Demonstration of DNA binding factors interacting with a fragment of the canine prostate arginine esterase gene promoter

• Published in: FEBS letters Vol. 303; no. 2; pp. 117 - 120
• Main Authors: Chapdelaine, Pierre, Gue´rin, Sylvain, Tremblay, Roland R., Dube´, Jean Y.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.06.1992; Elsevier
• Subjects: Androgen action; Animals; Base Sequence; Biological and medical sciences; Carboxylic Ester Hydrolases - genetics; Carboxylic Ester Hydrolases - metabolism; DNA; DNA binding factor; DNA-Binding Proteins - metabolism; Dogs; Fundamental and applied biological sciences. Psychology; Gene regulation; Male; Methylation; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Orchiectomy; Promoter Regions, Genetic; Prostate - enzymology; Prostatic secretory protein; Transcription. Transcription factor. Splicing. Rna processing; DNA binding factor; Androgen action; Prostatic secretory protein; Gene regulation; Fissipedia; Carnivora; Vertebrata; Mammalia; Esterase; Enzyme; Transcription promoter; Nucleotide fragment; DNA binding protein; Molecular interaction; Dog; Prostate
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80501-7

We have studied, by the gel mobility shift assay, the interaction of DNA binding proteins with a fragment of the proximal promoter (from nucleotides −177 to −47) of the androgen-regulated canine prostate arginine esterase gene. Several shifted bands were obtained using nuclear extracts from various tissues. In the case of the prostate, the intensity of some of the shifted bands was decreased or increased when the extracts were prepared from animals that had been castrated 12 days earlier. Several of the DNA-protein complexes could be assigned to an interaction with part or all of the sequence GGGGGTGGGGG from −124 to −114. We also obtained evidence for the presence of protein(s) interacting with an Spl motif present in the same fragment. These results suggest that some ubiquitous factors different from the androgen receptors could be involved in the regulation of the arginine esterase gene.