scholarly journals Azidophenyl as a click-transformable redox label of DNA suitable for electrochemical detection of DNA–protein interactions

2015 ◽  
Vol 6 (1) ◽  
pp. 575-587 ◽  
Author(s):  
Jana Balintová ◽  
Jan Špaček ◽  
Radek Pohl ◽  
Marie Brázdová ◽  
Luděk Havran ◽  
...  
Keyword(s):  
Electrochemical Detection ◽  
Protein Interactions ◽  
Click Reaction ◽  
Redox Label ◽  
Dna Protein Interactions

A new azido-based DNA redox label which can be transformed into nitrophenyltriazole by a CuAAC click reaction was developed. It was used for the mapping of DNA–protein interactions with electrochemical detection.

Tail labelled oligonucleotide probes for the detection of DNA-protein interactions

2011 ◽  
Author(s):  
Hana Pivoňková ◽  
Kateřina Němcová ◽  
Petra Horáková ◽  
Luděk Havran ◽  
Hana Macíčková-Cahová ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Oligonucleotide Probes ◽  
Dna Protein Interactions

Multiple DNA-protein interactions at the CpG island of the human pseudoautosomal geneMIC2

1993 ◽  
Vol 19 (1) ◽  
pp. 51-63 ◽  
Author(s):  
A. Braghetti ◽  
G. Piazzi ◽  
L. Lanfranco ◽  
C. Mondello
Keyword(s):  
Protein Interactions ◽  
Cpg Island ◽  
Dna Protein Interactions

scholarly journals A yeast one-hybrid system to detect methylation-dependent DNA–protein interactions

2004 ◽  
Vol 313 (4) ◽  
pp. 922-925 ◽  
Author(s):  
Shu-Ying Feng ◽  
Kazuhisa Ota ◽  
Yoichi Yamada ◽  
Norio Sawabu ◽  
Takashi Ito
Keyword(s):  
Hybrid System ◽  
Protein Interactions ◽  
Dna Protein Interactions

scholarly journals In vivo analysis of DNA-protein interactions on the human erythropoietin enhancer.

1997 ◽  
Vol 17 (2) ◽  
pp. 851-856 ◽  
Author(s):  
B Hu ◽  
E Wright ◽  
L Campbell ◽  
K L Blanchard
Keyword(s):  
Oxygen Tension ◽  
Protein Interactions ◽  
Proximal Promoter ◽  
Low Oxygen ◽  
Initiation Rate ◽  
Cobalt Exposure ◽  
In Cells ◽  
Dna Protein Interactions

The erythropoietin (EPO) gene is one of the best examples of a mammalian gene controlled by oxygen tension. The DNA elements responsible for hypoxia-induced transcription consist of a short region of the proximal promoter and a <50-bp 3' enhancer. The elements act cooperatively to increase the transcriptional initiation rate approximately 100-fold in response to low oxygen tension in Hep3B cells. Two distinct types of transactivating proteins have been demonstrated to bind the response elements in the human EPO enhancer in vitro: one shows hypoxia-inducible DNA binding activity, while the other activity binds DNA under normoxic and hypoxic conditions. We have investigated the DNA-protein interactions on the human EPO enhancer in living tissue culture cells that produce EPO in a regulated fashion (Hep3B) and in cells that do not express EPO under any conditions tested (HeLa). We have identified in vivo DNA-protein interactions on the control elements in the human EPO enhancer by ligation-mediated PCR technology. We show that the putative protein binding sites in the EPO enhancer are occupied in vivo under conditions of normoxia, hypoxia, and cobalt exposure in EPO-producing cells. These sites are not occupied in cells that do not produce EPO. We also provide evidence for a conformational change in the topography of the EPO enhancer in response to hypoxia and cobalt exposure.

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