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Journal of Dairy Science Vol. 80 No. 7 1389-1397
© 1997 by American Dairy Science Association ®
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Polymorphisms of Bovine ß-Lactoglobulin Promoter and Differences in the Binding Affinity of Activator Protein-2 Transcription Factor

Lorraine S. Lum 1, Peter Dovccaron 1, and Juan F. Medrano 1

1 Department of Animal Science, University of California, Davis 95616-8521

Differential production of the two most common allelic variants of ß-lactoglobulin (LG), ß-LG A and ß-LG B, has been observed using PAGE. This study evaluated 733 bp of the ß-LG promoter region and 92 bp of the first exon for possible polymorphisms using denaturing gradient gel electrophoresis and nucleotide sequence analysis. Within this region, 13 single nucleotide substitution polymorphisms were detected. Twelve polymorphisms were allele specific, and one appeared to be polymorphic only for the B allele. Several potential binding sites for transcription factors were found within the promoter sequence. This study investigated the role of the G to C transversion within a consensus binding site for activator protein-2 at position –430 bp upstream from the transcription initiation site. Using the DNase-I footprint assay, we confirmed the functional importance of this point mutation and showed different binding affinities of activator protein-2 for both alleles. We discuss the possible regulatory role of activator protein-2 in the transcriptional regulation of the ß-LG gene and propose the activator protein-2 transcription factor as a modulator of gene expression of ß-LG.

Key Words: activator protein-2 • ßbeta;-lactoglobulin • promoter • transcription factor

Submitted on March 25, 1996
Accepted on November 18, 1996




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Copyright © 1997 by the American Dairy Science Association ®.