Characterization of the nucleic acid binding activity of inner core protein VP6 of African horse sickness virus

2005 ◽  
Vol 150 (10) ◽  
pp. 2037-2050 ◽  
Author(s):  
P. J. de Waal ◽  
H. Huismans
Keyword(s):  
Nucleic Acid ◽  
Inner Core ◽  
Core Protein ◽  
Binding Activity ◽  
African Horse Sickness ◽  
Nucleic Acid Binding ◽  
African Horse Sickness Virus ◽  
Nucleic Acid Binding Activity

Crystallization of hepatitis B virus core protein shells: determination of cryoprotectant conditions and preliminary X-ray characterization

1999 ◽  
Vol 55 (2) ◽  
pp. 557-560 ◽  
Author(s):  
S. A. Wynne ◽  
A. G. W. Leslie ◽  
P. J. G. Butler ◽  
R. A. Crowther
Keyword(s):  
Hepatitis B Virus ◽  
Nucleic Acid ◽  
Hepatitis B ◽  
Inner Core ◽  
Core Protein ◽  
Sub Saharan Africa ◽  
Icosahedral Symmetry ◽  
Nucleic Acid Binding ◽  
Cell Parameters ◽  
B Virus

Hepatitis B virus causes liver cirrhosis and hepatocellular cancer and is a major cause of death, particularly in Asia and sub-Saharan Africa. The virus consists of an inner core or nucleocapsid, which encloses the viral nucleic acid, with an outer lipid envelope containing surface-antigen proteins. The core protein, when expressed in E. coli, assembles into spherical shells containing 180 or 240 subunits, arranged with T = 3 or T = 4 icosahedral symmetry. The C-terminal region of the protein is involved in nucleic acid binding, and deletion of this region does not prevent capsid formation. C-terminally deleted hepatitis B core shells containing 240 subunits have been crystallized and data has been collected to 3.6 Å resolution from frozen crystals, using butanediol as a cryoprotectant. The crystals have C2 symmetry, with unit-cell parameters a = 538.0, b = 353.0, c = 369.6 Å, β = 132.3°.

scholarly journals Investigating the Novel Nucleic Acid Binding Activity of Polybromo-1 Bromodomains

2020 ◽  
Vol 118 (3) ◽  
pp. 75a
Author(s):  
Saumya M. De Silva ◽  
Nicholas J. Schnicker ◽  
Catherine A. Musselman
Keyword(s):  
Nucleic Acid ◽  
Binding Activity ◽  
The Novel ◽  
Nucleic Acid Binding ◽  
Nucleic Acid Binding Activity

scholarly journals Structure and nucleic acid binding activity of the nucleoporin Nup157

2013 ◽  
Vol 110 (41) ◽  
pp. 16450-16455 ◽  
Author(s):  
H.-S. Seo ◽  
B. J. Blus ◽  
N. Z. Jankovic ◽  
G. Blobel
Keyword(s):  
Nucleic Acid ◽  
Binding Activity ◽  
Nucleic Acid Binding ◽  
Nucleic Acid Binding Activity

scholarly journals The Nucleic Acid Binding Activity of Bleomycin Hydrolase Is Involved in Bleomycin Detoxification

1998 ◽  
Vol 18 (6) ◽  
pp. 3580-3585 ◽  
Author(s):  
Wenjin Zheng ◽  
Stephen Albert Johnston
Keyword(s):  
Nucleic Acid ◽  
Binding Activity ◽  
Dual Function ◽  
Nucleic Acid Binding ◽  
Peptide Cleavage ◽  
Dna And Rna ◽  
Double Stranded Dna ◽  
Bleomycin Hydrolase ◽  
Nucleic Acid Binding Activity ◽  
Rna And Dna

ABSTRACT Yeast bleomycin hydrolase, Gal6p, is a cysteine peptidase that detoxifies the anticancer drug bleomycin. Gal6p is a dual-function protein capable of both nucleic acid binding and peptide cleavage. We now demonstrate that Gal6p exhibits sequence-independent, high-affinity binding to single-stranded DNA, nicked double-stranded DNA, and RNA. A region of the protein that is involved in binding both RNA and DNA substrates is delineated. Immunolocalization reveals that the Gal6 protein is chiefly cytoplasmic and thus may be involved in binding cellular RNAs. Variant Gal6 proteins that fail to bind nucleic acid also exhibit reduced ability to protect cells from bleomycin toxicity, suggesting that the nucleic acid binding activity of Gal6p is important in bleomycin detoxification and may be involved in its normal biological functions.

scholarly journals Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains

Molecules ◽  
2018 ◽  
Vol 23 (10) ◽  
pp. 2614 ◽  
Author(s):  
Tyler Weaver ◽  
Emma Morrison ◽  
Catherine Musselman
Keyword(s):  
Nucleic Acid ◽  
Molecular Mechanisms ◽  
Binding Activity ◽  
Nucleic Acid Binding ◽  
Post Translational Modification ◽  
Histone Proteins ◽  
Post Translational Modifications ◽  
Histone Binding ◽  
Functional Implications ◽  
Nucleic Acid Binding Activity

The eukaryotic genome is packaged into the cell nucleus in the form of chromatin, a complex of genomic DNA and histone proteins. Chromatin structure regulation is critical for all DNA templated processes and involves, among many things, extensive post-translational modification of the histone proteins. These modifications can be “read out” by histone binding subdomains known as histone reader domains. A large number of reader domains have been identified and found to selectively recognize an array of histone post-translational modifications in order to target, retain, or regulate chromatin-modifying and remodeling complexes at their substrates. Interestingly, an increasing number of these histone reader domains are being identified as also harboring nucleic acid binding activity. In this review, we present a summary of the histone reader domains currently known to bind nucleic acids, with a focus on the molecular mechanisms of binding and the interplay between DNA and histone recognition. Additionally, we highlight the functional implications of nucleic acid binding in chromatin association and regulation. We propose that nucleic acid binding is as functionally important as histone binding, and that a significant portion of the as yet untested reader domains will emerge to have nucleic acid binding capabilities.

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