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J Biol Chem, Vol. 275, Issue 8, 5958-5965, February 25, 2000

Structural Analysis of alpha -Enolase
MAPPING THE FUNCTIONAL DOMAINS INVOLVED IN DOWN-REGULATION OF THE c-myc PROTOONCOGENE*

Aruna SubramanianDagger and Donald M. Miller§

From the Dagger  Comprehensive Cancer Center and Department of Biochemistry, University of Alabama at Birmingham, Birmingham, Alabama 35294-3300 and the § James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40206

Myc-binding protein-1 (MBP-1) is a 37-kDa protein with sequence homology to the 3' portion of the alpha -enolase gene. alpha -Enolase is a 48-kDa protein, which plays a critical role in the glycolytic pathway. MBP-1 binds to the c-myc P2 promoter and down-regulates c-myc expression. We have investigated the role of alpha -enolase in regulation of the c-myc protooncogene. RNase protection assay shows that alpha -enolase is transcribed into a single RNA species in HeLa cells. A start codon, 400 base pairs downstream of the alpha -enolase ATG, corresponds to the MBP-1 ATG, suggesting that MBP-1 is an alternative translation initiation product of the alpha -enolase RNA. Domain mapping was performed using constructs containing truncations of the alpha -enolase gene. In vitro binding to the c-myc gene was abolished after deletion of the N-terminal portion of alpha -enolase. In order to determine the relationship between DNA binding activity and transcription inhibition, we performed co-transfection assays in HeLa cells. These studies confirmed that an N-terminal deletion of alpha -enolase is unable to down-regulate c-myc promoter activity. Our data suggest that alpha -enolase plays an important role in regulation of c-myc promoter activity in the form of an alternative translation product MBP-1, which is distinct from its role as a glycolytic enzyme.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: 529 S. Jackson St., Louisville, KY 40206. Tel.: 502-562-4790; Fax: 502-562-4368; E-mail: donaldmi@ulh.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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