A novel polynuclear Cu(i)–sulfur cluster with 1,2-dithiolate-o-carborane ligands as a potential in vitro antitumour agent and its DNA binding properties

2013 ◽  
Vol 42 (14) ◽  
pp. 4777 ◽  
Author(s):  
Zhong Han ◽  
Jin Jiang ◽  
Jing Lu ◽  
Dacheng Li ◽  
Shuang Cheng ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Properties ◽  
Sulfur Cluster ◽  
Antitumour Agent ◽  
Dna Binding Properties

Synthesis and DNA-binding Properties of a Cationic Seven-coordinate Manganese(II) Complex Formed with the Tripodal Ligand Tris(Nmethylbenzimidazol- 2-ylmethyl)amine and Salicylate

2012 ◽  
Vol 67 (8) ◽  
pp. 819-826 ◽  
Author(s):  
Huilu Wu ◽  
Ying Bai ◽  
Jingkun Yuan ◽  
Hua Wang ◽  
Guolong Pan ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Mode ◽  
X Ray Diffraction ◽  
Binding Properties ◽  
Tripodal Ligand ◽  
Spectrophotometric Methods ◽  
Physico Chemical ◽  
Dna Binding Properties ◽  
Hydroxyl Radical Scavenge

A ternary cationic Mn(II) complex with the tripodal ligand tris(2-(N-methyl) benzimidazylmethyl)amine (Mentb), salicylate and DMF as ligands and nitrate as counterion, [Mn(Mentb)(salicylate)DMF](NO3), was synthesized and characterized by physico-chemical and spectroscopic methods. The crystal structure of the Mn(II) complex has been determined by single-crystal X-ray diffraction and revealed that the central Mn(II) atom is seven-coordinated. The DNA-binding properties of the Mn(II) complex were investigated by spectrophotometric methods and viscosity measurements, and the results suggest that the Mn(II) complex binds to DNA via an intercalation binding mode. Additionally, the complex exhibited potential hydroxyl radical scavenge properties in in vitro studies

Synthesis, Crystal Structure, DNA-binding Properties and Antioxidant Activities of a Lutetium(III) Complex with the Bis(N-salicylidene)-3- oxapentane-1,5-diamine Ligand

2013 ◽  
Vol 68 (3) ◽  
pp. 257-266 ◽  
Author(s):  
Guolong Pan ◽  
Yuchen Bai ◽  
Hua Wang ◽  
Jin Kong ◽  
Furong Shi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Antioxidant Activities ◽  
Radical Scavenging ◽  
Binding Mode ◽  
Binding Properties ◽  
Metal Centers ◽  
Spectrophotometric Methods ◽  
Dna Binding Properties

A Schiff base ligand bis(N-salicylidene)-3-oxapentane-1,5-diamine (H2L) and its lutetium(III) complex, with composition Lu2(L)2(NO3)2, were synthesized and characterized by physico-chemical and spectroscopic methods. The crystal structure of the Lu(III) complex has been determined by single-crystal X-ray diffraction. It reveals a centrosymmetric binuclear neutral entity where Lu(III) metal centers are bridged by two phenoxo oxygen atoms. The DNA-binding properties of the Lu(III) complex were investigated by spectrophotometric methods and viscosity measurements, and the results suggest that the Lu(III) complex binds to DNA via a groove binding mode. Additionally, the antioxidant activity of the Lu(III) complex was determined by the superoxide and hydroxyl radical scavenging methods in vitro, which indicate that it is a scavenger for OH· and O-· 2 radicals.

scholarly journals Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway.

1993 ◽  
Vol 13 (4) ◽  
pp. 1983-1997 ◽  
Author(s):  
A Nakai ◽  
R I Morimoto
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Dna Binding ◽  
Heat Shock Transcription Factor ◽  
Heat Shock Gene ◽  
Regulatory Sequences ◽  
Regulatory Pathway ◽  
Binding Properties ◽  
Dna Binding Properties

We have cloned three avian heat shock transcription factor (HSF) genes corresponding to a novel factor, HSF3, and the avian homologs of mammalian HSF1 and HSF2. The predicted amino acid sequence of HSF3 is approximately 40% related to the sequence of HSF1 and HSF2. The sequences for all three factors exhibit extensive identify in the DNA binding motifs and the heptad repeats of hydrophobic amino acids which are common to all eukaryotic HSFs. Despite these overall similarities, each avian HSF exhibits distinct DNA binding properties. HSF2 when expressed in vitro binds constitutively to the heat shock element promoter sequence, whereas neither HSF1 nor HSF3 expressed in vitro binds to DNA. HSF1 DNA binding is induced upon heat shock or treatment with nonionic detergents, whereas the DNA binding properties of HSF3 are not induced by these conditions in vitro. These results suggest that HSF3 activation may involve an induction pathway distinct from the traditional forms of heat shock gene induction. HSF3 DNA binding activity, however, is obtained when the carboxyl-terminal region including the distal heptad repeat is deleted, indicating the presence of negative cis-regulatory sequences. The HSF3 message, like HSF1 and HSF2 messages, is coexpressed during development and in most tissues, which suggests a general role for the regulatory pathway involving HSF3.

Hox proteins have different affinities for a consensus DNA site that correlate with the positions of their genes on the hox cluster

1994 ◽  
Vol 14 (7) ◽  
pp. 4532-4545
Author(s):  
I Pellerin ◽  
C Schnabel ◽  
K M Catron ◽  
C Abate
Keyword(s):  
Dna Binding ◽  
Target Genes ◽  
Hox Genes ◽  
Regulatory Elements ◽  
Binding Properties ◽  
Hox Proteins ◽  
Hox Cluster ◽  
Dna Binding Properties

The hox genes, members of a family of essential developmental regulators, have the intriguing property that their expression in the developing murine embryo is colinear with their chromosomal organization. Members of the hox gene family share a conserved DNA binding domain, termed the homeodomain, which mediates interactions of Hox proteins with DNA regulatory elements in the transcriptional control regions of target genes. In this study, we characterized the DNA binding properties of five representative members of the Hox family: HoxA5, HoxB4, HoxA7, HoxC8, and HoxB1. To facilitate a comparative analysis of their DNA binding properties, we produced the homeodomain regions of these Hox proteins in Escherichia coli and obtained highly purified polypeptides. We showed that these Hox proteins interact in vitro with a common consensus DNA site that contains the motif (C/G)TAATTG. We further showed that the Hox proteins recognize the consensus DNA site in vivo, as determined by their ability to activate transcription through this site in transient transfection assays. Although they interact optimally with the consensus DNA site, the Hox proteins exhibit subtle, but distinct, preferences for DNA sites that contain variations of the nucleotides within the consensus motif. In addition to their modest differences in DNA binding specificities, the Hox proteins also vary in their relative affinities for DNA. Intriguingly, their relative affinities correlate with the positions of their respective genes on the hox cluster. These findings suggest that subtle differences in DNA binding specificity combined with differences in DNA binding affinity constitute features of the "Hox code" that contribute to the selective functions of Hox proteins during murine embryogenesis.

The in vitro DNA binding properties of NDP kinase are related to its oligomeric state

FEBS Letters ◽  
1997 ◽  
Vol 418 (1-2) ◽  
pp. 53-57 ◽  
Author(s):  
Sébastien Mesnildrey ◽  
Fabrice Agou ◽  
Michel Véron
Keyword(s):  
Dna Binding ◽  
Ndp Kinase ◽  
Oligomeric State ◽  
Binding Properties ◽  
Dna Binding Properties
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