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Am J Physiol Endocrinol Metab (April 23, 2002). doi:10.1152/ajpendo.00057.2002
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Articles in PresS, published online ahead of print April 23, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00057.2002
Submitted on February 11, 2002
Accepted on April 20, 2002

The N-Terminus of PTB-Associated Splicing Factor Binds to the Porcine P450scc Insulin-like Growth Factor Response Element

Randall J. Urban1*, Yvonne H. Bodenburg1, and Thomas G. Wood1

1 Internal Medicine, The University of Texas Medical Branch, Galveston, Texas, USA

* To whom correspondence should be addressed. E-mail: rurban{at}utmb.edu.

An IGF-I response element (IGFRE) in the porcine P-450 cholesterol side-chain cleavage gene (P450scc) regulates transcription through the binding of two proteins, Sp1 and PTB-associated splicing factor (PSF). PSF is a component of spliceosomes and contains RNA binding domains. In this study, we localized the N-terminus amino acid residues necessary for binding of PSF to the IGFRE. Three C-terminus truncated proteins (304, 214, and 134 aa) of PSF were designed to empirically partition the N-terminus region while excluding the RNA binding domains. Southwestern analysis showed that only the largest expressed truncated protein, P3, strongly bound the porcine P450scc IGFRE. Truncated PSF protein expression in Y1 adrenal cells showed that P3 repressed transcriptional activity of the IGFRE similar to full-length PSF while P2 (minimal binding to the IGFRE) had no effect. In conclusion, the N-terminus region of PSF contains the amino acid residues necessary for binding to the porcine P450scc IGFRE and repressing the transcriptional activity of the element.




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