Genomic organization of human B-ATF, a target for regulation by EBV and HTLV-1

B-ATF is a member of the ATF/AP-1 superfamily of basic leucine zipper (bZIP) transcription factors. The ZIP regions of these proteins facilitate the formation of stable homodimers or heterodimers which bind to consensus DNA sites through adjacent basic amino acid residues. The B-ATF cDNA encodes a 1...

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Published in:Mammalian genome 1998-10, Vol.9 (10), p.849-852
Main Authors: Meyer, N P, Johansen, L M, Tae, H J, Budde, P P, Williams, K L, Taparowsky, E J
Format: Article
Language:English
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Summary:B-ATF is a member of the ATF/AP-1 superfamily of basic leucine zipper (bZIP) transcription factors. The ZIP regions of these proteins facilitate the formation of stable homodimers or heterodimers which bind to consensus DNA sites through adjacent basic amino acid residues. The B-ATF cDNA encodes a 125-amino acid protein with a centrally located bZIP domain. Previously, we have shown that B-ATF forms heterodimers with Jun proteins, but not with Fos or with a number of other bZIP proteins including ATF-2, CREB, or NF-IL6. B-ATF/Jun heterodimers bind consensus ATF/AP-1 DNA sites and, in contrast to Fos/Jun heterodimers, B-ATF/Jun complexes interfere with the transcriptional activation of target genes (Echlin and Taparowsky, in preparation). This suggests that the major cellular function of B-ATF is as a negative regulator of ATF/AP-1 transcriptional events. Furthermore, the observation that EBV and HTLV-1 up-regulate the expression of B-ATF in cells implies that these viruses may influence cellular gene expression patterns through increased production of B-ATF. As a first step towards defining the cis-acting regulatory elements controlling transcription of the B-ATF gene in normal cells and in virus-infected cells, we determined the structure and organization of the human B-ATF genomic locus.
ISSN:0938-8990
1432-1777
DOI:10.1007/s003359900881