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Submitted on March 8, 2005
Accepted on May 3, 2005
University of Kentucky Medical Center, Division of Nephrology, Bone and Mineral Metabolism, 800 Rose Street, Lexington, KY 40536-0298; University of Kentucky Medical Center, Department of Physiology, 800 Rose Street, Lexington, KY 40536-0298, University of Kentucky Medical Center, Department of Molecular and Cellular Biochemistry, 800 Rose Street, Lexington, KY 40536-0298
* To whom correspondence should be addressed. E-mail: njhosz0{at}uky.edu.
We previously identified a highly conserved Sp1 DNA element in mammalian parathyroid hormone (PTH) promoters that acted as an enhancer of gene transcription and bound Sp1 and Sp3 proteins present in parathyroid gland nuclear extracts. More recently, an 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 as 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.
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