UMMS Affiliation

Program in Gene Function and Expression; Program in Molecular Medicine

Date

4-15-1997

Document Type

Article

Medical Subject Headings

Amino Acid Sequence; Animals; Base Sequence; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors; Basic-Leucine Zipper Transcription Factors; Binding Sites; Cloning, Molecular; DNA Footprinting; DNA Primers; DNA-Binding Proteins; Deoxyribonuclease I; Dimerization; Escherichia coli; Humans; *Introns; Molecular Sequence Data; Open Reading Frames; Ornithine Decarboxylase; Polymerase Chain Reaction; Protein Multimerization; Proto-Oncogene Proteins c-myc; Rats; Recombinant Proteins; Transcription Factors

Disciplines

Genetics and Genomics

Abstract

The oncoprotein c-Myc plays an important role in cell proliferation, transformation, inhibition of differentiation and apoptosis. These functions most likely result from the transcription factor activity of c-Myc. As a heterodimer with Max, the c-Myc protein binds to the E-box sequence (CACGTG), which is also recognized by USF dimers. In order to test differences in target gene recognition of c-Myc/Max, Max and USF dimers, we compared the DNA binding characteristics of these proteins in vitro using vaccinia viruses expressing full-length c-Myc and Max proteins. As expected, purified c-Myc/max binds specifically to a consensus E-box. The optimal conditions for DNA binding by either c-Myc/Max, Max or USF dimers differ with respect to ionic strength and Mg2+ ion concentration. Most interestingly, the c-Myc/Max complex binds with a high affinity to its natural target, the rat ODC gene, which contains two adjacent, consensus E-boxes. High affinity binding results from teh ability of c-Myc/Max dimers to bind cooperatively to these E-boxes. We propose that differential cooperative binding by E-box binding transcription factors could contribute to target gene specificity.

Rights and Permissions

Citation: Nucleic Acids Res. 1997 Apr 15;25(8):1493-501. Link to article on publisher's site

Comments

At the time of publication, Albertha J. Marian Walhout was not yet affiliated with the University of Massachusetts Medical School.

Related Resources

Link to Article in PubMed

PubMed ID

9162900

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