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PMID: 2478959 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Binding of a pancreatic nuclear protein is correlated with amylase enhancer activity.

Nucleic acids research ·Vol. 17 ·No. 20 ·1989-10-25 ·Pages 8185-95

Howard G, Keller PR, Johnson TM, Meisler MH

Abstract

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.

MeSH Terms
Amylases/genetics Animals Base Sequence Cell Line Enhancer Elements, Genetic Genes Mice Molecular Sequence Data Mutation Nuclear Proteins/isolation & purification,metabolism Pancreas/enzymology
Chemicals
Nuclear Proteins Amylases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Howard G
Department of Human Genetics, University of Michigan Medical School, Ann Arbor 48109-0618.
Keller P R
Johnson T M
Meisler M H
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/17.20.8185
Published
1989-10-25
Pages
8185-95
Language
English
Region
England
NLM ID
0411011
PMCID
PMC334957
Subset
IM
Grants
NIDDK NIH HHS · DK 08137 · United States
NIDDK NIH HHS · DK36089 · United States
NICHD NIH HHS · HD07247 · United States
External Links
PubMed source DOI: 10.1093/nar/17.20.8185 PMC Full Text View journal details
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