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- W3136130153 abstract "Abstract The tumor suppressor p53 protein activates expression of a vast gene network in response to stress stimuli for cellular integrity. The molecular mechanism underlying how p53 targets RNA polymerase II (Pol II) to regulate transcription remains unclear. To elucidate the p53/Pol II interaction, we have determined a 4.6 Å resolution structure of the human p53/Pol II assembly via single particle cryo-electron microscopy. Our structure reveals that p53’s DNA binding domain targets the upstream DNA binding site within Pol II. This association introduces conformational changes of the Pol II clamp into a further-closed state. A cavity was identified between p53 and Pol II that could possibly host DNA. The transactivation domain of p53 binds the surface of Pol II’s jaw that contacts downstream DNA. These findings suggest that p53’s functional domains directly regulate DNA binding activity of Pol II to mediate transcription, thereby providing insights into p53-regulated gene expression." @default.
- W3136130153 created "2021-03-29" @default.
- W3136130153 creator A5007012292 @default.
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- W3136130153 creator A5077862062 @default.
- W3136130153 date "2021-03-25" @default.
- W3136130153 modified "2023-09-27" @default.
- W3136130153 title "Structure of the p53/RNA polymerase II assembly" @default.
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- W3136130153 doi "https://doi.org/10.1038/s42003-021-01934-4" @default.
- W3136130153 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7994806" @default.
- W3136130153 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33767390" @default.
- W3136130153 hasPublicationYear "2021" @default.
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