Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element.
作者： Randall J. Urban , Yvonne Bodenburg , Alexander Kurosky , Thomas G. Wood , Slavisa Gasic
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摘要: The porcine P-450 cholesterol side-chain cleavage enzyme gene (P450scc) contains a 30-bp region [insulin-like growth factor response element (IGFRE)] that mediates insulin-like I (IGF-I)-stimulated expression and binds Sp1. In this study, we showed polypyrimidine tract-binding protein (PTB)-associated splicing (PSF), an RNA-binding component of spliceosomes, to the IGFRE. Southwestern analysis with IGFRE oligonucleotide (from Sp1-immunodepleted HeLa extract) fractionated on SDS-PAGE at 100 kDa. Microsequence 100-kDa band proteins detected PSF. DNA affinity chromatography, using mutant does not bind Sp1, isolated immunoreacted PSF antibody. Deoxyribonuclease (DNase I) footprint recombinant 5′ Sp1-binding GC box IGFRE, oligonucleotides further delineated palindrome, CTGAGTC. Functional these mutants ...
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