doses of WHI3 produce large cells, and a large excess of WHI3 produces a lethal arrest in G1 phase. WHI3 seems to be a dose-dependent inhibitor of Start. Whi3 and its partially redundant homolog Whi4 have an RNA-binding domain, and mutagenesis experiments indicate that this RNA-binding domain is essential for Whi3 function. CLN3-1 whi3 cells are extremely small, nearly sterile, and largely nonresponsive to mating factor. Fertility is restored by deletion of CLN2, suggesting that whi3 cells may have abnormally high levels of CLN2 function.

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
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