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 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.

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 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 Assessing nucleic acid binding activity of four dinoflagellate cold shock domain proteins from Symbiodinium kawagutii and Lingulodinium polyedra

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Bahareh Zaheri ◽  
David Morse
Keyword(s):  
Transcription Factors ◽  
Nucleic Acid ◽  
Transcriptional Control ◽  
Cold Shock ◽  
Binding Activity ◽  
Dependent Manner ◽  
Nucleic Acid Binding ◽  
Mobility Shift ◽  
Double Stranded Dna ◽  
Cold Shock Domain

Abstract Background Dinoflagellates have a generally large number of genes but only a small percentage of these are annotated as transcription factors. Cold shock domain (CSD) containing proteins (CSPs) account for roughly 60% of these. CSDs are not prevalent in other eukaryotic lineages, perhaps suggesting a lineage-specific expansion of this type of transcription factors in dinoflagellates, but there is little experimental data to support a role for dinoflagellate CSPs as transcription factors. Here we evaluate the hypothesis that dinoflagellate CSPs can act as transcription factors by binding double-stranded DNA in a sequence dependent manner. Results We find that both electrophoretic mobility shift assay (EMSA) competition experiments and selection and amplification binding (SAAB) assays indicate binding is not sequence specific for four different CSPs from two dinoflagellate species. Competition experiments indicate all four CSPs bind to RNA better than double-stranded DNA. Conclusion Dinoflagellate CSPs do not share the nucleic acid binding properties expected for them to function as bone fide transcription factors. We conclude the transcription factor complement of dinoflagellates is even smaller than previously thought suggesting that dinoflagellates have a reduced dependance on transcriptional control compared to other eukaryotes.

Sign in / Sign up

Export Citation Format

Share Document