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Publication : Isolation and characterization of nuclear proteins that bind to T cell receptor V beta decamer motif.

First Author  Lee MR Year  1992
Journal  J Immunol Volume  148
Issue  6 Pages  1906-12
PubMed ID  1531847 Mgi Jnum  J:49483
Mgi Id  MGI:1289108 Doi  10.4049/jimmunol.148.6.1906
Citation  Lee MR, et al. (1992) Isolation and characterization of nuclear proteins that bind to T cell receptor V beta decamer motif. J Immunol 148(6):1906-12
abstractText  TCR V beta promoter contains a highly conserved decamer homologous to cAMP response element (CRE). Recent studies have identified this CRE decamer as the dominant transcription-activating element within the TCR V beta promoter. We have isolated cDNA clones, TCR-ATF1 and TCR-ATF2, encoding DNA-binding proteins that recognize this CRE motif. The nucleotide sequence of TCR-ATF1 has not previously been reported, whereas that of TCR-ATF2 was homologous to CRE-BP1, ATF-2, and mXBP. Both TCR-ATF1 and TCR-ATF2 shared a conserved leucine zipper and DNA binding motif with other CRE-binding proteins. TCR-ATF1 and TCR-ATF2 were expressed in all cell lines examined and in mouse embryos as early as 12.5 days. Despite binding to the same CRE motif, TCR-ATF1 and TCR- ATF2 were different from CREB in the fine nucleotide specificity. TCR- ATF bound methylated CRE and CRE mutant M4 (4C----G) that were not recognized by CREB. Additionally, TCR-ATF1 weakly recognized two other single nucleotide mutants of V beta-CRE that were not bound by TCR-ATF2 and CREB. We have further demonstrated that TCR beta-chain expression was immediately activated by cAMP. Such induction is likely mediated through V beta-CRE sequence, because the inclusion of V beta-CRE in a vector with minimum promoter (pBLCAT2) conferred the cAMP inducibility of CAT activity.
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