scholarly journals A Complex Deoxyribonucleic Acid Response Element in the Rat Ca2+/Calmodulin-Dependent Protein Kinase IV Gene 5′-Flanking Region Mediates Thyroid Hormone Induction and Chicken Ovalbumin Upstream Promoter Transcription Factor 1 Repression

2002 ◽  
Vol 16 (11) ◽  
pp. 2439-2451 ◽  
Author(s):  
Yan-Yun Liu ◽  
Gregory A. Brent
Keyword(s):  
Transcription Factor ◽  
Thyroid Hormone ◽  
Protein Kinase ◽  
Deoxyribonucleic Acid ◽  
Dependent Protein Kinase ◽  
Upstream Promoter ◽  
Dependent Protein ◽  
Flanking Region ◽  
Transcription Factor 1 ◽  
Chicken Ovalbumin

scholarly journals Overexpression of Zinc Finger Transcription Factor ZAT6 Enhances Salt Tolerance

2018 ◽  
Vol 13 (1) ◽  
pp. 431-445 ◽  
Author(s):  
Wei Tang ◽  
Caroline Luo
Keyword(s):  
Transcription Factor ◽  
Salt Stress ◽  
Protein Kinase ◽  
Stress Tolerance ◽  
Zinc Finger ◽  
Salt Stress Tolerance ◽  
Dependent Protein Kinase ◽  
Zinc Finger Transcription Factor ◽  
Transgenic Cell ◽  
Dependent Protein

AbstractThe purpose of the present investigation is to examine the function of the C2H2-type zinc finger transcription factor of Arabidopsis thaliana 6 (ZAT6) in salt stress tolerance in cells of rice (Oryza sativa L.), cotton (Gossypium hirsutum L.) and slash pine (Pinus elliottii Engelm.). Cells of O. sativa, G. hirsutum, and P. elliottii overexpressing ZAT6 were generated using Agrobacterium-mediated genetic transformation. Molecular and functional analysis of transgenic cell lines demonstrate that overexpression of ZAT6 increased tolerance to salt stress by decreasing lipid peroxidation and increasing the content of abscisic acid (ABA) and GA8, as well as enhancing the activities of antioxidant enzymes such as ascorbate peroxidise (APOX), catalase (CAT), glutathione reductase (GR), and superoxide dismutase (SOD). In rice cells, ZAT6 also increased expression of Ca2+-dependent protein kinase genes OsCPK9 and OsCPK25 by 5–7 fold under NaCl stress. Altogether, our results suggest that overexpression of ZAT6 enhanced salt stress tolerance by increasing antioxidant enzyme activity, hormone content and expression of Ca2+-dependent protein kinase in transgenic cell lines of different plant species.

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.

scholarly journals Thyroid Hormone Activation of Transcription Is Potentiated by Activators of cAMP-dependent Protein Kinase

1996 ◽  
Vol 271 (36) ◽  
pp. 21950-21955 ◽  
Author(s):  
Dale C. Leitman ◽  
Cláudia H. R. M. Costa ◽  
Hans Graf ◽  
John D. Baxter ◽  
Ralff C. J. Ribeiro
Keyword(s):  
Thyroid Hormone ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Activation Of Transcription ◽  
Dependent Protein
Sign in / Sign up

Export Citation Format

Share Document