Synthesis and in vitro biochemical properties, DNA binding and DNA cleavage ability of copper complexes of hydroxyflavone derivatives of novel organosulfur compounds as therapeutic agent

2021 ◽  
pp. 1-39
Author(s):  
B. Ebenezer ◽  
K. Nagashri
Keyword(s):  
Dna Binding ◽  
Dna Cleavage ◽  
Copper Complexes ◽  
Therapeutic Agent ◽  
Biochemical Properties ◽  
Organosulfur Compounds ◽  
Derivatives Of

New binuclear Ni(ii) metallates containing ONS chelators: synthesis, characterisation, DNA binding, DNA cleavage, protein binding, antioxidant activity, antimicrobial and in vitro cytotoxicity

2017 ◽  
Vol 41 (7) ◽  
pp. 2543-2560 ◽  
Author(s):  
G. Kalaiarasi ◽  
Ruchi Jain ◽  
H. Puschman ◽  
S. Poorna Chandrika ◽  
K. Preethi ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Dna Binding ◽  
Protein Binding ◽  
Hela Cell ◽  
Antiproliferative Activity ◽  
Dna Cleavage ◽  
In Vitro Cytotoxicity ◽  
Hela Cell Lines ◽  
Mcf 7

Four new binuclear nickel(ii) metallates showed promising antiproliferative activity against MCF-7 and HeLa cell lines and were much less toxic against HaCaT.

scholarly journals Differential biochemical properties of three canonical Dps proteins from the cyanobacterium Nostoc punctiforme suggest distinct cellular functions

2018 ◽  
Vol 293 (43) ◽  
pp. 16635-16646 ◽  
Author(s):  
Christoph Howe ◽  
Felix Ho ◽  
Anja Nenninger ◽  
Patrícia Raleiras ◽  
Karin Stensjö
Keyword(s):  
Dna Binding ◽  
Iron Oxidation ◽  
Gel Filtration ◽  
Biochemical Property ◽  
Biochemical Properties ◽  
Oxidation Catalysis ◽  
Nostoc Punctiforme ◽  
Experimental Conditions ◽  
Specific Expression

DNA-binding proteins from starved cells (Dps, EC: 1.16.3.1) have a variety of different biochemical activities such as DNA-binding, iron sequestration, and H2O2 detoxification. Most bacteria commonly feature one or two Dps enzymes, whereas the cyanobacterium Nostoc punctiforme displays an unusually high number of five Dps proteins (NpDps1–5). Our previous studies have indicated physiological differences, as well as cell-specific expression, among these five proteins. Three of the five NpDps proteins, NpDps1, -2, and -3, were classified as canonical Dps proteins. To further investigate their properties and possible importance for physiological function, here we characterized and compared them in vitro. Nondenaturing PAGE, gel filtration, and dynamic light-scattering experiments disclosed that the three NpDps proteins exist as multimeric protein species in the bacterial cell. We also demonstrate Dps-mediated iron oxidation catalysis in the presence of H2O2. However, no iron oxidation with O2 as the electron acceptor was detected under our experimental conditions. In modeled structures of NpDps1, -2, and -3, protein channels were identified that could serve as the entrance for ferrous iron into the dodecameric structures. Furthermore, we could demonstrate pH-dependent DNA-binding properties for NpDps2 and -3. This study adds critical insights into the functions and stabilities of the three canonical Dps proteins from N. punctiforme and suggests that each of the Dps proteins within this bacterium has a specific biochemical property and function.

scholarly journals Hin Recombinase Mutants Functionally Disrupted in Interactions with Fis

2001 ◽  
Vol 183 (1) ◽  
pp. 28-35 ◽  
Author(s):  
Oliver Z. Nanassy ◽  
Kelly T. Hughes
Keyword(s):  
Dna Binding ◽  
Dna Cleavage ◽  
Genetic Screen ◽  
Recombination Reaction ◽  
Genetic Classification ◽  
Hin Recombinase

ABSTRACT A previous genetic screen was designed to separate Hin recombinase mutants into distinct classes based on the stage in the recombination reaction at which they are blocked (O. Nanassy, Zoltan, and K. T. Hughes, Genetics 149:1649–1663, 1998). One class of DNA binding-proficient, recombination-deficient mutants was predicted by genetic classification to be defective in the step prior to invertasome formation. Based on the genetic criteria, mutants from this class were also inferred to be defective in interactions with Fis. In order to understand how the genetic classification relates to individual biochemical steps in the recombination reaction these mutants, R123Q, T124I, and A126T, were purified and characterized for DNA cleavage and recombination activities. Both the T124I and A126T mutants were partially active, whereas the R123Q mutant was inactive. The A126T mutant was not as defective for recombination as the T124I allele and could be partially rescued for recombination both in vivo and in vitro by increasing the concentration of Fis protein. Rescue of the A126T allele required the Fis protein to be DNA binding proficient. A model for a postsynaptic role for Fis in the inversion reaction is presented.

scholarly journals An amino-terminal c-myc domain required for neoplastic transformation activates transcription.

1990 ◽  
Vol 10 (11) ◽  
pp. 5914-5920 ◽  
Author(s):  
G J Kato ◽  
J Barrett ◽  
M Villa-Garcia ◽  
C V Dang
Keyword(s):  
Dna Binding ◽  
Leucine Zipper ◽  
Nuclear Dna ◽  
Neoplastic Transformation ◽  
Biochemical Properties ◽  
Regulatory Function ◽  
Ras Gene ◽  
Amino Terminal

The product of the c-myc proto-oncogene is a nuclear phosphoprotein whose normal cellular function has not yet been defined. c-Myc has a number of biochemical properties, however, that suggest that it may function as a potential regulator of gene transcription. Specifically, it is a nuclear DNA-binding protein with a short half-life, a high proline content, segments that are rich in glutamine and acidic residues, and a carboxyl-terminal oligomerization domain containing the leucine zipper and helix-loop-helix motifs that serve as oligomerization domains in known regulators of transcription, such as C/EBP, Jun, Fos, GCN4, MyoD, E12, and E47. In an effort to establish that c-Myc might regulate transcription in vivo, we sought to determine whether regions of the c-Myc protein could activate transcription in an in vitro system. We report here that fusion proteins in which segments of human c-Myc are linked to the DNA-binding domain of the yeast transcriptional activator GAL4 can activate transcription from a reporter gene linked to GAL4-binding sites. Three independent activation regions are located between amino acids 1 and 143, a region that has been shown to be required for neoplastic transformation of primary rat embryo cells in cooperation with a mutated ras gene. These results demonstrate that domains of the c-Myc protein can function to regulate transcription in a model system and suggest that alterations of Myc transcriptional regulatory function may lead to neoplastic transformation.

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