A new visible-light-driven photoelectrochemical biosensor for probing DNA–protein interactions

2015 ◽  
Vol 51 (39) ◽  
pp. 8381-8384 ◽  
Author(s):  
Zheng-Yuan Ma ◽  
Yi-Fan Ruan ◽  
Nan Zhang ◽  
Wei-Wei Zhao ◽  
Jing-Juan Xu ◽  
...  
Keyword(s):  
Dna Binding ◽  
Visible Light ◽  
Protein Interactions ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Dna Interaction ◽  
Visible Light Driven ◽  
Photoelectrochemical Biosensor ◽  
Dna Protein Interactions

A novel photoelectrochemical approach was achieved for the detection of a DNA binding protein via the protein–DNA interaction.

scholarly journals HDAC inhibitor Givinostat targets DNA-binding of human CGGBP1

2020 ◽  
Author(s):  
Manthan Patel ◽  
Divyesh Patel ◽  
Subhamoy Datta ◽  
Umashankar Singh
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Histone Deacetylases ◽  
Antineoplastic Agent ◽  
Dna Binding Protein ◽  
Dna Interaction ◽  
Cancer Cell Proliferation ◽  
Screening Assay ◽  
Chemical Inhibitors ◽  
Simple Screening

ABSTRACTThe antineoplastic agent Givinostat inhibits histone deacetylases. We present here our finding that the DNA-binding of human CGGBP1 is also inhibited by Givinostat. CGGBP1, a DNA-binding protein, is required for cancer cell proliferation. In our quest to exploit the potential anti-proliferative effects of CGGBP1 inhibition, we have developed a simple screening assay to identify chemical inhibitors of DNA-protein interactions. We have applied this screen for human CGGBP1 on a library of 1685 compounds and found that Givinostat is a direct inhibitor of CGGBP1-DNA interaction. The mechanism of action of Givinostat should thus extend beyond HDACs to include the inhibition of the myriad functions of CGGBP1 that depend on its binding to the DNA.

scholarly journals HDAC inhibitor Givinostat targets DNA-binding of human CGGBP1

2020 ◽  
Author(s):  
Manthan Patel ◽  
Divyesh Patel ◽  
Subhamoy Datta ◽  
Umashankar Singh
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Histone Deacetylases ◽  
Antineoplastic Agent ◽  
Dna Binding Protein ◽  
Dna Interaction ◽  
Cancer Cell Proliferation ◽  
Screening Assay ◽  
Chemical Inhibitors ◽  
Simple Screening

Abstract The antineoplastic agent Givinostat inhibits histone deacetylases. We present here our finding that the DNA-binding of human CGGBP1 is also inhibited by Givinostat. CGGBP1, a DNA-binding protein, is required for cancer cell proliferation. In our quest to exploit the potential anti-proliferative effects of CGGBP1 inhibition, we have developed a simple screening assay to identify chemical inhibitors of DNA-protein interactions. We have applied this screen for human CGGBP1 on a library of 1685 compounds and found that Givinostat is a direct inhibitor of CGGBP1-DNA interaction. The mechanism of action of Givinostat should thus extend beyond HDACs to include the inhibition of the myriad functions of CGGBP1 that depend on its binding to the DNA.

scholarly journals Structure–function relationships of the competence lipoprotein ComL and SSB in meningococcal transformation

Microbiology ◽  
2011 ◽  
Vol 157 (5) ◽  
pp. 1329-1342 ◽  
Author(s):  
Afsaneh V. Benam ◽  
Emma Lång ◽  
Kristian Alfsnes ◽  
Burkhard Fleckenstein ◽  
Alexander D. Rowe ◽  
...  
Keyword(s):  
Dna Binding ◽  
Outer Membrane ◽  
Solid Phase ◽  
Binding Protein ◽  
3D Models ◽  
Dna Binding Protein ◽  
Dna Interaction ◽  
Direct Role ◽  
Exogenous Dna ◽  
Ms Analysis

Neisseria meningitidis, the meningococcus, is naturally competent for transformation throughout its growth cycle. The uptake of exogenous DNA into the meningococcus cell during transformation is a multi-step process. Beyond the requirement for type IV pilus expression for efficient transformation, little is known about the neisserial proteins involved in DNA binding, uptake and genome integration. This study aimed to identify and characterize neisserial DNA binding proteins in order to further elucidate the multi-factorial transformation machinery. The meningococcus inner membrane and soluble cell fractions were searched for DNA binding components by employing 1D and 2D gel electrophoresis approaches in combination with a solid-phase overlay assay with DNA substrates. Proteins that bound DNA were identified by MS analysis. In the membrane fraction, multiple components bound DNA, including the neisserial competence lipoprotein ComL. In the soluble fraction, the meningococcus orthologue of the single-stranded DNA binding protein SSB was predominant. The DNA binding activity of the recombinant ComL and SSB proteins purified to homogeneity was verified by electromobility shift assay, and the ComL–DNA interaction was shown to be Mg2+-dependent. In 3D models of the meningococcus ComL and SSB predicted structures, potential DNA binding sites were suggested. ComL was found to co-purify with the outer membrane, directly interacting with the secretin PilQ. The combined use of 1D/2D solid-phase overlay assays with MS analysis was a useful strategy for identifying DNA binding components. The ComL DNA binding properties and outer membrane localization suggest that this lipoprotein plays a direct role in neisserial transformation, while neisserial SSB is a DNA binding protein that contributes to the terminal part of the transformation process.

Protein-Protein Interactions between the Escherichia coli Single-Stranded DNA-Binding Protein and Exonuclease I

1996 ◽  
Vol 145 (5) ◽  
pp. 619 ◽  
Author(s):  
Margarita Sandigursky ◽  
Frances Mendez ◽  
Robert E. Bases ◽  
Tomohiro Matsumoto ◽  
William A. Franklin
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Protein Interactions ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Protein Protein Interactions ◽  
Single Stranded Dna ◽  
Exonuclease I

scholarly journals HDAC inhibitor Givinostat targets DNA-binding of human CGGBP1

2020 ◽  
Author(s):  
Manthan Patel ◽  
Divyesh Patel ◽  
Subhamoy Datta ◽  
Umashankar Singh
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Histone Deacetylases ◽  
Antineoplastic Agent ◽  
Dna Binding Protein ◽  
Dna Interaction ◽  
Cancer Cell Proliferation ◽  
Screening Assay ◽  
Chemical Inhibitors ◽  
Simple Screening

Abstract The antineoplastic agent Givinostat inhibits histone deacetylases. We present here our finding that the DNA-binding of human CGGBP1 is also inhibited by Givinostat. CGGBP1, a DNA-binding protein, is required for cancer cell proliferation. In our quest to exploit the potential anti-proliferative effects of CGGBP1 inhibition, we have developed a simple screening assay to identify chemical inhibitors of DNA-protein interactions. We have applied this screen for human CGGBP1 on a library of 1685 compounds and found that Givinostat is a direct inhibitor of CGGBP1-DNA interaction. The mechanism of action of Givinostat should thus extend beyond HDACs to include the inhibition of the myriad functions of CGGBP1 that depend on its binding to the DNA.

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