A low-temperature-responsive gene from barley encodes a protein with single-stranded nucleic acid-binding activity which is phosphorylated in vitro

1996 ◽  
Vol 30 (5) ◽  
pp. 947-959 ◽  
Author(s):  
M. Alison Dunn ◽  
Kate Brown ◽  
Robert Lightowlers ◽  
Monica A. Hughes
Keyword(s):  
Nucleic Acid ◽  
Low Temperature ◽  
Binding Activity ◽  
Nucleic Acid Binding ◽  
Temperature Responsive ◽  
Responsive Gene ◽  
Nucleic Acid Binding Activity

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.

scholarly journals Nucleic Acid Binding Activity of Pns6 Encoded by Genome Segment 6 of Rice Ragged Stunt Oryzavirus

2004 ◽  
Vol 36 (7) ◽  
pp. 457-466 ◽  
Author(s):  
Chao-Gang Shao ◽  
Hui-Juan Lü ◽  
Jian-Hua Wu ◽  
Zu-Xun Gong
Keyword(s):  
Nucleic Acid ◽  
Western Blotting ◽  
Subcellular Fractionation ◽  
Binding Activity ◽  
Genome Segment ◽  
Nucleic Acid Binding ◽  
Structural Protein ◽  
Mobility Shift ◽  
Dna And Rna ◽  
Nucleic Acid Binding Activity

Abstract The ORF of genome segment 6 (S6) of rice ragged stunt oryzavirus (RRSV) Philippines isolate was cloned and sequenced based on the S6 sequence of the Thailand isolate. Pns6, the 71 kD product of S6 expressed in E. coli, was demonstrated to be a viral non-structural protein of RRSV by Western blotting. The gel mobility shift assays showed that Pns6 had nucleic acid binding activity. Pns6 could interact with single-and double-stranded forms of DNA and RNA, showing a preference for single-stranded nucleic acid and a slight preference for RRSV ssRNA over the rice ssRNA, as demonstrated by both competition and displacement assays. The binding of Pns6 to nucleic acids is strong and sequence non-specific. By using five truncated derivatives of Pns6, it was found that the basic region from amino acid 201 to 273 of Pns6 was the unique nucleic acid binding domain. Subcellular fractionation of leaf tissues of RRSV-infected rice plants and subsequent Western blotting had shown that Pns6 accumulated predominately in the cytoplasmic membrane fraction. The possible role of RRSV Pns6 in virus replication and assembly is discussed.

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