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As a first step towards understanding the mechanism underlying the differential gene expression of the two variants of the rat proteinase-inhibitor α 1 -Inhibitor 3 (α 1 I3) corresponding genomic clones were isolated. The 100% similarity between the sequence of one genomic clone and that of the α 1 -I3 variant I cDNA strongly suggested that its 5′-sequence represented the upstream region of the corresponding gene. Several putative  cis -regulatory elements were identified as well as a polypyrimidine tract located between the transcription start site of the α 1 -I3 variant I mRNA and the AUG codon. The polypyrimidine tract functions as a positive  cis -element in a heterologous promoter. By electrophoretic mobility shift assays (EMSA) we have shown that a GST (glutathione S-transferase) fusion of the rat polypyrimidine tract binding protein (PTB) has a high affinity for the pyrimidine-rich sense strand but not for the complementary sequence of the 5′-untranslated region of the α 1 -I3 variant I gene.

biological chemistry

A High Affinity Binding Site for the Polypyrimidine Tract Binding Protein (PTB) Is Located in the 5'-Untranslated Region of the Rat Proteinase α1-Inhibitor 3 Variant I Gene