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TitleStructure of the p53/RNA polymerase II assembly.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 397, Year 2021
Publish dateMar 25, 2021
AuthorsShu-Hao Liou / Sameer K Singh / Robert H Singer / Robert A Coleman / Wei-Li Liu /
PubMed AbstractThe 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 ...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.
External linksCommun Biol / PubMed:33767390 / PubMed Central
MethodsEM (single particle)
Resolution4.6 Å
Structure data

22294

6xre

EMDB-22294, PDB-6xre:
Structure of the p53/RNA polymerase II assembly
Method: EM (single particle) / Resolution: 4.6 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • Homo sapien (human)
KeywordsTRANSCRIPTION / TRANSFERASE / Activator / tumor suppressor

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