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Volume 272, Number 19, Issue of May 9, 1997 pp. 12793-12800
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

ATF-2 and C/EBPalpha Can Form a Heterodimeric DNA Binding Complex in Vitro
FUNCTIONAL IMPLICATIONS FOR TRANSCRIPTIONAL REGULATION

(Received for publication, February 14, 1997)

Jon D. Shuman , JaeHun Cheong and John E. Coligan

From the Laboratory of Molecular Structure, NIAID, National Institutes of Health, Rockville, Maryland 20892-1727

We screened an expression cDNA library with a radiolabeled C/EBPalpha fusion protein and isolated three independent cDNAs encoding ATF-2, a bZIP protein that binds cAMP response elements (CRE). This interaction requires the respective bZIP domains, which form a typical bZIP heterodimer with altered DNA binding selectivity. C/EBPalpha and ATF-2 homodimers bind CRE sites, but ATF-2:C/EBPalpha heterodimers do not. Heterodimers bind an asymmetric sequence composed of one consensus half-site for each monomer, and may thus have a unique regulatory function. As predicted, co-transfection of ATF-2 with C/EBPalpha results in decreased activation of transcription driven from consensus C/EBP-binding sites. In contrast, C/EBPalpha and ATF-2 function cooperatively to activate transcription driven by the asymmetric sequence. Both factors are expressed in liver, where immunoprecipitation experiments show that ATF-2 co-precipitates with C/EBPalpha . These results are consistent with the interpretation that C/EBPalpha and ATF-2 can associate in vivo. Moreover, the formation of ATF-2:C/EBPbeta heterodimers suggests that cross-family dimerization with ATF-2 may be a general property for C/EBP family proteins.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.