scholarly journals Coordinated Transcriptional Regulation of Cytochrome P450 3As by Nuclear Transcription Factor Y and Specificity Protein 1

2019 ◽  
Vol 95 (5) ◽  
pp. 507-518 ◽  
Author(s):  
Ruohong Chen ◽  
Jun Jiang ◽  
Zhangsheng Hu ◽  
Wenchu Ye ◽  
Qianqian Yuan ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Transcriptional Regulation ◽  
Cytochrome P450 ◽  
Specificity Protein 1 ◽  
Nuclear Transcription Factor ◽  
Specificity Protein

Spot 14 protein interacts and co-operates with chicken ovalbumin upstream promoter-transcription factor 1 in the transcription of the L-type pyruvate kinase gene through a specificity protein 1 (Sp1) binding site

2001 ◽  
Vol 358 (1) ◽  
pp. 175-183 ◽  
Author(s):  
Emmanuel COMPE ◽  
Georges de SOUSA ◽  
Kamel FRANCÇOIS ◽  
Régis ROCHE ◽  
Roger RAHMANI ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Pyruvate Kinase ◽  
Nuclear Proteins ◽  
Kinase Gene ◽  
Specificity Protein 1 ◽  
Upstream Promoter ◽  
Spot 14 ◽  
Specificity Protein ◽  
Transcription Factor 1 ◽  
Chicken Ovalbumin

In hepatocytes, the amount of the Spot 14 (S14) protein is closely related to the full expression of enzymes involved in the glycolytic and lipogenic pathways. In the present study we address the role played by this protein in the control of transcription of the L-type pyruvate kinase (L-PK) gene in primary hepatocytes. We show that human S14, which by itself does not bind to the L-PK promoter, physically interacts with the human chicken ovalbumin upstream promoter-transcription factor 1 (COUP-TF1) and induces the switch of this factor from a repressor to an activator. However, the enhancing activity of S14 and COUP-TF1 depends on the presence of a proximal GC-rich box (the L0 element) that specifically binds nuclear proteins from the livers of rats fed a glucose-rich diet. Moreover, the L0 element, which strongly binds dephosphorylated specificity protein 1 (Sp1), loses all affinity when this factor is phosphorylated by cAMP-dependent protein kinase. Mutations that affect binding of Sp1 and nuclear proteins to the L0 box also decrease basal transcription and impair glucose responsiveness of the promoter. These results therefore shed light on the mechanism by which the S14 protein, whose concentration rapidly rises after glucose intake, contributes to the full activity of the L-PK promoter.

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