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p53 dynamically directs TFIID assembly on target gene promoters

R. A. Coleman, Z. Qiao, S. K. Singh, C. S. Peng, M. Cianfrocco, Z. Zhang, A. Piasecka, H. Aldeborgh, G. Basishvili, W. L. Liu
doi: https://doi.org/10.1101/083014
R. A. Coleman
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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  • For correspondence: robert.coleman2@einstein.yu.edu
Z. Qiao
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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S. K. Singh
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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C. S. Peng
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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M. Cianfrocco
2Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA
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Z. Zhang
3Surrozen, 240 East Grand Avenue, 2nd Floor, South San Francisco, CA 94080, USA
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A. Piasecka
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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H. Aldeborgh
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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G. Basishvili
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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W. L. Liu
1Gruss-Lipper Biophotonics Center, Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
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Abstract

The p53 tumor suppressor protein is a central regulator that turns on vast gene networks to maintain cellular integrity upon various stimuli. p53 activates transcription initiation in part by aiding recruitment of TFIID to the promoter. However, the precise means by which p53 dynamically interacts with TFIID to facilitate assembly on target gene promoters remains elusive. To address this key question, we have undertaken an integrated approach involving single molecule fluorescence microscopy, single particle cryo-electron microscopy, and biochemistry. Our real-time single molecule imaging demonstrates that TFIID alone binds poorly to native p53 target promoters. p53 unlocks TFIID’s ability to bind DNA by increasing TFIID contacts with both the core promoter and a region surrounding p53’s response element (RE). Analysis of single molecule dissociation kinetics reveals that TFIID interacts with promoters via transient and prolonged DNA binding modes that are each regulated by p53. Importantly, our structural work reveals that TFIID’s conversion from a canonical form to a rearranged DNA-binding conformation is enhanced in the presence of DNA and p53. Notably, TFIID’s interaction with DNA induces p53 to rapidly dissociate, effectively liberating the RE on the promoter. Collectively, these findings indicate that p53 dynamically escorts and loads the basal transcription machinery onto its target promoters.

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Posted February 24, 2017.
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p53 dynamically directs TFIID assembly on target gene promoters
R. A. Coleman, Z. Qiao, S. K. Singh, C. S. Peng, M. Cianfrocco, Z. Zhang, A. Piasecka, H. Aldeborgh, G. Basishvili, W. L. Liu
bioRxiv 083014; doi: https://doi.org/10.1101/083014
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p53 dynamically directs TFIID assembly on target gene promoters
R. A. Coleman, Z. Qiao, S. K. Singh, C. S. Peng, M. Cianfrocco, Z. Zhang, A. Piasecka, H. Aldeborgh, G. Basishvili, W. L. Liu
bioRxiv 083014; doi: https://doi.org/10.1101/083014

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