scholarly journals Contrasting Mammalian Parathyroid Hormone (PTH) Promoters: Nuclear Factor-Y Binds to a Deoxyribonucleic Acid Element Unique to the Human PTH Promoter and Acts as a Transcriptional Enhancer

Endocrinology ◽  
2004 ◽  
Vol 145 (6) ◽  
pp. 2713-2720 ◽  
Author(s):  
Alexander P. Alimov ◽  
M. Chris Langub ◽  
Hartmut H. Malluche ◽  
Ok-Kyong Park-Sarge ◽  
Nicholas J. Koszewski
Keyword(s):  
Parathyroid Hormone ◽  
Deoxyribonucleic Acid ◽  
Nuclear Factor ◽  
Transcriptional Enhancer ◽  
Nuclear Factor Y ◽  
Acid Element

scholarly journals Transactivation of the Parathyroid Hormone Promoter by Specificity Proteins and the Nuclear Factor Y Complex

Endocrinology ◽  
2005 ◽  
Vol 146 (8) ◽  
pp. 3409-3416 ◽  
Author(s):  
Alexander P. Alimov ◽  
Ok-Kyong Park-Sarge ◽  
Kevin D. Sarge ◽  
Hartmut H. Malluche ◽  
Nicholas J. Koszewski
Keyword(s):  
Parathyroid Hormone ◽  
Binding Site ◽  
Gene Transcription ◽  
Nuclear Factor ◽  
Nuclear Factor Y ◽  
Specificity Protein 1 ◽  
Nuclear Extracts ◽  
Promoter Construct ◽  
Helical Turn ◽  
Specificity Protein

Abstract We previously identified a highly conserved specificity protein 1 (Sp1) DNA element in mammalian PTH promoters that acted as an enhancer of gene transcription and bound Sp1 and Sp3 proteins present in parathyroid gland nuclear extracts. More recently, a nuclear factor (NF)-Y element (NF-Yprox) was also described by our group, which was located approximately 30 bp downstream from the Sp1 site in the human PTH (hPTH) promoter and by itself acted as a weak enhancer of gene transcription. We now report that Sp proteins and NF-Y can synergistically enhance transcription of a minimal hPTH promoter construct. Positioning of the Sp1 DNA element appears to be critical for this synergism because deviations of one half of a helical turn caused an approximate 60% decrease in transactivation. Finally, examination of the bovine PTH (bPTH) promoter also revealed Sp1/NF-Y synergism, in conjunction with the identification of an analogous NF-Y binding site similarly positioned downstream from the bPTH Sp1 element. In summary, synergistic transactivation of the hPTH and bPTH promoters is observed by Sp proteins and the NF-Y complex. The conservation of this transactivation in the human and bovine promoters suggests that this may be a principle means of enhancing PTH gene transcription.

scholarly journals Sp3/Sp1 in the Parathyroid Gland: Identification of an Sp1 Deoxyribonucleic Acid Element in the Parathyroid Hormone Promoter

Endocrinology ◽  
2003 ◽  
Vol 144 (7) ◽  
pp. 3138-3147 ◽  
Author(s):  
Alexander P. Alimov ◽  
M. Chris Langub ◽  
Hartmut H. Malluche ◽  
Nicholas J. Koszewski
Keyword(s):  
Parathyroid Hormone ◽  
Parathyroid Gland ◽  
Deoxyribonucleic Acid ◽  
Acid Element

scholarly journals Managing the sugar factory: A new feather in the cap for nuclear factor Y

2018 ◽  
Vol 293 (20) ◽  
pp. 7905-7906 ◽  
Author(s):  
Sabyasachi Sen ◽  
Chandrima Das
Keyword(s):  
Nuclear Factor ◽  
Sugar Factory ◽  
Nuclear Factor Y

Binding of nuclear factor EF-C to a functional domain of the hepatitis B virus enhancer region

1989 ◽  
Vol 9 (7) ◽  
pp. 2787-2797
Author(s):  
P Ostapchuk ◽  
G Scheirle ◽  
P Hearing
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Inverted Repeat ◽  
Functional Domain ◽  
Nuclear Factor ◽  
Transcriptional Enhancer ◽  
Base Pairs ◽  
Enhancer Region ◽  
B Virus

Nuclear factor EF-C is present in extracts prepared from human HepG2 liver cells and from other, nonliver cell lines and binds to the hepatitis B virus and polyomavirus transcriptional enhancer regions in vitro. An inverted repeat (5'-GTTGCNNNGCAAC-3') is located within both binding regions. Diethyl pyrocarbonate interference binding assays and competition binding experiments using altered binding sites demonstrated that EF-C contacts symmetrical nucleotides within the inverted repeat. Mutations that changed the length of the spacer region between the arms of the inverted repeat were introduced in the hepatitis enhancer region. Introduction of 1 or 2 base pairs between the repeats did not affect EF-C binding, but deletion of 1 base pair or introduction of 3 to 9 base pairs reduced binding dramatically. Introduction of 10 base pairs restored partial EF-C binding ability. These and other results suggest that EF-C binding is stabilized by dimerization. In vivo assays for enhancer function using these mutants demonstrated that the EF-C binding site is a functional and important component of the hepatitis B virus enhancer region.

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