FUNCTIONAL CHARACTERIZATION OF FOUR NATURALLY OCCURRING VARIANTS OF HUMAN PREGNANE X RECEPTOR (PXR): ONE VARIANT CAUSES DRAMATIC LOSS OF BOTH DNA BINDING ACTIVITY AND THE TRANSACTIVATION OF THE CYP3A4 PROMOTER/ENHANCER REGION

2004 ◽  
Vol 32 (1) ◽  
pp. 149-154 ◽  
Author(s):  
Satoru Koyano ◽  
Kouichi Kurose ◽  
Yoshiro Saito ◽  
Shogo Ozawa ◽  
Ryuichi Hasegawa ◽  
...  
Keyword(s):  
Dna Binding ◽  
Functional Characterization ◽  
Pregnane X Receptor ◽  
Binding Activity ◽  
Enhancer Region ◽  
Dna Binding Activity ◽  
Naturally Occurring

scholarly journals Diversification of Transcription Factor NF-κB in Protists

2021 ◽  
Author(s):  
Leah M. Williams ◽  
Sainetra Sridhar ◽  
Jason Samaroo ◽  
Ebubechi K. Adindu ◽  
Anvitha Addanki ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Transcriptional Activation ◽  
Functional Characterization ◽  
Binding Activity ◽  
Life Stages ◽  
Rna Seq ◽  
Dna Binding Activity ◽  
Inhibitory Domain

In this report, we investigate the evolution of transcription factor NF-κB by examining its structure, activity, and regulation in two protists using phylogenetic, cellular, and biochemical techniques. In Capsaspora owczarzaki (Co), we find that full-length NF-κB has an N-terminal DNA-binding domain and a C-terminal Ankyrin (ANK) repeat inhibitory domain, and its DNA-binding activity is more similar to metazoan NF-κB rather than Rel proteins. As with mammalian NF-κB proteins, removal of the ANK repeats is required for Co-NF-κB to enter the nucleus, bind DNA, and activate transcription. However, C-terminal processing of Co-NF-κB is not induced by co-expression of IKK in human cells. Exogenously expressed Co-NF-κB localizes to the nucleus in Co cells. NF-κB mRNA and DNA-binding levels differ across three life stages of Capsaspora, suggesting distinct roles for NF-κB in these life stages. RNA-seq and GO analyses identify possible gene targets and biological functions of Co-NF-κB. We also show that three NF-κB-like proteins from the choanoflagellate Acanthoeca spectabilis (As) all consist of primarily the N-terminal conserved Rel Homology domain sequences of NF-κB, and lack C-terminal ANK repeats. All three As-NF-κB proteins constitutively enter the nucleus of human and Co cells, but differ in their DNA-binding and transcriptional activation activities. Furthermore, all three As-NF-κB proteins can form heterodimers, indicating that NF-κB diversified into multi-subunit families at least two times during evolution. Overall, these results present the first functional characterization of NF-κB in a taxonomic kingdom other than Animalia and provide information about the evolution and diversification of this biologically important transcription factor.

Characterization of the DNA Binding Activity of the ZFY Zinc Finger Domain

Biochemistry ◽  
2010 ◽  
Vol 49 (4) ◽  
pp. 679-686 ◽  
Author(s):  
Jennifer Grants ◽  
Erin Flanagan ◽  
Andrea Yee ◽  
Paul J. Romaniuk
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Binding Activity ◽  
Zinc Finger Domain ◽  
Dna Binding Activity

scholarly journals Biochemical characterization of L1 repressor mutants with altered operator DNA binding activity

Bacteriophage ◽  
2012 ◽  
Vol 2 (2) ◽  
pp. 79-88 ◽  
Author(s):  
Amitava Bandhu ◽  
Tridib Ganguly ◽  
Biswanath Jana ◽  
Amritangshu Chakravarty ◽  
Anindya Biswas ◽  
...  
Keyword(s):  
Dna Binding ◽  
Biochemical Characterization ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Operator Dna

scholarly journals Characterization of the Novel DNA Binding Activity of the BRG1 At-Hook-Bromodomain and Effect of Cancer Mutations

2018 ◽  
Vol 114 (3) ◽  
pp. 569a
Author(s):  
Julio C. Sanchez ◽  
Liyang Zhang ◽  
Amber Liu ◽  
Miles A. Pufall ◽  
Catherine A. Musselman
Keyword(s):  
Dna Binding ◽  
Binding Activity ◽  
The Novel ◽  
Dna Binding Activity ◽  
Cancer Mutations

scholarly journals Characterization of the Novel DNA Binding Activity of the BRG1 At-Hook-Bromodomain

2019 ◽  
Vol 116 (3) ◽  
pp. 332a
Author(s):  
Julio C. Sanchez ◽  
Liyang Zhang Zhang ◽  
Miles Pufall ◽  
Catherine Musselman
Keyword(s):  
Dna Binding ◽  
Binding Activity ◽  
The Novel ◽  
Dna Binding Activity

Characterization of the DNA-Binding Activity of HIV-1 Integrase Using a Filter Binding Assay

1995 ◽  
Vol 217 (3) ◽  
pp. 802-810 ◽  
Author(s):  
I.R. Haugan ◽  
B.M. Nilsen ◽  
S. Worland ◽  
L. Olsen ◽  
D.E. Helland
Keyword(s):  
Dna Binding ◽  
Binding Assay ◽  
Binding Activity ◽  
Dna Binding Activity ◽  
Hiv 1

scholarly journals Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension

1996 ◽  
Vol 271 (4) ◽  
pp. C1172-C1180 ◽  
Author(s):  
B. H. Jiang ◽  
G. L. Semenza ◽  
C. Bauer ◽  
H. H. Marti
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Mammalian Cells ◽  
Functional Characterization ◽  
Hypoxia Inducible Factor ◽  
Binding Activity ◽  
Maximal Response ◽  
Hypoxia Inducible Factor 1 ◽  
Dna Binding Activity

Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric basic helix-loop-helix protein implicated in the transcriptional activation of genes encoding erythropoietin, glycolytic enzymes, and vascular endothelial growth factor in hypoxic mammalian cells. In this study, we have quantitated HIF-1 DNA-binding activity and protein levels of the HIF-1 alpha and HIF-1 beta subunits in human HeLa cells exposed to O2 concentrations ranging from 0 to 20% in the absence or presence of 1 mM KCN to inhibit oxidative phosphorylation and cellular O2 consumption. HIF-1 DNA-binding activity, HIF-1 alpha protein and HIF-1 beta protein each increased exponentially as cells were subjected to decreasing O2 concentrations, with a half maximal response between 1.5 and 2% O2 and a maximal response at 0.5% O2, both in the presence and absence of KCN. The HIF-1 response was greatest over O2 concentrations associated with ischemic/hypoxic events in vivo. These results provide evidence for the involvement of HIF-1 in O2 homeostasis and represent a functional characterization of the putative O2 sensor that initiates hypoxia signal transduction leading to HIF-1 expression.

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