Design, spectroscopic properties and effects of novel catechol spiroborates derived from Schiff bases in the antioxidant, antibacterial and DNA binding activity

2021 ◽  
pp. 122228
Author(s):  
Ahmet KILIC ◽  
Rahime SÖYLEMEZ ◽  
Veysi OKUMUŞ
Keyword(s):  
Dna Binding ◽  
Schiff Bases ◽  
Spectroscopic Properties ◽  
Binding Activity ◽  
Dna Binding Activity

Studies on the effect of remote substituents on the DNA binding activity of novel chiral Schiff bases

2021 ◽  
Vol 1234 ◽  
pp. 130179
Author(s):  
Aditi Bora ◽  
Subir Kr Maiti ◽  
Anmol Singh ◽  
Pranjit Barman
Keyword(s):  
Dna Binding ◽  
Schiff Bases ◽  
Binding Activity ◽  
Dna Binding Activity

scholarly journals Structure of the p53/RNA polymerase II assembly

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Shu-Hao Liou ◽  
Sameer K. Singh ◽  
Robert H. Singer ◽  
Robert A. Coleman ◽  
Wei-Li Liu
Keyword(s):  
Dna Binding ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Conformational Changes ◽  
P53 Protein ◽  
Binding Activity ◽  
Transactivation Domain ◽  
Pol Ii ◽  
Dna Binding Activity ◽  
Regulated Gene Expression

AbstractThe tumor suppressor p53 protein activates expression of a vast gene network in response to stress stimuli for cellular integrity. The molecular mechanism underlying how p53 targets RNA polymerase II (Pol II) to regulate transcription remains unclear. To elucidate the p53/Pol II interaction, we have determined a 4.6 Å resolution structure of the human p53/Pol II assembly via single particle cryo-electron microscopy. Our structure reveals that p53’s DNA binding domain targets the upstream DNA binding site within Pol II. This association introduces conformational changes of the Pol II clamp into a further-closed state. A cavity was identified between p53 and Pol II that could possibly host DNA. The transactivation domain of p53 binds the surface of Pol II’s jaw that contacts downstream DNA. These findings suggest that p53’s functional domains directly regulate DNA binding activity of Pol II to mediate transcription, thereby providing insights into p53-regulated gene expression.

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