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Nucleic Acids Research, 1989, Vol. 17, No. 20 8185-8194
© 1989

MOLECULAR BIOLOGY

Binding of a pancreatic nuclear protein is correlated with amytase enhancer activity

Georgette Howard, Paul R. Keller, Thomas M. Johnson and Miriam H. Meisler*

Department of Human Genetics, University of Michigan Medical School Ann Arbor, MI 48109-0618, USA

*To whom correspondence should be addressed

Received June 23, 1989. Revised September 8, 1989. Accepted September 8, 1989.

The mouse amylase gene Amy-2.2 is expressed at high levels specifically in the acinar cells of the pancreas. The region between –172 and –110 of this gene includes sequence elements common to pancreas-specific genes. Nuclear proteins with specific affinity for this region were partially purified from rat pancreas. The consensus element of another pancreas-specific gene, elastase 1, competes for protein binding to the amylase sequences. Binding was localized by DNase I protection to the sequence –156 to –122. Site-directed mutagenesis of this sequence resulted in concomitant loss of protein binding and enhancer activity. Photo-affinity labelling of pancreatic nuclear extracts identified one predominant binding protein with a molecular weight of approximately 75 kDa. The data indicate that binding of this nuclear protein is essential for the enhancer activity of this pancreas-specific element.


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