A role for the non-conserved N-terminal domain of the TATA-binding protein in the crosstalk between cell signaling pathways and steroid receptors
| Autor: | James R. Lambert, Steven K. Nordeen |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: | |
| Zdroj: | AIMS Molecular Science, Vol 2, Iss 2, Pp 64-76 (2015) |
| Druh dokumentu: | article |
| ISSN: | 2372-028X 2372-0301 |
| DOI: | 10.3934/molsci.2015.2.64/fulltext.html |
| Popis: | Transcriptional induction by steroid receptors is coupled to cellular signal transduction pathways although, in general, the mechanisms governing these events are not well defined. Using TATA-binding protein (TBP) specificity mutants that recognize a TGTA box, we show that yeast TBP expressed in mammalian cells can support steroid-mediated gene induction to a similar degree as human TBP, however yeast TBP does not support the 8-Bromo-cAMP-mediated potentiation of glucocorticoid receptor (GR)-dependent transactivation. Chimeras between yeast and human TBP reveal that it is the non-conserved N-terminus of TBP that governs the potentiation of GR action. While the conserved core of TBP is sufficient for TATA-element binding and preinitiation complex formation, the role of the N-terminus has remained elusive. Our results suggest a role of the N-terminus of human TBP in coupling cell signaling events to steroid-mediated transcription, thereby establishing one of the few described functional roles of this polypeptide domain in a physiological process. |
| Databáze: | Directory of Open Access Journals |
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