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Science 11 January 1991:
Vol. 251. no. 4990, pp. 186 - 189
DOI: 10.1126/science.1987636
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Articles

Science, Vol 251, Issue 4990, 186-189
Copyright © 1991 by American Association for the Advancement of Science

articles

Methylation-sensitive sequence-specific DNA binding by the c-Myc basic region

GC Prendergast and EB Ziff

Howard Hughes Medical Institute, Department of Biochemistry, New York, NY.

The function of the c-Myc oncoprotein and its role in cell growth control is unclear. A basic region of c-Myc is structurally related to the basic motifs of helix-loop-helix (HLH) and leucine zipper proteins, which provide sequence-specific DNA binding function. The c-Myc basic region was tested for its ability to bind DNA by attaching it to the HLH dimerization interface of the E12 enhancer binding factor. Dimers of the chimeric protein, termed E6, specifically bound an E box element (GGCCACGTGACC) recognized by other HLH proteins in a manner dependent on the integrity of the c-Myc basic motif. Methylation of the core CpG in the E box recognition site specifically inhibited binding by E6, but not by two other HLH proteins. Expression of E6 (but not an E6 DNA binding mutant) suppressed the ability of c-myc to cooperate with H-ras in a rat embryo fibroblast transformation assay, suggesting that the DNA recognition specificity of E6 is related to that of c-Myc in vivo.


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Embryonic lethality in mice homozygous for a targeted disruption of the N-myc gene..
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Myc and Max associate in vivo..
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Max: functional domains and interaction with c-Myc..
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X. He, J. Futterer, and T. Hohn (2001)
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