A role for the non-conserved N-terminal domain of the TATA-binding protein in the crosstalk between cell signaling pathways and steroid receptors

James R. Lambert; Steven K. Nordeen; James R. Lambert; Steven K. Nordeen

doi:10.3934/molsci.2015.2.64

AIMS Molecular Science

2015, Volume 2, Issue 2: 64-76. doi: 10.3934/molsci.2015.2.64

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A role for the non-conserved N-terminal domain of the TATA-binding protein in the crosstalk between cell signaling pathways and steroid receptors

James R. Lambert ^,,
Steven K. Nordeen

Department of Pathology, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA

Received: 28 October 2014 Accepted: 13 March 2015 Published: 25 March 2015

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.
- TBP,
- glucocorticoid receptor,
- cyclic AMP,
- steroid receptor,
- coactivator,
- crosstalk,
- protein kinase A
Citation: James R. Lambert, Steven K. Nordeen. A role for the non-conserved N-terminal domain of the TATA-binding protein in the crosstalk between cell signaling pathways and steroid receptors[J]. AIMS Molecular Science, 2015, 2(2): 64-76. doi: 10.3934/molsci.2015.2.64

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Abstract

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.

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